Summary: Apolipoprotein C-II

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Wikipedia: Apolipoprotein C2
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This is the Wikipedia entry entitled "Apolipoprotein C2". More...

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Apolipoprotein C2 Edit Wikipedia article

Apolipoprotein C-II

PDB rendering based on 1by6.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
1BY6, 1I5J, 1O8T, 1SOH

Identifiers

Symbols

APOC2; APO-CII; APOC-II

External IDs

OMIM: 608083 MGI: 88054 HomoloGene: 47928 GeneCards: APOC2 Gene

Gene Ontology
Molecular function	• lipid binding • phospholipase activator activity • protein homodimerization activity • phospholipase binding • lipase inhibitor activity • lipoprotein lipase activator activity
Cellular component	• extracellular region • extracellular space • very-low-density lipoprotein particle • low-density lipoprotein particle • intermediate-density lipoprotein particle • spherical high-density lipoprotein particle • chylomicron
Biological process	• lipid metabolic process • positive regulation of phospholipase activity • positive regulation of triglyceride catabolic process • positive regulation of very-low-density lipoprotein particle remodeling • negative regulation of very-low-density lipoprotein particle clearance • lipid catabolic process • negative regulation of cholesterol transport • cholesterol efflux • phospholipid efflux • triglyceride-rich lipoprotein particle remodeling • chylomicron remodeling • very-low-density lipoprotein particle remodeling • chylomicron remnant clearance • high-density lipoprotein particle clearance • lipoprotein metabolic process • cholesterol homeostasis • reverse cholesterol transport • small molecule metabolic process • positive regulation of fatty acid biosynthetic process • negative regulation of lipid metabolic process • negative regulation of receptor-mediated endocytosis • positive regulation of lipoprotein lipase activity • positive regulation of phospholipid catabolic process • triglyceride homeostasis
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
45.45 – 45.45 Mb

Chr 7:
19.67 – 19.68 Mb

PubMed search

[1]

[2]

Apo-CII

nmr structure of human apolipoprotein c-ii in the presence of sds

Identifiers

Symbol

Apo-CII

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Apolipoprotein C2 or Apolipoprotein C-II is a protein that in humans is encoded by the APOC2 gene.

The protein encoded by this gene is secreted in plasma where it is a component of very low density lipoproteins and chylomicrons. This protein activates the enzyme lipoprotein lipase in capillaries,^[1] which hydrolyzes triglycerides and thus provides free fatty acids for cells. Mutations in this gene cause hyperlipoproteinemia type IB, characterized by xanthomas, pancreatitis, and hepatosplenomegaly, but no increased risk for atherosclerosis. Lab tests will show elevated blood levels of triglycerides, cholesterol, and chylomicrons^[2]

[edit] Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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Statin Pathway edit

^ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430". http://www.wikipathways.org/index.php/Pathway:WP430.

[edit] See also

Apolipoprotein C

[edit] References

^ Kim SY, Park SM, Lee ST (2006). "Apolipoprotein C-II is a novel substrate for matrix metalloproteinases". Biochem. Biophys. Res. Commun. 339 (1): 47–54. doi:10.1016/j.bbrc.2005.10.182. PMID 16314153.
^ "Entrez Gene: APOC2 apolipoprotein C-II". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=344.

