Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagen alpha-2(IV) chain

Gene

COL4A2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(IV) chain
Gene namesi
Name:COL4A2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 227›227Collagen alpha-2(IV) chainPRO_0000059411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi19 ↔ 108PROSITE-ProRule annotation1 Publication
Disulfide bondi52 ↔ 105PROSITE-ProRule annotation1 Publication
Disulfide bondi64 ↔ 70PROSITE-ProRule annotation1 Publication
Disulfide bondi127 ↔ 223PROSITE-ProRule annotation1 Publication
Disulfide bondi161 ↔ 220PROSITE-ProRule annotation1 Publication
Disulfide bondi173 ↔ 180PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiQ7SIB3.
PRIDEiQ7SIB3.

Interactioni

Subunit structurei

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005916.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Beta strandi12 – 154Combined sources
Beta strandi25 – 3713Combined sources
Beta strandi40 – 434Combined sources
Helixi49 – 513Combined sources
Beta strandi52 – 554Combined sources
Beta strandi61 – 655Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 735Combined sources
Beta strandi78 – 836Combined sources
Helixi95 – 1017Combined sources
Beta strandi104 – 1096Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi131 – 14414Combined sources
Beta strandi150 – 1523Combined sources
Helixi158 – 1603Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi170 – 1734Combined sources
Helixi175 – 1773Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi195 – 1995Combined sources
Beta strandi206 – 2094Combined sources
Helixi214 – 2163Combined sources
Beta strandi219 – 2257Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3DX-ray2.00C/F/I/L1-227[»]
1T60X-ray1.50C/F/I/L/O/R/U/X1-227[»]
1T61X-ray1.50C/F1-227[»]
ProteinModelPortaliQ7SIB3.
SMRiQ7SIB3. Positions 2-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 227224Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Domaini

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ7SIB3.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q7SIB3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ISIGYLLVKH SQTDQEPMCP VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG
60 70 80 90 100
SCLARFSTMP FLYCNPGDVC YYASRNDKSY WLSTTAPLPM MPVAEEDIRP
110 120 130 140 150
YISRCSVCEA PAVAIAVHSQ DVSIPHCPAG WRSLWIGYSF LMHTAAGDEG
160 170 180 190 200
GGQSLVSPGS CLEDFRATPF IECNGARGTC HYYANKYSFW LTTIPEQSFQ
210 220
GTPSADTLKA GLIRTHISRC QVCMKNL
Length:227
Mass (Da):25,061
Last modified:December 15, 2003 - v1
Checksum:iBC81FF77053BEBD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3DX-ray2.00C/F/I/L1-227[»]
1T60X-ray1.50C/F/I/L/O/R/U/X1-227[»]
1T61X-ray1.50C/F1-227[»]
ProteinModelPortaliQ7SIB3.
SMRiQ7SIB3. Positions 2-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005916.

Proteomic databases

PaxDbiQ7SIB3.
PRIDEiQ7SIB3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ7SIB3.

Miscellaneous databases

EvolutionaryTraceiQ7SIB3.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement membranes."
    Sundaramoorthy M., Meiyappan M., Todd P., Hudson B.G.
    J. Biol. Chem. 277:31142-31153(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiCO4A2_BOVIN
AccessioniPrimary (citable) accession number: Q7SIB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 15, 2003
Last modified: November 11, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.