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8  structures 999  species 1  interaction 4881  sequences 137  architectures

Family: Fasciclin (PF02469)

Summary: Fasciclin domain

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Fasciclin domain Edit Wikipedia article

Fasciclin
PDB 1nyo EBI.jpg
solution structure of the antigenic tb protein mpt70/mpb70
Identifiers
Symbol Fasciclin
Pfam PF02469
InterPro IPR000782
SCOP 1o70
SUPERFAMILY 1o70

In molecular biology, the fasciclin domain (FAS1 domain) is an extracellular domain of about 140 amino acid residues. It has been suggested that the FAS1 domain represents an ancient cell adhesion domain common to plants and animals;[1] related FAS1 domains are also found in bacteria.[2]

The crystal structure of FAS1 domains 3 and 4 of fasciclin I from Drosophila melanogaster (Fruit fly) has been determined, revealing a novel domain fold consisting of a seven-stranded beta wedge and at least five alpha helices; two well-ordered N-acetylglucosamine groups attached to a conserved asparagine are located in the interface region between the two FAS1 domains.[3] Fasciclin I is an insect neural cell adhesion molecule involved in axonal guidance that is attached to the membrane by a GPI-anchored protein.

FAS1 domains are present in many secreted and membrane-anchored proteins. These proteins are usually GPI anchored and consist of: (i) a single FAS1 domain, (ii) a tandem array of FAS1 domains, or (iii) FAS1 domain(s) interspersed with other domains.

Proteins known to contain a FAS1 domain include:

  • Fasciclin I (4 FAS1 domains).
  • Volvox major cell adhesion protein (2 FAS1 domains).[1]

The FAS1 domains of both human periostin and BIgH3 proteins were found to contain vitamin K-dependent gamma-carboxyglutamate residues.[8] Gamma-carboxyglutamate residues are more commonly associated with GLA domains, where they occur through post-translational modification catalysed by the vitamin K-dependent enzyme gamma-glutamylcarboxylase.

See also[edit]

References[edit]

  1. ^ a b Huber O, Sumper M (September 1994). "Algal-CAMs: isoforms of a cell adhesion molecule in embryos of the alga Volvox with homology to Drosophila fasciclin I". EMBO J. 13 (18): 4212–22. PMC 395348. PMID 7925267. 
  2. ^ Ulstrup JC, Jeansson S, Wiker HG, Harboe M (February 1995). "Relationship of secretion pattern and MPB70 homology with osteoblast-specific factor 2 to osteitis following Mycobacterium bovis BCG vaccination". Infect. Immun. 63 (2): 672–5. PMC 173047. PMID 7822037. 
  3. ^ Clout NJ, Tisi D, Hohenester E (February 2003). "Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I". Structure 11 (2): 197–203. doi:10.1016/S0969-2126(03)00002-9. PMID 12575939. 
  4. ^ Kim JE, Kim SJ, Lee BH, Park RW, Kim KS, Kim IS (October 2000). "Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-beta-induced gene, betaig-h3". J. Biol. Chem. 275 (40): 30907–15. doi:10.1074/jbc.M002752200. PMID 10906123. 
  5. ^ Faik A, Abouzouhair J, Sarhan F (November 2006). "Putative fasciclin-like arabinogalactan-proteins (FLA) in wheat (Triticum aestivum) and rice (Oryza sativa): identification and bioinformatic analyses". Mol. Genet. Genomics 276 (5): 478–94. doi:10.1007/s00438-006-0159-z. PMID 16944204. 
  6. ^ Kzhyshkowska J, Gratchev A, Martens JH, Pervushina O, Mamidi S, Johansson S, Schledzewski K, Hansen B, He X, Tang J, Nakayama K, Goerdt S (December 2004). "Stabilin-1 localizes to endosomes and the trans-Golgi network in human macrophages and interacts with GGA adaptors". J. Leukoc. Biol. 76 (6): 1151–61. doi:10.1189/jlb.0504300. PMID 15345724. 
  7. ^ Matsumoto S, Matsuo T, Ohara N, Hotokezaka H, Naito M, Minami J, Yamada T (March 1995). "Cloning and sequencing of a unique antigen MPT70 from Mycobacterium tuberculosis H37Rv and expression in BCG using E. coli-mycobacteria shuttle vector". Scand. J. Immunol. 41 (3): 281–7. doi:10.1111/j.1365-3083.1995.tb03565.x. PMID 7871388. 
  8. ^ Coutu DL, Wu JH, Monette A, Rivard GE, Blostein MD, Galipeau J (June 2008). "Periostin, a member of a novel family of vitamin K-dependent proteins, is expressed by mesenchymal stromal cells". J. Biol. Chem. 283 (26): 17991–8001. doi:10.1074/jbc.M708029200. PMID 18450759. 

