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P53420 (CO4A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1690 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.8

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 in kidney, eye, basement membranes of lens capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal kidney and fetal lung. Ref.7 reports similar levels of expression of alpha 3 and alpha 4 type IV collagens in kidney, but Ref.1 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. Ref.1 Ref.7

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.

Involvement in disease

Alport syndrome, autosomal recessive (APSAR) [MIM:203780]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.10

Hematuria, benign familial (BFH) [MIM:141200]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13

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

Signal peptide1 – 3838 Potential
Chain39 – 16901652Collagen alpha-4(IV) chain
PRO_0000005850

Regions

Domain1465 – 1690226Collagen IV NC1
Region39 – 64267S domain
Region65 – 14591395Triple-helical region
Motif94 – 963Cell attachment site Potential
Motif145 – 1473Cell attachment site Potential
Motif189 – 1913Cell attachment site Potential
Motif310 – 3123Cell attachment site Potential
Motif724 – 7263Cell attachment site Potential
Motif785 – 7873Cell attachment site Potential
Motif989 – 9913Cell attachment site Potential
Motif1212 – 12143Cell attachment site Potential

Sites

Site1206 – 12072Cleavage; by collagenase By similarity

Amino acid modifications

Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Potential
Disulfide bond1480 ↔ 1569Or C-1480 with C-1566 By similarity
Disulfide bond1513 ↔ 1566Or C-1513 with C-1569 By similarity
Disulfide bond1525 ↔ 1531 By similarity
Disulfide bond1588 ↔ 1686Or C-1588 with C-1683 By similarity
Disulfide bond1622 ↔ 1683Or C-1622 with C-1686 By similarity
Disulfide bond1634 ↔ 1641 By similarity

Natural variations

Natural variant61I → T. Ref.12
Corresponds to variant rs16823264 [ dbSNP | Ensembl ].
VAR_031622
Natural variant1161G → E in BFH. Ref.13
VAR_031623
Natural variant441 – 4466Missing in APSAR.
VAR_008148
Natural variant4821P → S. Ref.12 Ref.13
Corresponds to variant rs2229814 [ dbSNP | Ensembl ].
VAR_022069
Natural variant5451G → A. Ref.2 Ref.12
Corresponds to variant rs1800516 [ dbSNP | Ensembl ].
VAR_008149
Natural variant5701E → Q. Ref.2
VAR_008150
Natural variant5941E → G.
Corresponds to variant rs35998949 [ dbSNP | Ensembl ].
VAR_055680
Natural variant6701V → I.
Corresponds to variant rs34236495 [ dbSNP | Ensembl ].
VAR_055681
Natural variant7591P → L.
Corresponds to variant rs36121515 [ dbSNP | Ensembl ].
VAR_055682
Natural variant8971G → E in BFH. Ref.11
VAR_001912
Natural variant9311A → T. Ref.2
Corresponds to variant rs75875272 [ dbSNP | Ensembl ].
VAR_008151
Natural variant9601G → R in BFH. Ref.12 Ref.13
VAR_031624
Natural variant9991G → E in BFH. Ref.13
Corresponds to variant rs13027659 [ dbSNP | Ensembl ].
VAR_031625
Natural variant10041P → L. Ref.1 Ref.2
Corresponds to variant rs1800517 [ dbSNP | Ensembl ].
VAR_008152
Natural variant10301G → V in APSAR. Ref.2
VAR_008153
Natural variant11321P → L in BFH. Ref.13
VAR_031626
Natural variant12011G → S in APSAR. Ref.10
VAR_001913
Natural variant13271V → M. Ref.1 Ref.2 Ref.5
Corresponds to variant rs2229813 [ dbSNP | Ensembl ].
VAR_031627
Natural variant14021P → S. Ref.2
VAR_008154
Natural variant14031S → P. Ref.1 Ref.2 Ref.5
Corresponds to variant rs3752895 [ dbSNP | Ensembl ].
VAR_031628
Natural variant15721P → L in APSAR. Ref.2
VAR_008155

Experimental info

Sequence conflict1361 – 13633GPR → AIS in AAY24061. Ref.3
Sequence conflict1659 – 16602LQ → FE in BAA04214. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P53420 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: C55711CDF14A57DB

FASTA1,690164,038
        10         20         30         40         50         60 
MWSLHIVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYIGPCGGR DCSVCHCVPE 

        70         80         90        100        110        120 
KGSRGPPGPP GPQGPIGPLG APGPIGLSGE KGMRGDRGPP GAAGDKGDKG PTGVPGFPGL 

       130        140        150        160        170        180 
DGIPGHPGPP GPRGKPGMSG HNGSRGDPGF PGGRGALGPG GPLGHPGEKG EKGNSVFILG 

       190        200        210        220        230        240 
AVKGIQGDRG DPGLPGLPGS WGAGGPAGPT GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG 

