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Protein

Collagen alpha-4(IV) chain

Gene

COL4A4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • extracellular matrix structural constituent Source: UniProtKB

GO - Biological processi

  • collagen catabolic process Source: Reactome
  • extracellular matrix organization Source: Reactome
  • glomerular basement membrane development Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000081052-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-4(IV) chain
Gene namesi
Name:COL4A4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2206. COL4A4.

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

  • basal lamina Source: UniProtKB
  • collagen type IV trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Alport syndrome, autosomal recessive (APSAR)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness.
See also OMIM:203780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008148441 – 446Missing in APSAR. 6
Natural variantiVAR_0081531030G → V in APSAR. 1 Publication1
Natural variantiVAR_0019131201G → S in APSAR. 1 PublicationCorresponds to variant rs121912858dbSNPEnsembl.1
Natural variantiVAR_0081551572P → L in APSAR. 1 PublicationCorresponds to variant rs121912863dbSNPEnsembl.1
Hematuria, benign familial (BFH)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant condition characterized by non-progressive isolated microscopic hematuria that does not result in renal failure. It is characterized pathologically by thinning of the glomerular basement membrane.
See also OMIM:141200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031623116G → E in BFH. 1 Publication1
Natural variantiVAR_001912897G → E in BFH. 1 PublicationCorresponds to variant rs121912860dbSNPEnsembl.1
Natural variantiVAR_031624960G → R in BFH. 2 PublicationsCorresponds to variant rs769783985dbSNPEnsembl.1
Natural variantiVAR_031625999G → E in BFH. 1 PublicationCorresponds to variant rs13027659dbSNPEnsembl.1
Natural variantiVAR_0316261132P → L in BFH. 1 Publication1

Keywords - Diseasei

Alport syndrome, Deafness, Disease mutation

Organism-specific databases

DisGeNETi1286.
MalaCardsiCOL4A4.
MIMi141200. phenotype.
203780. phenotype.
OpenTargetsiENSG00000081052.
Orphaneti88918. Autosomal dominant Alport syndrome.
88919. Autosomal recessive Alport syndrome.
97562. Benign familial hematuria.
PharmGKBiPA26721.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL4A4.
DMDMi259016360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Sequence analysisAdd BLAST38
ChainiPRO_000000585039 – 1690Collagen alpha-4(IV) chainAdd BLAST1652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi142N-linked (GlcNAc...)Sequence analysis1
Glycosylationi669N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1480 ↔ 1569Or C-1480 with C-1566PROSITE-ProRule annotation
Disulfide bondi1513 ↔ 1566Or C-1513 with C-1569PROSITE-ProRule annotation
Disulfide bondi1525 ↔ 1531PROSITE-ProRule annotation
Disulfide bondi1588 ↔ 1686Or C-1588 with C-1683PROSITE-ProRule annotation
Disulfide bondi1622 ↔ 1683Or C-1622 with C-1686PROSITE-ProRule annotation
Disulfide bondi1634 ↔ 1641PROSITE-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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1206 – 1207Cleavage; by collagenaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP53420.
PaxDbiP53420.
PeptideAtlasiP53420.
PRIDEiP53420.

PTM databases

iPTMnetiP53420.
PhosphoSitePlusiP53420.

Expressioni

Tissue specificityi

Alpha 3 and alpha 4 type IV collagens are colocalized and present in kidney, eye, basement membranes of lens capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal kidney and fetal lung. PubMed:8083201 reports similar levels of expression of alpha 3 and alpha 4 type IV collagens in kidney, but PubMed:7523402 reports that in kidney levels of alpha 3 type IV collagen are significantly lower than those of alpha 4 type IV collagen. Highest levels of expression of alpha 4 type IV collagen are detected in kidney, calvaria, neuroretina and cardiac muscle. Lower levels of expression are observed in brain, lung and thymus, and no expression is detected in choroid plexus, liver, adrenal, pancreas, ileum or skin.2 Publications

Gene expression databases

BgeeiENSG00000081052.
CleanExiHS_COL4A4.
GenevisibleiP53420. HS.

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

IntActiP53420. 1 interactor.
STRINGi9606.ENSP00000379866.

