P08572 (CO4A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-2(IV) chain

Cleaved into the following chain:

1. Canstatin

Gene names

Name:

COL4A2

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	1712 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. Ref.13 Ref.17 Ref.18 Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins. Ref.13 Ref.17 Ref.18
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. Proteolytic processing produces the C-terminal NC1 peptide, canstatin.
Involvement in disease	Porencephaly 2 (POREN2) [MIM:614483]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.23
Sequence similarities	Belongs to the type IV collagen family. Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara extracellular matrix organization Non-traceable author statement Ref.6. Source: UniProtKB negative regulation of angiogenesis Inferred from direct assay Ref.13. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	collagen type IV Traceable author statement Ref.4Ref.3. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent Traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COL4A1	P02462	2	EBI-2432506,EBI-2432478

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Propeptide

26 – 183

158

N-terminal propeptide (7S domain)

PRO_0000005824

Chain

184 – 1712

1529

Collagen alpha-2(IV) chain

PRO_0000005825

Chain

1486 – 1712

227

Canstatin

PRO_0000283775

Regions

Domain

1489 – 1712

224

Collagen IV NC1

Region

184 – 1484

1301

Triple-helical region

Amino acid modifications

Glycosylation

138

1

N-linked (GlcNAc...) Ref.1

Disulfide bond

1504 ↔ 1593

Disulfide bond

1537 ↔ 1590

Disulfide bond

1549 ↔ 1555

Disulfide bond

1612 ↔ 1708

Disulfide bond

1646 ↔ 1705

Disulfide bond

1658 ↔ 1665

Natural variations

Natural variant

192

1

V → F Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs62621885 [ dbSNP | Ensembl ].

VAR_067551

Natural variant

517

1

R → K. Ref.3 Ref.21 Ref.23
Corresponds to variant rs7990383 [ dbSNP | Ensembl ].

VAR_048796

Natural variant

683

1

G → A. Ref.3 Ref.21 Ref.23
Corresponds to variant rs3803230 [ dbSNP | Ensembl ].

VAR_048797

Natural variant

701

1

K → R Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs78829338 [ dbSNP | Ensembl ].

VAR_067552

Natural variant

718

1

P → S Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs9583500 [ dbSNP | Ensembl ].

VAR_067836

Natural variant

1037

1

G → E in POREN2. Ref.22

VAR_067837

Natural variant

1109

1

R → Q Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.23
Corresponds to variant rs184812559 [ dbSNP | Ensembl ].

VAR_067553

Natural variant

1123

1

E → G Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. Ref.23

VAR_067554

Natural variant

1150

1

Q → K Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. Ref.23

VAR_067555

Natural variant

1152

1

G → D in POREN2; incomplete penetrance. Ref.22

VAR_067838

Natural variant

1389

1

G → R Probable disease-associated mutation found in a family with porencephaly and small-vessel disease in the form of scattered white matter lesions; impairs COL4A2 and COL4A1 secretion; the mutant protein is retained in the endoplasmic reticulum. Ref.24

VAR_067556

Natural variant

1399

1

V → I. Ref.8 Ref.23
Corresponds to variant rs45520539 [ dbSNP | Ensembl ].

VAR_067557

Natural variant

1690

1

A → T Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. Ref.23

VAR_067558

Experimental info

Sequence conflict

471

1

R → P in CAA29076. Ref.3

Sequence conflict

1041

1

V → L in AAA52043. Ref.7

Sequence conflict

1419

1

M → I in CAA29098. Ref.8

Sequence conflict

1575

1

M → I in AAA58422. Ref.12

Sequence conflict

1636

1

G → V in AAA52043. Ref.7

Sequence conflict

1663

1

G → H AA sequence Ref.11

Sequence conflict

1701

1

H → G AA sequence Ref.11

Secondary structure

1

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1712

Helix Strand Turn

Details...

