Q14031 (CO4A6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-6(IV) chain

Gene names

Name:

COL4A6

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	1691 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
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	Deletions covering the N-terminal regions of COL4A5 and COL4A6, which are localized in a head-to-head manner, are found in the chromosome Xq22.3 centromeric deletion syndrome. This results in a phenotype with features of diffuse leiomyomatosis and Alport syndrome (DL-ATS). Ref.6 Ref.7
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
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara collagen catabolic process Traceable author statement. Source: Reactome extracellular matrix disassembly Traceable author statement. Source: Reactome
Cellular_component	collagen type IV Non-traceable author statement Ref.1. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q14031-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q14031-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MLINK → MHPG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 1691	1669	Collagen alpha-6(IV) chain		PRO_0000005853
Regions
	Domain	1467 – 1691	225	Collagen IV NC1
	Region	23 – 46	24	7S domain
	Region	47 – 1463	1417	Triple-helical region
	Motif	515 – 517	3	Cell attachment site Potential
	Motif	560 – 562	3	Cell attachment site Potential
	Motif	986 – 988	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1482 ↔ 1571		Or C-1482 with C-1568 By similarity
	Disulfide bond	1515 ↔ 1568		Or C-1515 with C-1571 By similarity
	Disulfide bond	1527 ↔ 1533		By similarity
	Disulfide bond	1590 ↔ 1687		Or C-1590 with C-1684 By similarity
	Disulfide bond	1624 ↔ 1684		Or C-1624 with C-1687 By similarity
	Disulfide bond	1636 ↔ 1643		By similarity
Natural variations
	Alternative sequence	1 – 5	5	MLINK → MHPG in isoform B.		VSP_001174
	Natural variant	455	1	S → A. Ref.3 Corresponds to variant rs1042065 [ dbSNP | Ensembl ].		VAR_015216
	Natural variant	455	1	S → P. Corresponds to variant rs1042065 [ dbSNP | Ensembl ].		VAR_059242
	Natural variant	1110	1	N → K. Ref.3 Corresponds to variant rs1042067 [ dbSNP | Ensembl ].		VAR_015217
	Natural variant	1126	1	P → S. Corresponds to variant rs35179844 [ dbSNP | Ensembl ].		VAR_032972
	Natural variant	1130	1	G → E in a colorectal cancer sample; somatic mutation. Ref.8		VAR_035748
	Natural variant	1162	1	I → V. Corresponds to variant rs34466065 [ dbSNP | Ensembl ].		VAR_032973
	Natural variant	1362	1	L → P. Corresponds to variant rs35363062 [ dbSNP | Ensembl ].		VAR_032974
Experimental info
	Sequence conflict	170	1	M → I in AAA19569. Ref.2
	Sequence conflict	170	1	M → I in AAA16338. Ref.5
	Sequence conflict	272 – 273	2	IS → LR in AAB19038. Ref.3
	Sequence conflict	272 – 273	2	IS → LR in AAB19039. Ref.3
	Sequence conflict	366	1	V → D in AAB19038. Ref.3
	Sequence conflict	366	1	V → D in AAB19039. Ref.3
	Sequence conflict	518	1	R → Q in AAB19038. Ref.3
	Sequence conflict	518	1	R → Q in AAB19039. Ref.3
	Sequence conflict	917	1	P → S in BAA04809. Ref.1
	Sequence conflict	917	1	P → S in AAB19038. Ref.3
	Sequence conflict	917	1	P → S in AAB19039. Ref.3
	Sequence conflict	1302 – 1313	12	Missing in BAA04809. Ref.1
	Sequence conflict	1356	1	P → A in BAA04809. Ref.1
	Sequence conflict	1365	1	D → H in AAB19038. Ref.3