This article incorporates text from the public domain Pfam and InterPro IPR000782

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

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Fasciclin domain Provide feedback

This extracellular domain is found repeated four times in grasshopper fasciclin I as well as in proteins from mammals, sea urchins, plants, yeast and bacteria [1].

Literature references

  1. Kawamoto T, Noshiro M, Shen M, Nakamasu K, Hashimoto K, Kawashima-Ohya Y, Gotoh O, Kato Y; , Biochim Biophys Acta 1998;1395:288-292.: Structural and phylogenetic analyses of RGD-CAP/beta ig-h3, a fasciclin-like adhesion protein expressed in chick chondrocytes. PUBMED:9512662 EPMC:9512662


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000782

The FAS1 (fasciclin-like) domain is an extracellular module of about 140 amino acid residues. It has been suggested that the FAS1 domain represents an ancient cell adhesion domain common to plants and animals [PUBMED:7925267]; related FAS1 domains are also found in bacteria [PUBMED:7822037].

The crystal structure of FAS1 domains 3 and 4 of fasciclin I from Drosophila melanogaster (Fruit fly) has been determined, revealing a novel domain fold consisting of a seven-stranded beta wedge and at least five alpha helices; two well-ordered N-acetylglucosamine groups attached to a conserved asparagine are located in the interface region between the two FAS1 domains [PUBMED:12575939]. Fasciclin I is an insect neural cell adhesion molecule involved in axonal guidance that is attached to the membrane by a GPI-anchored protein.

FAS1 domains are present in many secreted and membrane-anchored proteins. These proteins are usually GPI anchored and consist of: (i) a single FAS1 domain, (ii) a tandem array of FAS1 domains, or (iii) FAS1 domain(s) interspersed with other domains.

Proteins known to contain a FAS1 domain include:

  • Fasciclin I (4 FAS1 domains).
  • Human TGF-beta induced Ig-H3 (BIgH3) protein (4 FAS1 domains), where the FAS1 domains mediate cell adhesion through an interaction with alpha3/beta1 integrin; mutation in the FAS1 domains result in corneal dystrophy [PUBMED:10906123].
  • Volvox major cell adhesion protein (2 FAS1 domains) [PUBMED:7925267].
  • Arabidopsis fasciclin-like arabinogalactan proteins (2 FAS1 domains) [PUBMED:16944204].
  • Mammalian stabilin protein, a family of fasciclin-like hyaluronan receptor homologues (7 FAS1 domains)[PUBMED:15345724].
  • Human extracellular matrix protein periostin (4 FAS1 domains).
  • Bacterial immunogenic protein MPT70 (1 FAS1 domain) [PUBMED:7871388].

The FAS1 domains of both human periostin (SWISSPROT) and BIgH3 (SWISSPROT) proteins were found to contain vitamin K-dependent gamma-carboxyglutamate residues [PUBMED:18450759]. Gamma-carboxyglutamate residues are more commonly associated with GLA domains (INTERPRO), where they occur through post-translational modification catalysed by the vitamin K-dependent enzyme gamma-glutamylcarboxylase.

Domain organisation

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Alignments

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(122)
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(1077)
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  Seed
(122)
Full
(4881)
Representative proteomes NCBI
(4995)
Meta
(1077)
RP15
(870)
RP35
(1506)
RP55
(2063)
RP75
(2602)
Alignment:
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  Seed
(122)
Full
(4881)
Representative proteomes NCBI
(4995)
Meta
(1077)
RP15
(870)
RP35
(1506)
RP55
(2063)
RP75
(2602)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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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.

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_562 (release 5.4)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 122
Number in full: 4881
Average length of the domain: 128.40 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 47.97 %

HMM information View help on HMM parameters

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 21.1 21.1
Trusted cut-off 21.1 21.1
Noise cut-off 21.0 21.0
Model length: 128
Family (HMM) version: 17
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Species distribution

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Interactions

There is 1 interaction for this family. More...

Fasciclin

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 Fasciclin domain has been found. There are 8 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.

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