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Q29442 (CO4A4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-4(IV) chain
Gene names
Name:COL4A4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length453 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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

Tissue specificity

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

Domain

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.

Post-translational modification

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.

Sequence similarities

Belongs to the type IV collagen family.

Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 453›453Collagen alpha-4(IV) chain
PRO_0000059413

Regions

Domain228 – 453226Collagen IV NC1
Region‹1 – 222›222Triple-helical region

Amino acid modifications

Disulfide bond243 ↔ 332Or C-243 with C-329 By similarity
Disulfide bond276 ↔ 329Or C-276 with C-332 By similarity
Disulfide bond288 ↔ 294 By similarity
Disulfide bond351 ↔ 449Or C-351 with C-446 By similarity
Disulfide bond385 ↔ 446Or C-385 with C-449 By similarity
Disulfide bond397 ↔ 404 By similarity

Experimental info

Sequence conflict2191I → P AA sequence Ref.2
Sequence conflict2191I → P AA sequence Ref.3
Sequence conflict2191I → P AA sequence Ref.5
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q29442 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F7ED410AE9A65BC1

FASTA45346,385
        10         20         30         40         50         60 
GPPGPPGAPG KALKGDIPDP GLPGDQGPPG PDGPRGVPGP PGPPGSVDLL KGEPGDCGLP 

        70         80         90        100        110        120 
GPPGLPGPPG PPGHKGFPGC DGKHGQKGPM GFPGPQGPPG SPGPPGDKGL PGPPGRRGPL 

       130        140        150        160        170        180 
GPPGSRGEPG PPADLDACPR IPGLPGVPGP RGPEGTMGLP GMRGPPGPGC KGEPGLDGRR 

       190        200        210        220        230        240 
GEDGLPGSPG PPGHKGDMGE AGCPGAPGPP GPMGDPGPIG FGPGYLSGFL LVLHSQTDGE 

       250        260        270        280        290        300 
PTCPMGMPRL WTGYSLLYLE GQERAHNQDL GLAGSCLPIF STLPFAYCNI HQVCHYARRN 

       310        320        330        340        350        360 
DRSYWLASTA PLPMTPLSED EIRPYISRCA VCEAPAQAVA VHSQDQSIPP CPRAWRSLWI 

       370        380        390        400        410        420 
GYSFLMHTGA GDQGGGQALM SPGSCLEDFR AAPFLECQGR QGTCHFFANK YSFWLTTVRP 

       430        440        450 
DLQFSSAPLP DTLKESHAQR QKISRCQVCV KHS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77480 mRNA. Translation: AAA30458.2. Sequence problems.
PIRS18804.
UniGeneBt.91476.

3D structure databases

ProteinModelPortalQ29442.
SMRQ29442. Positions 228-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000018302.

Proteomic databases

PRIDEQ29442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085652.
HOVERGENHBG004933.
InParanoidQ29442.

Family and domain databases

Gene3D2.170.240.10. 1 hit.
InterProIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamPF01413. C4. 2 hits.
PF01391. Collagen. 3 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCO4A4_BOVIN
AccessionPrimary (citable) accession number: Q29442
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families