Structurei

3D structure databases

ProteinModelPortaliP53420.
SMRiP53420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1465 – 1690Collagen IV NC1PROSITE-ProRule annotationAdd BLAST226

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 647S domainAdd BLAST26
Regioni65 – 1459Triple-helical regionAdd BLAST1395

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi94 – 96Cell attachment siteSequence analysis3
Motifi145 – 147Cell attachment siteSequence analysis3
Motifi189 – 191Cell attachment siteSequence analysis3
Motifi310 – 312Cell attachment siteSequence analysis3
Motifi724 – 726Cell attachment siteSequence analysis3
Motifi785 – 787Cell attachment siteSequence analysis3
Motifi989 – 991Cell attachment siteSequence analysis3
Motifi1212 – 1214Cell attachment siteSequence analysis3

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, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410YAVF. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiP53420.
KOiK06237.
OMAiPPGYKGF.
OrthoDBiEOG091G0613.
PhylomeDBiP53420.
TreeFamiTF344135.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 14 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSLHIVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYIGPCGGR
60 70 80 90 100
DCSVCHCVPE KGSRGPPGPP GPQGPIGPLG APGPIGLSGE KGMRGDRGPP
110 120 130 140 150
GAAGDKGDKG PTGVPGFPGL DGIPGHPGPP GPRGKPGMSG HNGSRGDPGF
160 170 180 190 200
PGGRGALGPG GPLGHPGEKG EKGNSVFILG AVKGIQGDRG DPGLPGLPGS
210 220 230 240 250
WGAGGPAGPT GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG QMGDPGEVGQ
260 270 280 290 300
QGSPGPTLLV EPPDFCLYKG EKGIKGIPGM VGLPGPPGRK GESGIGAKGE
310 320 330 340 350
KGIPGFPGPR GDPGSYGSPG FPGLKGELGL VGDPGLFGLI GPKGDPGNRG
360 370 380 390 400
HPGPPGVLVT PPLPLKGPPG DPGFPGRYGE TGDVGPPGPP GLLGRPGEAC
410 420 430 440 450
AGMIGPPGPQ GFPGLPGLPG EAGIPGRPDS APGKPGKPGS PGLPGAPGLQ
460 470 480 490 500
GLPGSSVIYC SVGNPGPQGI KGKVGPPGGR GPKGEKGNEG LCACEPGPMG
510 520 530 540 550
PPGPPGLPGR QGSKGDLGLP GWLGTKGDPG PPGAEGPPGL PGKHGASGPP
560 570 580 590 600
GNKGAKGDMV VSRVKGHKGE RGPDGPPGFP GQPGSHGRDG HAGEKGDPGP
610 620 630 640 650
PGDHEDATPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGHP
660 670 680 690 700
GVRGPDGLKG QKGDTISCNV TYPGRHGPPG FDGPPGPKGF PGPQGAPGLS
710 720 730 740 750
GSDGHKGRPG TPGTAEIPGP PGFRGDMGDP GFGGEKGSSP VGPPGPPGSP
760 770 780 790 800
GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG IKGPRGDPGC PGAEGPAGIP
810 820 830 840 850
GFLGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG LPGYPGSPGA
860 870 880 890 900
PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG
910 920 930 940 950
PPGPKGPRGL PGFPGFPGER GKPGAEGCPG AKGEPGEKGM SGLPGDRGLR
960 970 980 990 1000
GAKGAIGPPG DEGEMAIISQ KGTPGEPGPP GDDGFPGERG DKGTPGMQGR
1010 1020 1030 1040 1050
RGEPGRYGPP GFHRGEPGEK GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ
1060 1070 1080 1090 1100
GEPGSPGPPG FSGIDGARGP KGNKGDPASH FGPPGPKGEP GSPGCPGHFG
1110 1120 1130 1140 1150
ASGEQGLPGI QGPRGSPGRP GPPGSSGPPG CPGDHGMPGL RGQPGEMGDP
1160 1170 1180 1190 1200
GPRGLQGDPG IPGPPGIKGP SGSPGLNGLH GLKGQKGTKG ASGLHDVGPP
1210 1220 1230 1240 1250
GPVGIPGLKG ERGDPGSPGI SPPGPRGKKG PPGPPGSSGP PGPAGATGRA
1260 1270 1280 1290 1300
PKDIPDPGPP GDQGPPGPDG PRGAPGPPGL PGSVDLLRGE PGDCGLPGPP
1310 1320 1330 1340 1350
GPPGPPGPPG YKGFPGCDGK DGQKGPVGFP GPQGPHGFPG PPGEKGLPGP
1360 1370 1380 1390 1400
PGRKGPTGLP GPRGEPGPPA DVDDCPRIPG LPGAPGMRGP EGAMGLPGMR