Beta strand

1490 – 1495

6

Beta strand

1497 – 1500

4

Beta strand

1509 – 1522

14

Beta strand

1525 – 1528

4

Helix

1534 – 1536

3

Beta strand

1537 – 1540

4

Beta strand

1546 – 1550

5

Turn

1551 – 1553

3

Beta strand

1554 – 1558

5

Beta strand

1563 – 1568

6

Helix

1580 – 1586

7

Beta strand

1589 – 1597

9

Beta strand

1599 – 1603

5

Beta strand

1605 – 1608

4

Beta strand

1616 – 1629

14

Beta strand

1635 – 1637

3

Helix

1643 – 1645

3

Beta strand

1646 – 1649

4

Beta strand

1655 – 1659

5

Turn

1660 – 1663

4

Beta strand

1664 – 1666

3

Beta strand

1672 – 1677

6

Beta strand

1680 – 1684

5

Beta strand

1691 – 1694

4

Helix

1699 – 1701

3

Beta strand

1704 – 1710

7

Sequences

	Sequence		Length	Mass (Da)
	P08572 [UniParc]. Last modified April 3, 2007. Version 4. Checksum: E0DABEEAB349D8AF	FASTA	1,712	167,553
	10 20 30 40 50 60 MGRDQRAVAG PALRRWLLLG TVTVGFLAQS VLAGVKKFDV PCGGRDCSGG CQCYPEKGGR 70 80 90 100 110 120 GQPGPVGPQG YNGPPGLQGF PGLQGRKGDK GERGAPGVTG PKGDVGARGV SGFPGADGIP 130 140 150 160 170 180 GHPGQGGPRG RPGYDGCNGT QGDSGPQGPP GSEGFTGPPG PQGPKGQKGE PYALPKEERD 190 200 210 220 230 240 RYRGEPGEPG LVGFQGPPGR PGHVGQMGPV GAPGRPGPPG PPGPKGQQGN RGLGFYGVKG 250 260 270 280 290 300 EKGDVGQPGP NGIPSDTLHP IIAPTGVTFH PDQYKGEKGS EGEPGIRGIS LKGEEGIMGF 310 320 330 340 350 360 PGLRGYPGLS GEKGSPGQKG SRGLDGYQGP DGPRGPKGEA GDPGPPGLPA YSPHPSLAKG 370 380 390 400 410 420 ARGDPGFPGA QGEPGSQGEP GDPGLPGPPG LSIGDGDQRR GLPGEMGPKG FIGDPGIPAL 430 440 450 460 470 480 YGGPPGPDGK RGPPGPPGLP GPPGPDGFLF GLKGAKGRAG FPGLPGSPGA RGPKGWKGDA 490 500 510 520 530 540 GECRCTEGDE AIKGLPGLPG PKGFAGINGE PGRKGDRGDP GQHGLPGFPG LKGVPGNIGA 550 560 570 580 590 600 PGPKGAKGDS RTITTKGERG QPGVPGVPGM KGDDGSPGRD GLDGFPGLPG PPGDGIKGPP 610 620 630 640 650 660 GDPGYPGIPG TKGTPGEMGP PGLGLPGLKG QRGFPGDAGL PGPPGFLGPP GPAGTPGQID 670 680 690 700 710 720 CDTDVKRAVG GDRQEAIQPG CIGGPKGLPG LPGPPGPTGA KGLRGIPGFA GADGGPGPRG 730 740 750 760 770 780 LPGDAGREGF PGPPGFIGPR GSKGAVGLPG PDGSPGPIGL PGPDGPPGER GLPGEVLGAQ 790 800 810 820 830 840 PGPRGDAGVP GQPGLKGLPG DRGPPGFRGS QGMPGMPGLK GQPGLPGPSG QPGLYGPPGL 850 860 870 880 890 900 HGFPGAPGQE GPLGLPGIPG REGLPGDRGD PGDTGAPGPV GMKGLSGDRG DAGFTGEQGH 910 920 930 940 950 960 PGSPGFKGID GMPGTPGLKG DRGSPGMDGF QGMPGLKGRP GFPGSKGEAG FFGIPGLKGL 970 980 990 1000 1010 1020 AGEPGFKGSR GDPGPPGPPP VILPGMKDIK GEKGDEGPMG LKGYLGAKGI QGMPGIPGLS 1030 1040 1050 1060 1070 1080 GIPGLPGRPG HIKGVKGDIG VPGIPGLPGF PGVAGPPGIT GFPGFIGSRG DKGAPGRAGL 1090 1100 1110 1120 1130 1140 YGEIGATGDF GDIGDTINLP GRPGLKGERG TTGIPGLKGF FGEKGTEGDI GFPGITGVTG 1150 1160 1170 1180 1190 1200 VQGPPGLKGQ TGFPGLTGPP GSQGELGRIG LPGGKGDDGW PGAPGLPGFP GLRGIRGLHG 1210 1220 1230 1240 1250 1260 LPGTKGFPGS PGSDIHGDPG FPGPPGERGD PGEANTLPGP VGVPGQKGDQ GAPGERGPPG 1270 1280 1290 1300 1310 1320 SPGLQGFPGI TPPSNISGAP GDKGAPGIFG LKGYRGPPGP PGSAALPGSK GDTGNPGAPG 1330 1340 1350 1360 1370 1380 TPGTKGWAGD SGPQGRPGVF GLPGEKGPRG EQGFMGNTGP TGAVGDRGPK GPKGDPGFPG 1390 1400 1410 1420 1430 1440 APGTVGAPGI AGIPQKIAVQ PGTVGPQGRR GPPGAPGEMG PQGPPGEPGF RGAPGKAGPQ 1450 1460 1470 1480 1490 1500 GRGGVSAVPG FRGDEGPIGH QGPIGQEGAP GRPGSPGLPG MPGRSVSIGY LLVKHSQTDQ 1510 1520 1530 1540 1550 1560 EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN PGDVCYYASR 1570 1580 1590 1600 1610 1620 NDKSYWLSTT APLPMMPVAE DEIKPYISRC SVCEAPAIAI AVHSQDVSIP HCPAGWRSLW 1630 1640 1650 1660 1670 1680 IGYSFLMHTA AGDEGGGQSL VSPGSCLEDF RATPFIECNG GRGTCHYYAN KYSFWLTTIP 1690 1700 1710 EQSFQGSPSA DTLKAGLIRT HISRCQVCMK NL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete primary structure of the alpha 2 chain of human type IV collagen and comparison with the alpha 1(IV) chain." Hostikka S.L., Tryggvason K. J. Biol. Chem. 263:19488-19493(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Human basement membrane collagen (type IV). The amino acid sequence of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain reveals deletions in the alpha 1(IV) chain." Brazel D., Pollner R., Oberbaeumer I., Kuehn K. Eur. J. Biochem. 172:35-42(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1042, VARIANTS LYS-517 AND ALA-683. Tissue: Placenta.
[4]	"The genes for the alpha 1(IV) and alpha 2(IV) chains of human basement membrane collagen type IV are arranged head-to-head and separated by a bidirectional promoter of unique structure." Poeschl E., Pollner R., Kuehn K. EMBO J. 7:2687-2695(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[5]	"The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region." Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K. J. Biol. Chem. 263:17217-17220(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[6]	"Identification of a novel sequence element in the common promoter region of human collagen type IV genes, involved in the regulation of divergent transcription." Fischer G., Schmidt C., Opitz J., Cully Z., Kuehn K., Poeschl E. Biochem. J. 292:687-695(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. Tissue: Skin.
[7]	"Partial structure of the human alpha 2(IV) collagen chain and chromosomal localization of the gene (COL4A2)." Killen P.D., Francomano C.A., Yamada Y., Modi W.S., O'Brien S.J. Hum. Genet. 77:318-324(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1040-1712. Tissue: Placenta.
