P53420 (CO4A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-4(IV) chain

Gene names

Name:

COL4A4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1690 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Ref.8
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 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.

Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Alport syndrome Deafness Disease mutation
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome glomerular basement membrane development Inferred from mutant phenotype PubMed 17942953PubMed 19675380. Source: UniProtKB
Cellular_component	basal lamina Inferred from direct assay PubMed 2211832. Source: UniProtKB collagen type IV Inferred from direct assay Ref.1. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent Inferred from mutant phenotype PubMed 17942953PubMed 19675380. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38	Potential
	Chain	39 – 1690	1652	Collagen alpha-4(IV) chain		PRO_0000005850
Regions
	Domain	1465 – 1690	226	Collagen IV NC1
	Region	39 – 64	26	7S domain
	Region	65 – 1459	1395	Triple-helical region
	Motif	94 – 96	3	Cell attachment site Potential
	Motif	145 – 147	3	Cell attachment site Potential
	Motif	189 – 191	3	Cell attachment site Potential
	Motif	310 – 312	3	Cell attachment site Potential
	Motif	724 – 726	3	Cell attachment site Potential
	Motif	785 – 787	3	Cell attachment site Potential
	Motif	989 – 991	3	Cell attachment site Potential
	Motif	1212 – 1214	3	Cell attachment site Potential
Sites
	Site	1206 – 1207	2	Cleavage; by collagenase By similarity
Amino acid modifications
	Glycosylation	142	1	N-linked (GlcNAc...) Potential
	Glycosylation	669	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1480 ↔ 1569		Or C-1480 with C-1566 By similarity
	Disulfide bond	1513 ↔ 1566		Or C-1513 with C-1569 By similarity
	Disulfide bond	1525 ↔ 1531		By similarity
	Disulfide bond	1588 ↔ 1686		Or C-1588 with C-1683 By similarity
	Disulfide bond	1622 ↔ 1683		Or C-1622 with C-1686 By similarity
	Disulfide bond	1634 ↔ 1641		By similarity
Natural variations
	Natural variant	6	1	I → T. Ref.12 Corresponds to variant rs16823264 [ dbSNP | Ensembl ].		VAR_031622
	Natural variant	116	1	G → E in BFH. Ref.13		VAR_031623
	Natural variant	441 – 446	6	Missing in APSAR.		VAR_008148
	Natural variant	482	1	P → S. Ref.12 Ref.13 Corresponds to variant rs2229814 [ dbSNP | Ensembl ].		VAR_022069
	Natural variant	545	1	G → A. Ref.2 Ref.12 Corresponds to variant rs1800516 [ dbSNP | Ensembl ].		VAR_008149
	Natural variant	570	1	E → Q. Ref.2		VAR_008150
	Natural variant	594	1	E → G. Corresponds to variant rs35998949 [ dbSNP | Ensembl ].		VAR_055680
	Natural variant	670	1	V → I. Corresponds to variant rs34236495 [ dbSNP | Ensembl ].		VAR_055681
	Natural variant	759	1	P → L. Corresponds to variant rs36121515 [ dbSNP | Ensembl ].		VAR_055682
	Natural variant	897	1	G → E in BFH. Ref.11		VAR_001912
	Natural variant	931	1	A → T. Ref.2		VAR_008151
	Natural variant	960	1	G → R in BFH. Ref.12 Ref.13		VAR_031624
	Natural variant	999	1	G → E in BFH. Ref.13 Corresponds to variant rs13027659 [ dbSNP | Ensembl ].		VAR_031625
	Natural variant	1004	1	P → L. Ref.1 Ref.2 Corresponds to variant rs1800517 [ dbSNP | Ensembl ].		VAR_008152
	Natural variant	1030	1	G → V in APSAR. Ref.2		VAR_008153
	Natural variant	1132	1	P → L in BFH. Ref.13		VAR_031626
	Natural variant	1201	1	G → S in APSAR. Ref.10		VAR_001913
	Natural variant	1327	1	V → M. Ref.1 Ref.2 Ref.5 Corresponds to variant rs2229813 [ dbSNP | Ensembl ].		VAR_031627
	Natural variant	1402	1	P → S. Ref.2		VAR_008154
	Natural variant	1403	1	S → P. Ref.1 Ref.2 Ref.5 Corresponds to variant rs3752895 [ dbSNP | Ensembl ].		VAR_031628
	Natural variant	1572	1	P → L in APSAR. Ref.2		VAR_008155
Experimental info
	Sequence conflict	1361 – 1363	3	GPR → AIS in AAY24061. Ref.3
	Sequence conflict	1659 – 1660	2	LQ → FE in BAA04214. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P53420 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: C55711CDF14A57DB	FASTA	1,690	164,038
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00478572.
PIR	CGHU1B. A55360.
RefSeq	NP_000083.3. NM_000092.4.
UniGene	Hs.591645.
3D structure databases
ProteinModelPortal	P53420.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53420. 1 interaction.
STRING	9606.ENSP00000379866.
PTM databases
PhosphoSite	P53420.
Polymorphism databases
DMDM	259016360.
Proteomic databases
PaxDb	P53420.
PRIDE	P53420.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396625; ENSP00000379866; ENSG00000081052.
GeneID	1286.
KEGG	hsa:1286.
UCSC	uc021vxr.1. human.
Organism-specific databases
CTD	1286.
GeneCards	GC02M227867.
H-InvDB	HIX0030014.
HGNC	HGNC:2206. COL4A4.
MIM	120131. gene. 141200. phenotype. 203780. phenotype.
neXtProt	NX_P53420.
Orphanet	88919. Autosomal recessive Alport syndrome. 97562. Benign familial hematuria.
PharmGKB	PA26721.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000085652.
HOVERGEN	HBG004933.
InParanoid	P53420.
KO	K06237.
OMA	FRGDMGD.
OrthoDB	EOG4XGZZF.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization.
Gene expression databases
Bgee	P53420.
CleanEx	HS_COL4A4.
Genevestigator	P53420.
GermOnline	ENSG00000081052. Homo sapiens.
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. 19 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...
Other
ChiTaRS	COL4A4. human.
GenomeRNAi	1286.
NextBio	5201.
SOURCE	Search...

Entry information

Entry name

CO4A4_HUMAN

Accession

Primary (citable) accession number: P53420
Secondary accession number(s): A8MTZ1 , Q53RW9, Q53S42, Q53WR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 22, 2009
Last modified:	May 1, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.