Q29442 (CO4A4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-4(IV) chain

Gene names

Name:

COL4A4

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	453 AA.
Sequence status	Fragment.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Collagen Repeat
PTM	Disulfide bond Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	collagen type IV Inferred from direct assay PubMed 1447198. Source: UniProtKB
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 453	›453	Collagen alpha-4(IV) chain		PRO_0000059413
Regions
	Domain	228 – 453	226	Collagen IV NC1
	Region	‹1 – 222	›222	Triple-helical region
Amino acid modifications
	Disulfide bond	243 ↔ 332		Or C-243 with C-329 By similarity
	Disulfide bond	276 ↔ 329		Or C-276 with C-332 By similarity
	Disulfide bond	288 ↔ 294		By similarity
	Disulfide bond	351 ↔ 449		Or C-351 with C-446 By similarity
	Disulfide bond	385 ↔ 446		Or C-385 with C-449 By similarity
	Disulfide bond	397 ↔ 404		By similarity
Experimental info
	Sequence conflict	219	1	I → P AA sequence Ref.2
	Sequence conflict	219	1	I → P AA sequence Ref.3
	Sequence conflict	219	1	I → P AA sequence Ref.5
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q29442 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: F7ED410AE9A65BC1	FASTA	453	46,385
	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

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.
IPI	IPI01017560.
PIR	S18804.
UniGene	Bt.91476.
3D structure databases
ProteinModelPortal	Q29442.
SMR	Q29442. Positions 228-452.
ModBase	Search...
Proteomic databases
PRIDE	Q29442.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000085652.
HOVERGEN	HBG004933.
InParanoid	Q29442.
OrthoDB	EOG4XGZZF.
Family and domain databases
Gene3D	2.170.240.10. 1 hit.
InterPro	IPR016187. C-type_lectin_fold. IPR008160. Collagen. IPR001442. Collagen_VI_NC. [Graphical view]
Pfam	PF01413. C4. 2 hits. PF01391. Collagen. 3 hits. [Graphical view]
SMART	SM00111. C4. 2 hits. [Graphical view]
SUPFAM	SSF56436. C-type_lectin_fold. 2 hits.
PROSITE	PS51403. NC1_IV. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CO4A4_BOVIN

Accession

Primary (citable) accession number: Q29442

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program