       250        260        270        280        290        300 
QMGDPGEVGQ QGSPGPTLLV EPPDFCLYKG EKGIKGIPGM VGLPGPPGRK GESGIGAKGE 

       310        320        330        340        350        360 
KGIPGFPGPR GDPGSYGSPG FPGLKGELGL VGDPGLFGLI GPKGDPGNRG HPGPPGVLVT 

       370        380        390        400        410        420 
PPLPLKGPPG DPGFPGRYGE TGDVGPPGPP GLLGRPGEAC AGMIGPPGPQ GFPGLPGLPG 

       430        440        450        460        470        480 
EAGIPGRPDS APGKPGKPGS PGLPGAPGLQ GLPGSSVIYC SVGNPGPQGI KGKVGPPGGR 

       490        500        510        520        530        540 
GPKGEKGNEG LCACEPGPMG PPGPPGLPGR QGSKGDLGLP GWLGTKGDPG PPGAEGPPGL 

       550        560        570        580        590        600 
PGKHGASGPP GNKGAKGDMV VSRVKGHKGE RGPDGPPGFP GQPGSHGRDG HAGEKGDPGP 

       610        620        630        640        650        660 
PGDHEDATPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGHP GVRGPDGLKG 

       670        680        690        700        710        720 
QKGDTISCNV TYPGRHGPPG FDGPPGPKGF PGPQGAPGLS GSDGHKGRPG TPGTAEIPGP 

       730        740        750        760        770        780 
PGFRGDMGDP GFGGEKGSSP VGPPGPPGSP GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG 

       790        800        810        820        830        840 
IKGPRGDPGC PGAEGPAGIP GFLGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG 

       850        860        870        880        890        900 
LPGYPGSPGA PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG 

       910        920        930        940        950        960 
PPGPKGPRGL PGFPGFPGER GKPGAEGCPG AKGEPGEKGM SGLPGDRGLR GAKGAIGPPG 

       970        980        990       1000       1010       1020 
DEGEMAIISQ KGTPGEPGPP GDDGFPGERG DKGTPGMQGR RGEPGRYGPP GFHRGEPGEK 

      1030       1040       1050       1060       1070       1080 
GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ GEPGSPGPPG FSGIDGARGP KGNKGDPASH 

      1090       1100       1110       1120       1130       1140 
FGPPGPKGEP GSPGCPGHFG ASGEQGLPGI QGPRGSPGRP GPPGSSGPPG CPGDHGMPGL 

      1150       1160       1170       1180       1190       1200 
RGQPGEMGDP GPRGLQGDPG IPGPPGIKGP SGSPGLNGLH GLKGQKGTKG ASGLHDVGPP 

      1210       1220       1230       1240       1250       1260 
GPVGIPGLKG ERGDPGSPGI SPPGPRGKKG PPGPPGSSGP PGPAGATGRA PKDIPDPGPP 

      1270       1280       1290       1300       1310       1320 
GDQGPPGPDG PRGAPGPPGL PGSVDLLRGE PGDCGLPGPP GPPGPPGPPG YKGFPGCDGK 

      1330       1340       1350       1360       1370       1380 
DGQKGPVGFP GPQGPHGFPG PPGEKGLPGP PGRKGPTGLP GPRGEPGPPA DVDDCPRIPG 

      1390       1400       1410       1420       1430       1440 
LPGAPGMRGP EGAMGLPGMR GPSGPGCKGE PGLDGRRGVD GVPGSPGPPG RKGDTGEDGY 

      1450       1460       1470       1480       1490       1500 
PGGPGPPGPI GDPGPKGFGP GYLGGFLLVL HSQTDQEPTC PLGMPRLWTG YSLLYLEGQE 

      1510       1520       1530       1540       1550       1560 
KAHNQDLGLA GSCLPVFSTL PFAYCNIHQV CHYAQRNDRS YWLASAAPLP MMPLSEEAIR 

      1570       1580       1590       1600       1610       1620 
PYVSRCAVCE APAQAVAVHS QDQSIPPCPQ TWRSLWIGYS FLMHTGAGDQ GGGQALMSPG 

      1630       1640       1650       1660       1670       1680 
SCLEDFRAAP FLECQGRQGT CHFFANKYSF WLTTVKADLQ FSSAPAPDTL KESQAQRQKI 

