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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 229›229Collagen alpha-1(IV) chainPRO_0000059399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 111PROSITE-ProRule annotation1 Publication
Disulfide bondi53 ↔ 108PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 71PROSITE-ProRule annotation1 Publication
Cross-linki93 – 93S-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-linki211 – 211S-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.
PRIDEiQ7SIB2.

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

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi13 – 164Combined sources
Beta strandi25 – 3814Combined sources
Beta strandi41 – 444Combined sources
Helixi50 – 523Combined sources
Beta strandi53 – 564Combined sources
Beta strandi62 – 654Combined sources
Beta strandi71 – 744Combined sources
Beta strandi79 – 846Combined sources
Helixi98 – 1047Combined sources
Beta strandi107 – 1159Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi135 – 14713Combined sources
Helixi149 – 1513Combined sources
Beta strandi153 – 1553Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi173 – 1775Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi189 – 1946Combined sources
Helixi198 – 2003Combined sources
Beta strandi208 – 2103Combined sources
Helixi216 – 2183Combined sources
Beta strandi221 – 2266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIB2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 229225Collagen 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.
InParanoidiQ7SIB2.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

UniGeneiBt.32410.

Cross-referencesi

Sequence databases

UniGeneiBt.32410.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000035211.

Proteomic databases

PaxDbiQ7SIB2.
PRIDEiQ7SIB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiQ7SIB2.

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 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: February 17, 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.