	Sequence conflict	1365	1	D → H in AAB19039. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 9313294D4CE63067	FASTA	1,691	163,807
	10 20 30 40 50 60 MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG RPGPIGIQGP 70 80 90 100 110 120 TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP GFLGINGIPG HPGQPGPRGP 130 140 150 160 170 180 PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD 190 200 210 220 230 240 GITGPQGAPG FPGAVGPAGP PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG 250 260 270 280 290 300 PPPSTGELEF MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG 310 320 330 340 350 360 PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI DIDGAVISGN 370 380 390 400 410 420 PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL GPQGFPGLKG DQGNPGRTTI 430 440 450 460 470 480 GAAGLPGRDG LPGPPGPPGP PSPEFETETL HNKESGFPGL RGEQGPKGNL GLKGIKGDSG 490 500 510 520 530 540 FCACDGGVPN TGPPGEPGPP GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG 550 560 570 580 590 600 PKGKKGEPIL STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE 610 620 630 640 650 660 KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS KGITLPCIIP 670 680 690 700 710 720 GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG SPGLVHLPEL PGFPGPRGEK 730 740 750 760 770 780 GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT GDIFGAENGA PGEQGLQGLT GHKGFLGDSG 790 800 810 820 830 840 LPGLKGVHGK PGLLGPKGER GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG 850 860 870 880 890 900 HPGKKGTRGK KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG 910 920 930 940 950 960 SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP GPVGIPSPRR 970 980 990 1000 1010 1020 PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL PGAPGLPGII KGVSGKPGPP 1030 1040 1050 1060 1070 1080 GFMGIRGLPG LKGSSGITGF PGMPGESGSQ GIRGSPGLPG ASGLPGLKGD NGQTVEISGS 1090 1100 1110 1120 1130 1140 PGPKGQPGES GFKGTKGRDG LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE 1150 1160 1170 1180 1190 1200 PGLPGSSGHQ GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA 1210 1220 1230 1240 1250 1260 GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL PSLIAGQPGD 1270 1280 1290 1300 1310 1320 PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP GPKGPKGDQG IPGFSGLPGE 1330 1340 1350 1360 1370 1380 LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG 1390 1400 1410 1420 1430 1440 PLGLPGIDGI PGLTGDPGAQ GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG 1450 1460 1470 1480 1490 1500 PPGFEGAPGQ QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG 1510 1520 1530 1540 1550 1560 QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP IPMMPVSQTQ 1570 1580 1590 1600 1610 1620 IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG YSFLMHTAAG AEGGGQSLVS 1630 1640 1650 1660 1670 1680 PGSCLEDFRA TPFIECSGAR GTCHYFANKY SFWLTTVEER QQFGELPVSE TLKAGQLHTR 1690 VSRCQVCMKS L
	Isoform B [UniParc]. Checksum: A311225C5FF212B9	FASTA	1,690	163,629