1410 1420 1430 1440 1450
GPSGPGCKGE PGLDGRRGVD GVPGSPGPPG RKGDTGEDGY PGGPGPPGPI
1460 1470 1480 1490 1500
GDPGPKGFGP GYLGGFLLVL HSQTDQEPTC PLGMPRLWTG YSLLYLEGQE
1510 1520 1530 1540 1550
KAHNQDLGLA GSCLPVFSTL PFAYCNIHQV CHYAQRNDRS YWLASAAPLP
1560 1570 1580 1590 1600
MMPLSEEAIR PYVSRCAVCE APAQAVAVHS QDQSIPPCPQ TWRSLWIGYS
1610 1620 1630 1640 1650
FLMHTGAGDQ GGGQALMSPG SCLEDFRAAP FLECQGRQGT CHFFANKYSF
1660 1670 1680 1690
WLTTVKADLQ FSSAPAPDTL KESQAQRQKI SRCQVCVKYS
Length:1,690
Mass (Da):164,038
Last modified:September 22, 2009 - v3
Checksum:iC55711CDF14A57DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1361 – 1363GPR → AIS in AAY24061 (PubMed:15815621).Curated3
Sequence conflicti1659 – 1660LQ → FE in BAA04214 (PubMed:8365481).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0316226I → T.1 PublicationCorresponds to variant rs16823264dbSNPEnsembl.1
Natural variantiVAR_031623116G → E in BFH. 1 Publication1
Natural variantiVAR_008148441 – 446Missing in APSAR. 6
Natural variantiVAR_022069482P → S.2 PublicationsCorresponds to variant rs2229814dbSNPEnsembl.1
Natural variantiVAR_008149545G → A.2 PublicationsCorresponds to variant rs1800516dbSNPEnsembl.1
Natural variantiVAR_008150570E → Q.1 Publication1
Natural variantiVAR_055680594E → G.Corresponds to variant rs35998949dbSNPEnsembl.1
Natural variantiVAR_055681670V → I.Corresponds to variant rs34236495dbSNPEnsembl.1
Natural variantiVAR_055682759P → L.Corresponds to variant rs36121515dbSNPEnsembl.1
Natural variantiVAR_001912897G → E in BFH. 1 PublicationCorresponds to variant rs121912860dbSNPEnsembl.1
Natural variantiVAR_008151931A → T.1 PublicationCorresponds to variant rs75875272dbSNPEnsembl.1
Natural variantiVAR_031624960G → R in BFH. 2 PublicationsCorresponds to variant rs769783985dbSNPEnsembl.1
Natural variantiVAR_031625999G → E in BFH. 1 PublicationCorresponds to variant rs13027659dbSNPEnsembl.1
Natural variantiVAR_0081521004P → L.2 PublicationsCorresponds to variant rs1800517dbSNPEnsembl.1
Natural variantiVAR_0081531030G → V in APSAR. 1 Publication1
Natural variantiVAR_0316261132P → L in BFH. 1 Publication1
Natural variantiVAR_0019131201G → S in APSAR. 1 PublicationCorresponds to variant rs121912858dbSNPEnsembl.1
Natural variantiVAR_0316271327V → M.3 PublicationsCorresponds to variant rs2229813dbSNPEnsembl.1
Natural variantiVAR_0081541402P → S.1 Publication1
Natural variantiVAR_0316281403S → P.3 PublicationsCorresponds to variant rs3752895dbSNPEnsembl.1
Natural variantiVAR_0081551572P → L in APSAR. 1 PublicationCorresponds to variant rs121912863dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81053 mRNA. Translation: CAA56943.1.
Y17397
, Y17398, Y17399, Y17400, Y17401, Y17402, Y17403, Y17404, Y17405, Y17406, Y17407, Y17408, Y17409, Y17410, Y17411, Y17412, Y17413, Y17427, Y17426, Y17414, Y17415, Y17416, Y17417, Y17418, Y17419, Y17420, Y17443, Y17442, Y17441, Y17440, Y17439, Y17438, Y17437, Y17436, Y17435, Y17434, Y17433, Y17432, Y17431, Y17430, Y17429, Y17428, Y17421, Y17422, Y17423, Y17424, Y17425 Genomic DNA. Translation: CAA76763.1.
AC073149 Genomic DNA. Translation: AAY24061.1.
AC079235 Genomic DNA. Translation: AAY14670.1.
AB008496 Genomic DNA. Translation: BAA25065.1.
D17391 mRNA. Translation: BAA04214.1.
CCDSiCCDS42828.1.
PIRiA55360. CGHU1B.
RefSeqiNP_000083.3. NM_000092.4.
XP_005246338.1. XM_005246281.3.
UniGeneiHs.591645.