[8]	"Nucleotide sequence coding for the human type IV collagen alpha 2 chain cDNA reveals extensive homology with the NC-1 domain of alpha 1 (IV) but not with the collagenous domain or 3'-untranslated region." Hostikka S.L., Kurkinen M., Tryggvason K. FEBS Lett. 216:281-286(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1254-1712, VARIANT ILE-1399.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1351-1712. Tissue: Eye.
[10]	"Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13." Griffin C.A., Emanuel B.S., Hansen J.R., Cavenee W.K., Myers J.C. Proc. Natl. Acad. Sci. U.S.A. 84:512-516(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1485.
[11]	"The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen." Siebold B., Deutzmann R., Kuehn K. Eur. J. Biochem. 176:617-624(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1480-1535; 1545-1614; 1617-1701 AND 1705-1712. Tissue: Placenta.
[12]	"Duplication of type IV collagen COOH-terminal repeats and species-specific expression of alpha 1(IV) and alpha 2(IV) collagen genes." Myers J.C., Howard P.S., Jelen A.M., Dion A.S., Macarak E.J. J. Biol. Chem. 262:9231-9238(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
[13]	"Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor growth." Kamphaus G.D., Colorado P.C., Panka D.J., Hopfer H., Ramchandran R., Torre A., Maeshima Y., Mier J.W., Sukhatme V.P., Kalluri R. J. Biol. Chem. 275:1209-1215(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712, FUNCTION.
[14]	Peng X., Sun W., Yin B., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
[15]	"Molecular cloning and homologous sequence analysis of canstatin cDNA derived from Chinese hepatocytes." Li Y., Huang G., Qian G. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712. Tissue: Hepatocyte.
[16]	"Cloning and expression of canstatin in yeast." Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Yang M., Tan H.H. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
[17]	"Canstatin inhibits Akt activation and induces Fas-dependent apoptosis in endothelial cells." Panka D.J., Mier J.W. J. Biol. Chem. 278:37632-37636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF CANSTATIN.
[18]	"Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with alphavbeta3 and alphavbeta5 integrins." Magnon C., Galaup A., Mullan B., Rouffiac V., Bouquet C., Bidart J.M., Griscelli F., Opolon P., Perricaudet M. Cancer Res. 65:4353-4361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF CANSTATIN.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link." Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R., Bourenkov G.P., Bartunik H.D., Bode W. Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1485-1712.
[21]	"Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families with keratoconus." Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A., Rydzanicz M., Bejjani B.A., Gajecka M. Mol. Vis. 17:827-843(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-192; LYS-517; ALA-683; ARG-701 AND SER-718.
[22]	"De novo and inherited mutations in COL4A2, encoding the type IV collagen alpha2 chain cause porencephaly." Yoneda Y., Haginoya K., Arai H., Yamaoka S., Tsurusaki Y., Doi H., Miyake N., Yokochi K., Osaka H., Kato M., Matsumoto N., Saitsu H. Am. J. Hum. Genet. 90:86-90(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS POREN2 GLU-1037 AND ASP-1152.
[23]	"COL4A2 mutations impair COL4A1 and COL4A2 secretion and cause hemorrhagic stroke." Jeanne M., Labelle-Dumais C., Jorgensen J., Kauffman W.B., Mancini G.M., Favor J., Valant V., Greenberg S.M., Rosand J., Gould D.B. Am. J. Hum. Genet. 90:91-101(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ICH, VARIANTS PHE-192; LYS-517; ALA-683; ARG-701; SER-718; GLN-1109; GLY-1123; LYS-1150; ILE-1399 AND THR-1690, CHARACTERIZATION OF VARIANTS GLY-1123; LYS-1150 AND THR-1690.
[24]	"COL4A2 mutation associated with familial porencephaly and small-vessel disease." Verbeek E., Meuwissen M.E., Verheijen F.W., Govaert P.P., Licht D.J., Kuo D.S., Poulton C.J., Schot R., Lequin M.H., Dudink J., Halley D.J., de Coo R.I., den Hollander J.C., Oegema R., Gould D.B., Mancini G.M. Eur. J. Hum. Genet. 20:844-851(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-1389.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL139385, AL159153, AL161773 Genomic DNA. Translation: CAI17005.2.
AL159153, AL139385, AL161773 Genomic DNA. Translation: CAH72050.2.
AL161773, AL139385, AL159153 Genomic DNA. Translation: CAH71366.2.
X05562 mRNA. Translation: CAA29076.1.
M36963 Genomic DNA. Translation: AAA53099.1.
J04217 Genomic DNA. Translation: AAA53097.1.
X12784 Genomic DNA. Translation: CAA31275.1.
M24766 mRNA. Translation: AAA52043.1.
X05610 mRNA. Translation: CAA29098.1.
BC080644 mRNA. Translation: AAH80644.1.
J02760 mRNA. Translation: AAA58422.1.
AF258350 mRNA. Translation: AAF72631.1.
AF400430 mRNA. Translation: AAK92479.1.
AY450357 mRNA. Translation: AAR20245.1.
AY455978 mRNA. Translation: AAR18250.1.