	10 20 30 40 50 60 MHPGLWLLLV TLCLTEELAA AGEKSYGKPC GGQDCSGSCQ CFPEKGARGR PGPIGIQGPT 70 80 90 100 110 120 GPQGFTGSTG LSGLKGERGF PGLLGPYGPK GDKGPMGVPG FLGINGIPGH PGQPGPRGPP 130 140 150 160 170 180 GLDGCNGTQG AVGFPGPDGY PGLLGPPGLP GQKGSKGDPV LAPGSFKGMK GDPGLPGLDG 190 200 210 220 230 240 ITGPQGAPGF PGAVGPAGPP GLQGPPGPPG PLGPDGNMGL GFQGEKGVKG DVGLPGPAGP 250 260 270 280 290 300 PPSTGELEFM GFPKGKKGSK GEPGPKGFPG ISGPPGFPGL GTTGEKGEKG EKGIPGLPGP 310 320 330 340 350 360 RGPMGSEGVQ GPPGQQGKKG TLGFPGLNGF QGIEGQKGDI GLPGPDVFID IDGAVISGNP 370 380 390 400 410 420 GDPGVPGLPG LKGDEGIQGL RGPSGVPGLP ALSGVPGALG PQGFPGLKGD QGNPGRTTIG 430 440 450 460 470 480 AAGLPGRDGL PGPPGPPGPP SPEFETETLH NKESGFPGLR GEQGPKGNLG LKGIKGDSGF 490 500 510 520 530 540 CACDGGVPNT GPPGEPGPPG PWGLIGLPGL KGARGDRGSG GAQGPAGAPG LVGPLGPSGP 550 560 570 580 590 600 KGKKGEPILS TIQGMPGDRG DSGSQGFRGV IGEPGKDGVP GLPGLPGLPG DGGQGFPGEK 610 620 630 640 650 660 GLPGLPGEKG HPGPPGLPGN GLPGLPGPRG LPGDKGKDGL PGQQGLPGSK GITLPCIIPG 670 680 690 700 710 720 SYGPSGFPGT PGFPGPKGSR GLPGTPGQPG SSGSKGEPGS PGLVHLPELP GFPGPRGEKG 730 740 750 760 770 780 LPGFPGLPGK DGLPGMIGSP GLPGSKGATG DIFGAENGAP GEQGLQGLTG HKGFLGDSGL 790 800 810 820 830 840 PGLKGVHGKP GLLGPKGERG SPGTPGQVGQ PGTPGSSGPY GIKGKSGLPG APGFPGISGH 850 860 870 880 890 900 PGKKGTRGKK GPPGSIVKKG LPGLKGLPGN PGLVGLKGSP GSPGVAGLPA LSGPKGEKGS 910 920 930 940 950 960 VGFVGFPGIP GLPGIPGTRG LKGIPGSTGK MGPSGRAGTP GEKGDRGNPG PVGIPSPRRP 970 980 990 1000 1010 1020 MSNLWLKGDK GSQGSAGSNG FPGPRGDKGE AGRPGPPGLP GAPGLPGIIK GVSGKPGPPG 1030 1040 1050 1060 1070 1080 FMGIRGLPGL KGSSGITGFP GMPGESGSQG IRGSPGLPGA SGLPGLKGDN GQTVEISGSP 1090 1100 1110 1120 1130 1140 GPKGQPGESG FKGTKGRDGL IGNIGFPGNK GEDGKVGVSG DVGLPGAPGF PGVAGMRGEP 1150 1160 1170 1180 1190 1200 GLPGSSGHQG AIGPLGSPGL IGPKGFPGFP GLHGLNGLPG TKGTHGTPGP SITGVPGPAG 1210 1220 1230 1240 1250 1260 LPGPKGEKGY PGIGIGAPGK PGLRGQKGDR GFPGLQGPAG LPGAPGISLP SLIAGQPGDP 1270 1280 1290 1300 1310 1320 GRPGLDGERG RPGPAGPPGP PGPSSNQGDT GDPGFPGIPG PKGPKGDQGI PGFSGLPGEL 1330 1340 1350 1360 1370 1380 GLKGMRGEPG FMGTPGKVGP PGDPGFPGMK GKAGPRGSSG LQGDPGQTPT AEAVQVPPGP 1390 1400 1410 1420 1430 1440 LGLPGIDGIP GLTGDPGAQG PVGLQGSKGL PGIPGKDGPS GLPGPPGALG DPGLPGLQGP 1450 1460 1470 1480 1490 1500 PGFEGAPGQQ GPFGMPGMPG QSMRVGYTLV KHSQSEQVPP CPIGMSQLWV GYSLLFVEGQ 1510 1520 1530 1540 1550 1560 EKAHNQDLGF AGSCLPRFST MPFIYCNINE VCHYARRNDK SYWLSTTAPI PMMPVSQTQI 1570 1580 1590 1600 1610 1620 PQYISRCSVC EAPSQAIAVH SQDITIPQCP LGWRSLWIGY SFLMHTAAGA EGGGQSLVSP 1630 1640 1650 1660 1670 1680 GSCLEDFRAT PFIECSGARG TCHYFANKYS FWLTTVEERQ QFGELPVSET LKAGQLHTRV 1690 SRCQVCMKSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new collagen IV chain, alpha 6(IV), by cDNA isolation and assignment of the gene to chromosome Xq22, which is the same locus for COL4A5." Oohashi T., Sugimoto M., Mattei M.-G., Ninomiya Y. J. Biol. Chem. 269:7520-7526(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). Tissue: Eye and Kidney.
[2]	"Complete primary structure of the sixth chain of human basement membrane collagen, alpha 6(IV). Isolation of the cDNAs for alpha 6(IV) and comparison with five other type IV collagen chains." Zhou J., Ding M., Zhao Z., Reeders S.T. J. Biol. Chem. 269:13193-13199(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]	"Structure of the human type IV collagen COL4A6 gene, which is mutated in Alport syndrome-associated leiomyomatosis." Zhang X., Zhou J., Reeders S.T., Tryggvason K. Genomics 33:473-479(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), VARIANTS ALA-455 AND LYS-1110.