Genome annotation databases

EnsembliENST00000396625; ENSP00000379866; ENSG00000081052.
GeneIDi1286.
KEGGihsa:1286.
UCSCiuc061teu.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81053 mRNA. Translation: CAA56943.1.
Y17397
, Y17398, Y17399, Y17400, Y17401, Y17402, Y17403, Y17404, Y17405, Y17406, Y17407, Y17408, Y17409, Y17410, Y17411, Y17412, Y17413, Y17427, Y17426, Y17414, Y17415, Y17416, Y17417, Y17418, Y17419, Y17420, Y17443, Y17442, Y17441, Y17440, Y17439, Y17438, Y17437, Y17436, Y17435, Y17434, Y17433, Y17432, Y17431, Y17430, Y17429, Y17428, Y17421, Y17422, Y17423, Y17424, Y17425 Genomic DNA. Translation: CAA76763.1.
AC073149 Genomic DNA. Translation: AAY24061.1.
AC079235 Genomic DNA. Translation: AAY14670.1.
AB008496 Genomic DNA. Translation: BAA25065.1.
D17391 mRNA. Translation: BAA04214.1.
CCDSiCCDS42828.1.
PIRiA55360. CGHU1B.
RefSeqiNP_000083.3. NM_000092.4.
XP_005246338.1. XM_005246281.3.
UniGeneiHs.591645.

3D structure databases

ProteinModelPortaliP53420.
SMRiP53420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53420. 1 interactor.
STRINGi9606.ENSP00000379866.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP53420.
PhosphoSitePlusiP53420.

Polymorphism and mutation databases

BioMutaiCOL4A4.
DMDMi259016360.

Proteomic databases

EPDiP53420.
PaxDbiP53420.
PeptideAtlasiP53420.
PRIDEiP53420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396625; ENSP00000379866; ENSG00000081052.
GeneIDi1286.
KEGGihsa:1286.
UCSCiuc061teu.1. human.

Organism-specific databases

CTDi1286.
DisGeNETi1286.
GeneCardsiCOL4A4.
GeneReviewsiCOL4A4.
H-InvDBHIX0030014.
HGNCiHGNC:2206. COL4A4.
MalaCardsiCOL4A4.
MIMi120131. gene.
141200. phenotype.
203780. phenotype.
neXtProtiNX_P53420.
OpenTargetsiENSG00000081052.
Orphaneti88918. Autosomal dominant Alport syndrome.
88919. Autosomal recessive Alport syndrome.
97562. Benign familial hematuria.
PharmGKBiPA26721.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410YAVF. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiP53420.
KOiK06237.
OMAiPPGYKGF.
OrthoDBiEOG091G0613.
PhylomeDBiP53420.
TreeFamiTF344135.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000081052-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiCOL4A4. human.
GeneWikiiCOL4A4.
GenomeRNAii1286.
PROiP53420.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000081052.
CleanExiHS_COL4A4.
GenevisibleiP53420. HS.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 14 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO4A4_HUMAN
AccessioniPrimary (citable) accession number: P53420
Secondary accession number(s): A8MTZ1
, Q53RW9, Q53S42, Q53WR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: November 30, 2016
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.