IPI

IPI00306322.

PIR

CGHU2B. A32024.

RefSeq

NP_001837.2. NM_001846.2.

UniGene

Hs.508716.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LI1	X-ray	1.90	C/F	1485-1712	[»]

ProteinModelPortal

P08572.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08572. 10 interactions.

MINT

MINT-1180068.

STRING

9606.ENSP00000353654.

PTM databases

PhosphoSite

P08572.

Polymorphism databases

DMDM

143811377.

Proteomic databases

PaxDb

P08572.

PeptideAtlas

P08572.

PRIDE

P08572.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360467; ENSP00000353654; ENSG00000134871.

GeneID

1284.

KEGG

hsa:1284.

UCSC

uc001vqx.3. human.

Organism-specific databases

CTD

1284.

GeneCards

GC13P110958.

H-InvDB

HIX0011454.

HGNC

HGNC:2203. COL4A2.

HPA

CAB010751.

MIM

120090. gene.
614483. phenotype.
614519. phenotype.

neXtProt

NX_P08572.

Orphanet

2940. Porencephaly.

PharmGKB

PA26718.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000085652.

HOVERGEN

HBG004933.

InParanoid

P08572.

KO

K06237.

OMA

TTIPEQN.

OrthoDB

EOG4XGZZF.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P08572.

Bgee

P08572.

CleanEx

HS_COL4A2.

Genevestigator

P08572.

GermOnline

ENSG00000134871. 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. 20 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

COL4A2. human.

EvolutionaryTrace

P08572.

GenomeRNAi

1284.

NextBio

5187.

PMAP-CutDB

P08572.

SOURCE

Search...

Entry information

Entry name

CO4A2_HUMAN

Accession

Primary (citable) accession number: P08572
Secondary accession number(s): Q14052 , Q548C3, Q5VZA9, Q66K23

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 147 of the entry and version 4 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.