Jackson RL, Baker HN, Gilliam EB, Gotto AM (1977). "Primary structure of very low density apolipoprotein C-II of human plasma.". Proc. Natl. Acad. Sci. U.S.A. 74 (5): 1942–5. doi:10.1073/pnas.74.5.1942. PMC 431048. PMID 194244. //www.ncbi.nlm.nih.gov/pmc/articles/PMC431048/.
Lycksell PO, Ohman A, Bengtsson-Olivecrona G, et al. (1992). "Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII.". Eur. J. Biochem. 205 (1): 223–31. doi:10.1111/j.1432-1033.1992.tb16772.x. PMID 1555583.
Hegele RA, Connelly PW, Maguire GF, et al. (1992). "An apolipoprotein CII mutation, CIILys19----Thr' identified in patients with hyperlipidemia.". Dis. Markers 9 (2): 73–80. PMID 1782747.
Crecchio C, Capurso A, Pepe G (1990). "Identification of the mutation responsible for a case of plasmatic apolipoprotein CII deficiency (Apo CII-Bari).". Biochem. Biophys. Res. Commun. 168 (3): 1118–27. doi:10.1016/0006-291X(90)91145-I. PMID 1971748.
Bengtsson-Olivecrona G, Sletten K (1990). "Primary structure of the bovine analogues to human apolipoproteins CII and CIII. Studies on isoforms and evidence for proteolytic processing.". Eur. J. Biochem. 192 (2): 515–21. doi:10.1111/j.1432-1033.1990.tb19255.x. PMID 2209608.
Wei CF, Tsao YK, Robberson DL, et al. (1986). "The structure of the human apolipoprotein C-II gene. Electron microscopic analysis of RNA:DNA hybrids, complete nucleotide sequence, and identification of 5' homologous sequences among apolipoprotein genes.". J. Biol. Chem. 260 (28): 15211–21. PMID 2415514.
Fojo SS, Lohse P, Parrott C, et al. (1989). "A nonsense mutation in the apolipoprotein C-IIPadova gene in a patient with apolipoprotein C-II deficiency.". J. Clin. Invest. 84 (4): 1215–9. doi:10.1172/JCI114287. PMC 329780. PMID 2477392. //www.ncbi.nlm.nih.gov/pmc/articles/PMC329780/.
Jackson CL, Bruns GA, Breslow JL (1986). "Isolation of cDNA and genomic clones for apolipoprotein C-II". Meth. Enzymol.. Methods in Enzymology 128: 788–800. doi:10.1016/0076-6879(86)28106-9. ISBN 9780121820282. PMID 3014272.
Fojo SS, Law SW, Brewer HB (1987). "The human preproapolipoprotein C-II gene. Complete nucleic acid sequence and genomic organization". FEBS Lett. 213 (1): 221–6. doi:10.1016/0014-5793(87)81495-3. PMID 3030808.
Fojo SS, Stalenhoef AF, Marr K, et al. (1989). "A deletion mutation in the ApoC-II gene (ApoC-II Nijmegen) of a patient with a deficiency of apolipoprotein C-II". J. Biol. Chem. 263 (34): 17913–6. PMID 3192518.
Fojo SS, Beisiegel U, Beil U, et al. (1988). "Donor splice site mutation in the apolipoprotein (Apo) C-II gene (Apo C-IIHamburg) of a patient with Apo C-II deficiency". J. Clin. Invest. 82 (5): 1489–94. doi:10.1172/JCI113756. PMC 442713. PMID 3263393. //www.ncbi.nlm.nih.gov/pmc/articles/PMC442713/.
Connelly PW, Maguire GF, Hofmann T, Little JA (1987). "Structure of apolipoprotein C-IIToronto, a nonfunctional human apolipoprotein". Proc. Natl. Acad. Sci. U.S.A. 84 (1): 270–3. doi:10.1073/pnas.84.1.270. PMC 304185. PMID 3467353. //www.ncbi.nlm.nih.gov/pmc/articles/PMC304185/.
Fairwell T, Hospattankar AV, Brewer HB, Khan SA (1987). "Human plasma apolipoprotein C-II: total solid-phase synthesis and chemical and biological characterization". Proc. Natl. Acad. Sci. U.S.A. 84 (14): 4796–800. doi:10.1073/pnas.84.14.4796. PMC 305192. PMID 3474626. //www.ncbi.nlm.nih.gov/pmc/articles/PMC305192/.
Fojo SS, Taam L, Fairwell T, et al. (1986). "Human preproapolipoprotein C-II. Analysis of major plasma isoforms". J. Biol. Chem. 261 (21): 9591–4. PMID 3525527.
Das HK, Jackson CL, Miller DA, et al. (1987). "The human apolipoprotein C-II gene sequence contains a novel chromosome 19-specific minisatellite in its third intron". J. Biol. Chem. 262 (10): 4787–93. PMID 3558370.
Connelly PW, Maguire GF, Little JA (1988). "Apolipoprotein CIISt. Michael. Familial apolipoprotein CII deficiency associated with premature vascular disease". J. Clin. Invest. 80 (6): 1597–606. doi:10.1172/JCI113246. PMC 442428. PMID 3680515. //www.ncbi.nlm.nih.gov/pmc/articles/PMC442428/.
Baggio G, Manzato E, Gabelli C, et al. (1986). "Apolipoprotein C-II deficiency syndrome. Clinical features, lipoprotein characterization, lipase activity, and correction of hypertriglyceridemia after apolipoprotein C-II administration in two affected patients". J. Clin. Invest. 77 (2): 520–7. doi:10.1172/JCI112332. PMC 423374. PMID 3944267. //www.ncbi.nlm.nih.gov/pmc/articles/PMC423374/.
Menzel HJ, Kane JP, Malloy MJ, Havel RJ (1986). "A variant primary structure of apolipoprotein C-II in individuals of African descent". J. Clin. Invest. 77 (2): 595–601. doi:10.1172/JCI112342. PMC 423392. PMID 3944271. //www.ncbi.nlm.nih.gov/pmc/articles/PMC423392/.
Sharpe CR, Sidoli A, Shelley CS, et al. (1984). "Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance". Nucleic Acids Res. 12 (9): 3917–32. doi:10.1093/nar/12.9.3917. PMC 318799. PMID 6328445. //www.ncbi.nlm.nih.gov/pmc/articles/PMC318799/.
Jackson CL, Bruns GA, Breslow JL (1984). "Isolation and sequence of a human apolipoprotein CII cDNA clone and its use to isolate and map to human chromosome 19 the gene for apolipoprotein CII". Proc. Natl. Acad. Sci. U.S.A. 81 (10): 2945–9. doi:10.1073/pnas.81.10.2945. PMC 345197. PMID 6328478. //www.ncbi.nlm.nih.gov/pmc/articles/PMC345197/.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Apolipoprotein C-II Provide feedback