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in inherited smooth muscle tumors." Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P., de Paepe A., Tryggvason K., Reeders S.T. Science 261:1167-1169(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-542 (ISOFORM A), INVOLVEMENT IN DL-ATS.
[7]	"Alport syndrome with diffuse leiomyomatosis." Anker M.C., Arnemann J., Neumann K., Ahrens P., Schmidt H., Koenig R. Am. J. Med. Genet. A 119:381-385(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DL-ATS.
[8]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-1130.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21337 mRNA. Translation: BAA04809.1. U04845 mRNA. Translation: AAA19569.2. U47004 , U46959, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19038.1. U47004 , U46960, U46961, U46962, U46963, U46964, U46965, U46966, U46967, U46968, U46969, U46970, U46971, U46972, U46973, U46974, U46975, U46976, U46977, U46978, U46979, U46980, U46981, U46982, U46983, U46984, U46985, U46986, U46987, U46988, U46989, U46990, U46991, U46992, U46993, U46994, U46995, U46996, U46997, U46998, U46999, U47000, U47001, U47002, U47003 Genomic DNA. Translation: AAB19039.1. AL136080 , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40756.1. AL136080 , AL031177, AL034369, AL109943 Genomic DNA. Translation: CAI40758.1. AL034369 , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42045.1. AL034369 , AL031177, AL109943, AL136080 Genomic DNA. Translation: CAI42047.1. AL109943 , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42993.1. AL109943 , AL031177, AL034369, AL136080 Genomic DNA. Translation: CAI42995.1. AL031177 , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43139.1. AL031177 , AL034369, AL109943, AL136080 Genomic DNA. Translation: CAI43140.1. CH471120 Genomic DNA. Translation: EAX02688.1. L22763 mRNA. Translation: AAA16338.1.
IPI	IPI00472200. IPI00514030.
PIR	CGHU6B. A54122.
RefSeq	NP_001838.2. NM_001847.2. NP_378667.1. NM_033641.2.
UniGene	Hs.145586.
3D structure databases
ProteinModelPortal	Q14031.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14031. 1 interaction.
PTM databases
PhosphoSite	Q14031.
Polymorphism databases
DMDM	116241307.
Proteomic databases
PaxDb	Q14031.
PRIDE	Q14031.
Protocols and materials databases
DNASU	1288.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334504; ENSP00000334733; ENSG00000197565. ENST00000372216; ENSP00000361290; ENSG00000197565.
GeneID	1288.
KEGG	hsa:1288.
UCSC	uc004env.4. human. uc004enw.4. human.
Organism-specific databases
CTD	1288.
GeneCards	GC0XM107386.
H-InvDB	HIX0056214.
HGNC	HGNC:2208. COL4A6.
MIM	303631. gene.
neXtProt	NX_Q14031.
Orphanet	1018. X-linked diffuse leiomyomatosis - Alport syndrome.
PharmGKB	PA26723.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG004933.
KO	K06237.
OrthoDB	EOG4P2Q1K.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q14031.
Bgee	Q14031.
Genevestigator	Q14031.
GermOnline	ENSG00000197565. 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. 22 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
GenomeRNAi	1288.
NextBio	5213.
PMAP-CutDB	Q5JYH8.
SOURCE	Search...

Entry information

Entry name

CO4A6_HUMAN

Accession

Primary (citable) accession number: Q14031
Secondary accession number(s): Q12823 , Q14053, Q5JYH6, Q5JYH8, Q9NQM5, Q9NTX3, Q9UJ76, Q9UMG6, Q9Y4L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 17, 2006
Last modified:	May 29, 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.