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Q29442

- CO4A4_BOVIN

UniProt

Q29442 - CO4A4_BOVIN

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Protein

Collagen alpha-4(IV) chain

Gene

COL4A4

Organism
Bos taurus (Bovine)
Status
Reviewed - 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

  1. extracellular matrix structural constituent Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-4(IV) chain
Gene namesi
Name:COL4A4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane PROSITE-ProRule annotation
Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).By similarity

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. collagen type IV trimer Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 453›453Collagen alpha-4(IV) chainPRO_0000059413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi243 ↔ 332Or C-243 with C-329PROSITE-ProRule annotation
Disulfide bondi276 ↔ 329Or C-276 with C-332PROSITE-ProRule annotation
Disulfide bondi288 ↔ 294PROSITE-ProRule annotation
Disulfide bondi351 ↔ 449Or C-351 with C-446PROSITE-ProRule annotation
Disulfide bondi385 ↔ 446Or C-385 with C-449PROSITE-ProRule annotation
Disulfide bondi397 ↔ 404PROSITE-ProRule annotation

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

PRIDEiQ29442.

Expressioni

Tissue specificityi

Alpha 3 and alpha 4 type IV collagens are colocalized and present only in basement membranes of kidney, eye, cochlea, lung and brain.

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. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite protomer, respectively. Associates with LAMB2 at the neuromuscular junction and in GBM (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018302.

Structurei

3D structure databases

ProteinModelPortaliQ29442.
SMRiQ29442. Positions 228-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini228 – 453226Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni‹1 – 222›222Triple-helical regionAdd
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

eggNOGiNOG12793.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ29442.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 3 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q29442-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GPPGPPGAPG KALKGDIPDP GLPGDQGPPG PDGPRGVPGP PGPPGSVDLL
60 70 80 90 100
KGEPGDCGLP GPPGLPGPPG PPGHKGFPGC DGKHGQKGPM GFPGPQGPPG
110 120 130 140 150
SPGPPGDKGL PGPPGRRGPL GPPGSRGEPG PPADLDACPR IPGLPGVPGP
160 170 180 190 200
RGPEGTMGLP GMRGPPGPGC KGEPGLDGRR GEDGLPGSPG PPGHKGDMGE
210 220 230 240 250
AGCPGAPGPP GPMGDPGPIG FGPGYLSGFL LVLHSQTDGE PTCPMGMPRL
260 270 280 290 300
WTGYSLLYLE GQERAHNQDL GLAGSCLPIF STLPFAYCNI HQVCHYARRN
310 320 330 340 350
DRSYWLASTA PLPMTPLSED EIRPYISRCA VCEAPAQAVA VHSQDQSIPP
360 370 380 390 400
CPRAWRSLWI GYSFLMHTGA GDQGGGQALM SPGSCLEDFR AAPFLECQGR
410 420 430 440 450
QGTCHFFANK YSFWLTTVRP DLQFSSAPLP DTLKESHAQR QKISRCQVCV

KHS
Length:453
Mass (Da):46,385
Last modified:November 1, 1997 - v1
Checksum:iF7ED410AE9A65BC1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti219 – 2191I → P AA sequence (PubMed:1468209)Curated
Sequence conflicti219 – 2191I → P AA sequence (PubMed:2318822)Curated
Sequence conflicti219 – 2191I → P AA sequence (PubMed:2438283)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77480 mRNA. Translation: AAA30458.2. Sequence problems.
PIRiS18804.
UniGeneiBt.91476.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77480 mRNA. Translation: AAA30458.2 . Sequence problems.
PIRi S18804.
UniGenei Bt.91476.

3D structure databases

ProteinModelPortali Q29442.
SMRi Q29442. Positions 228-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000018302.

Proteomic databases

PRIDEi Q29442.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085652.
HOVERGENi HBG004933.
InParanoidi Q29442.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 3 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The alpha 4(IV) chain of basement membrane collagen. Isolation of cDNAs encoding bovine alpha 4(IV) and comparison with other type IV collagens."
    Mariyama M., Kalluri R., Hudson B.G., Reeders S.T.
    J. Biol. Chem. 267:1253-1258(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 317-328.
    Tissue: Lens.
  2. "Partial protein sequence of the globular domain of alpha 4(IV) collagen chain: sites of sequence variability and homology with alpha 2(IV)."
    Matsukura H., Michael A.F., Fish A.J., Butkowski R.J.
    Connect. Tissue Res. 28:231-244(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 217-255; 257-278; 303-314; 391-399 AND 411-434.
  3. "Glomerular basement membrane. Identification of a fourth chain, alpha 4, of type IV collagen."
    Gunwar S., Saus J., Noelken M.E., Hudson B.G.
    J. Biol. Chem. 265:5466-5469(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 217-246.
  4. "Glomerular basement membrane. Identification of dimeric subunits of the noncollagenous domain (hexamer) of collagen IV and the Goodpasture antigen."
    Gunwar S., Ballester F., Kalluri R., Timoneda J., Chonko A.M., Edwards S.J., Noelken M.E., Hudson B.G.
    J. Biol. Chem. 266:15318-15324(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 217-237.
  5. "Localization of the Goodpasture epitope to a novel chain of basement membrane collagen."
    Butkowski R.J., Langeveld J.P.M., Wieslander J., Hamilton J., Hudson B.G.
    J. Biol. Chem. 262:7874-7877(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 217-233.

Entry informationi

Entry nameiCO4A4_BOVIN
AccessioniPrimary (citable) accession number: Q29442
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 1, 2014
This is version 110 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3