Apolipoprotein C-II (ApoC-II) is the major activator of lipoprotein lipase, a key enzyme in the regulation of triglyceride levels in human serum [1].

Literature references

Storjohann R, Rozek A, Sparrow JT, Cushley RJ; , Biochim Biophys Acta 2000;1486:253-264.: Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine. PUBMED:10903476 EPMC:10903476

External database links

PANDIT:	PF05355
Pseudofam:	PF05355
SCOP:	1by6
SYSTERS:	Apo-CII

This tab holds annotation information from the InterPro database.

InterPro entry IPR008019

Apolipoprotein CII (apoC-II) is a surface constituent of plasma lipoproteins and the activator for lipoprotein lipase (LPL). It is therefore central for lipid transport in blood. Lipoprotein lipase is a key enzyme in the regulation of triglyceride levels in human serum [PUBMED:10903476]. It is the C-terminal helix of apoC-II that is responsible for the activation of LPL [PUBMED:12590574]. The active peptide of apoC-II occurs at residues 44-79 and has been shown to reverse the symptoms of genetic apoC-II deficiency in a human subject [PUBMED:10903476].

Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix. The first 12 residues of apoC-II are structurally heterogeneous but the rest of the protein forms a predominantly helical structure [PUBMED:11331005].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Cellular component	chylomicron (GO:0042627)
Molecular function	enzyme activator activity (GO:0008047)
Biological process	lipid transport (GO:0006869)
Biological process	lipid metabolic process (GO:0006629)

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

Viewing

You can see the alignments as HTML or in three different sequence viewers:

jalview: a Java applet developed at the University of Dundee. You will need Java installed before running jalview
HTML: an HTML page showing the whole alignment.Please note: full Pfam alignments can be very large. These HTML views are extremely large and often cause problems for browsers. Please use either jalview or the Pfam viewer if you have trouble viewing the HTML version
PP/Heatmap: an HTML-based representation of the alignment, coloured according to the posterior-probability (PP) values from the HMM. As for the standard HTML view, heatmap alignments can also be very large and slow to render.
Pfam viewer: an HTML-based viewer that uses DAS to retrieve alignment fragments on request

Reformatting

You can download (or view in your browser) a text representation of a Pfam alignment in various formats:

Selex
Stockholm
FASTA
MSF

You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.

Downloading

You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

	Seed (6)	Full (40)	Representative proteomes				NCBI (42)	Meta (0)
	Seed (6)	Full (40)	RP15 (1)	RP35 (2)	RP55 (6)	RP75 (19)	NCBI (42)	Meta (0)
Jalview	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (6)	Full (40)	Representative proteomes				NCBI (42)	Meta (0)
	Seed (6)	Full (40)	RP15 (1)	RP35 (2)	RP55 (6)	RP75 (19)	NCBI (42)	Meta (0)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

	Seed (6)	Full (40)	Representative proteomes				NCBI (42)	Meta (0)
	Seed (6)	Full (40)	RP15 (1)	RP35 (2)	RP55 (6)	RP75 (19)	NCBI (42)	Meta (0)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation

Seed source:

Pfam-B_6456 (release 7.8)

Previous IDs:

none

Type:

Family

Author:

Finn RD

Number in seed:

6

Number in full:

40

Average length of the domain:

73.00 aa

Average identity of full alignment:

46 %

Average coverage of the sequence by the domain:

75.96 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	22.1	22.1
Trusted cut-off	22.1	24.5
Noise cut-off	18.8	21.9

Model length:

78

Family (HMM) version:

6

Download:

download the raw HMM for this family

Species distribution

Sunburst
Tree

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.

How the sunburst is generated

The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.

In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:

superkingdom
kingdom
phylum
class
order
family
genus
species

Colouring and labels

Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.

As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.

Anomalies in the taxonomy tree

There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.

Missing taxonomic levels

Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.

Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".

Sub-species

Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

Too many species/sequences

For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.

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Tree controls

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The tree shows the occurrence of this domain across different species. More...

Species trees

We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.

Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.

If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.

Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.

Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.

We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.

You can use the tree controls to manipulate how the interactive tree is displayed:

show/hide the summary boxes
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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Apo-CII domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

Loading structure mapping...

Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: Apo-CII (PF05355)

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