      1690 
SRCQVCVKYS 

« Hide

References

« Hide 'large scale' references
[1]"Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains."
Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.
J. Biol. Chem. 269:26172-26177(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS LEU-1004; MET-1327 AND PRO-1403.
Tissue: Kidney.
[2]"Determination of the genomic structure of the COL4A4 gene and of novel mutations causing autosomal recessive Alport syndrome."
Boye E., Mollet G., Forestier L., Cohen-Solal L., Heidet L., Cochat P., Gruenfeld J.-P., Palcoux J.-B., Gubler M.-C., Antignac C.
Am. J. Hum. Genet. 63:1329-1340(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS APSAR VAL-1030 AND LEU-1572, VARIANTS ALA-545; GLN-570; THR-931; LEU-1004; MET-1327; SER-1402 AND PRO-1403.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and alpha4(IV) collagen chains are arranged head-to-head on chromosome 2q36."
Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H., Ninomiya Y.
FEBS Lett. 424:11-16(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
[5]"cDNA isolation and partial gene structure of the human alpha 4(IV) collagen chain."
Sugimoto M., Oohashi T., Yoshioka H., Matsuo N., Ninomiya Y.
FEBS Lett. 330:122-128(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1219-1690, VARIANTS MET-1327 AND PRO-1403.
Tissue: Eye.
[6]"Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha 4 chain of basement membrane collagen type IV and assignment of the gene to the distal long arm of human chromosome 2."
Kamagata Y., Mattei M.-G., Ninomiya Y.
J. Biol. Chem. 267:23753-23758(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1407-1507.
[7]"Complete primary structure of the human alpha 3(IV) collagen chain. Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human tissues."
Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.
J. Biol. Chem. 269:23013-23017(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter interactions with the alpha4 and alpha5 NC1 domains."
Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y., Hudson B.G.
J. Biol. Chem. 277:40075-40083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: HEXAMERIZATION.
[9]"The clinical spectrum of type IV collagen mutations."
Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.
Hum. Mutat. 9:477-499(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[10]"Identification of mutations in the alpha 3(IV) and alpha 4(IV) collagen genes in autosomal recessive Alport syndrome."
Mochizuki T., Lemmink H.H., Mariyama M., Antignac C., Gubler M.-C., Pirson Y., Verellen-Dumoulin C., Chan B., Schroeder C.H., Smeets H.J.M., Reeders S.T.
Nat. Genet. 8:77-82(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APSAR SER-1201.
[11]"Benign familial hematuria due to mutation of the type IV collagen alpha4 gene."
Lemmink H.H., Nillesen W.N., Mochizuki T., Schroeder C.H., Brunner H.G., van Oost B.A., Monnens L.A.H., Smeets H.J.M.
J. Clin. Invest. 98:1114-1118(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BFH GLU-897.
[12]"Mutations in the COL4A4 and COL4A3 genes cause familial benign hematuria."
Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A., Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M., Antignac C., Darnell A., Torra R.
J. Am. Soc. Nephrol. 13:1248-1254(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BFH ARG-960, VARIANTS THR-6; SER-482 AND ALA-545.
[13]"Mutations in the COL4A4 gene in thin basement membrane disease."
Buzza M., Dagher H., Wang Y.Y., Wilson D., Babon J.J., Cotton R.G., Savige J.
Kidney Int. 63:447-453(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BFH GLU-116; ARG-960; GLU-999 AND LEU-1132, VARIANT SER-482.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81053 mRNA. Translation: CAA56943.1.
Y17397 expand/collapse EMBL AC list , 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.
CCDSCCDS42828.1.
PIRCGHU1B. A55360.
RefSeqNP_000083.3. NM_000092.4.
XP_005246338.1. XM_005246281.1.
UniGeneHs.591645.

3D structure databases

ProteinModelPortalP53420.
SMRP53420. Positions 1465-1688.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107683. 1 interaction.
IntActP53420. 1 interaction.
STRING9606.ENSP00000379866.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP53420.

Polymorphism databases

DMDM259016360.

Proteomic databases

PaxDbP53420.
PRIDEP53420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396625; ENSP00000379866; ENSG00000081052.
GeneID1286.
KEGGhsa:1286.
UCSCuc021vxr.1. human.

Organism-specific databases

CTD1286.
GeneCardsGC02M227867.
GeneReviewsCOL4A4.
H-InvDBHIX0030014.
HGNCHGNC:2206. COL4A4.
MIM120131. gene.
141200. phenotype.
203780. phenotype.
neXtProtNX_P53420.
Orphanet88918. Autosomal dominant Alport syndrome.
88919. Autosomal recessive Alport syndrome.
97562. Benign familial hematuria.
PharmGKBPA26721.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085652.
HOVERGENHBG004933.
InParanoidP53420.
KOK06237.
OMAPPGYKGF.
OrthoDBEOG7RZ5P3.
PhylomeDBP53420.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP53420.
BgeeP53420.
CleanExHS_COL4A4.
GenevestigatorP53420.

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. 19 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL4A4. human.
GeneWikiCOL4A4.
GenomeRNAi1286.
NextBio5201.
PROP53420.
SOURCESearch...

Entry information

Entry nameCO4A4_HUMAN
AccessionPrimary (citable) accession number: P53420
Secondary accession number(s): A8MTZ1 expand/collapse secondary AC list , Q53RW9, Q53S42, Q53WR1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM