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Protein

Collagen alpha-1(IV) chain

Gene

COL4A1

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.

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IV) chain
Gene namesi
Name:COL4A1
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_0000059399‹1 – 229Collagen alpha-1(IV) chainAdd BLAST›229

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 111PROSITE-ProRule annotation1 Publication
Disulfide bondi53 ↔ 108PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 71PROSITE-ProRule annotation1 Publication
Cross-linki93S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-211)By similarity
Disulfide bondi130 ↔ 225PROSITE-ProRule annotation1 Publication
Disulfide bondi164 ↔ 222PROSITE-ProRule annotation1 Publication
Disulfide bondi176 ↔ 182PROSITE-ProRule annotation1 Publication
Cross-linki211S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-93)By similarity

Post-translational modificationi

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
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

PaxDbiQ7SIB2.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012849.

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.ENSBTAP00000035211.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi13 – 16Combined sources4
Beta strandi25 – 38Combined sources14
Beta strandi41 – 44Combined sources4
Helixi50 – 52Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi62 – 65Combined sources4
Beta strandi71 – 74Combined sources4
Beta strandi79 – 84Combined sources6
Helixi98 – 104Combined sources7
Beta strandi107 – 115Combined sources9
Beta strandi117 – 121Combined sources5
Beta strandi123 – 126Combined sources4
Beta strandi135 – 147Combined sources13
Helixi149 – 151Combined sources3
Beta strandi153 – 155Combined sources3
Helixi161 – 163Combined sources3
Beta strandi164 – 167Combined sources4
Beta strandi173 – 177Combined sources5
Beta strandi180 – 183Combined sources4
Beta strandi189 – 194Combined sources6
Helixi198 – 200Combined sources3
Beta strandi208 – 210Combined sources3
Helixi216 – 218Combined sources3
Beta strandi221 – 226Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M3DX-ray2.00A/B/D/E/G/H/J/K1-229[»]
1T60X-ray1.50A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/W1-229[»]
1T61X-ray1.50A/B/D/E1-229[»]
ProteinModelPortaliQ7SIB2.
SMRiQ7SIB2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 229Collagen IV NC1PROSITE-ProRule annotationAdd BLAST225

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.
InParanoidiQ7SIB2.

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.

Q7SIB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SVDHGFLVTR HSQTTDDPQC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA
60 70 80 90 100
GSCLRKFSTM PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN
110 120 130 140 150
IRPFISRCAV CEAPAMVMAV HSQTIQIPQC PTGWSSLWIG YSFVMHTSAG
160 170 180 190 200
AEGSGQALAS PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE
210 220
MFKKPTPSTL KAGELRTHVS RCQVCMRRT
Length:229
Mass (Da):25,374
Last modified:December 15, 2003 - v1
Checksum:i8A5E278FDEA52E94
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

UniGeneiBt.32410.

Cross-referencesi

Sequence databases

UniGeneiBt.32410.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M3DX-ray2.00A/B/D/E/G/H/J/K1-229[»]
1T60X-ray1.50A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/W1-229[»]
1T61X-ray1.50A/B/D/E1-229[»]
ProteinModelPortaliQ7SIB2.
SMRiQ7SIB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000035211.

Proteomic databases

PaxDbiQ7SIB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ7SIB2.

Miscellaneous databases

EvolutionaryTraceiQ7SIB2.

Gene expression databases

BgeeiENSBTAG00000012849.

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 nameiCO4A1_BOVIN
AccessioniPrimary (citable) accession number: Q7SIB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 15, 2003
Last modified: November 30, 2016
This is version 84 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.