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)DescriptionActionsGraphical viewLength
ChainiPRO_0000059411‹1 – 227Collagen alpha-2(IV) chainAdd BLAST›227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi12 – 15Combined sources4
Beta strandi25 – 37Combined sources13
Beta strandi40 – 43Combined sources4
Helixi49 – 51Combined sources3
Beta strandi52 – 55Combined sources4
Beta strandi61 – 65Combined sources5
Turni66 – 68Combined sources3
Beta strandi69 – 73Combined sources5
Beta strandi78 – 83Combined sources6
Helixi95 – 101Combined sources7
Beta strandi104 – 109Combined sources6
Beta strandi114 – 118Combined sources5
Beta strandi120 – 123Combined sources4
Beta strandi131 – 144Combined sources14
Beta strandi150 – 152Combined sources3
Helixi158 – 160Combined sources3
Beta strandi161 – 164Combined sources4
Beta strandi170 – 173Combined sources4
Helixi175 – 177Combined sources3
Beta strandi179 – 181Combined sources3
Beta strandi187 – 192Combined sources6
Beta strandi195 – 199Combined sources5
Beta strandi206 – 209Combined sources4
Helixi214 – 216Combined sources3
Beta strandi219 – 225Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 227Collagen IV NC1PROSITE-ProRule annotationAdd BLAST224

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.
InterProiIPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
InterProiIPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[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...

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 30, 2016
This is version 80 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.