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P08572 (CO4A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(IV) chain

Cleaved into the following chain:

  1. Canstatin
Gene names
Name:COL4A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1712 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. 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

Secretedextracellular spaceextracellular matrixbasement 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 processAngiogenesis
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCollagen
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

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: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

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-templated

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcollagen type IV trimer

Traceable author statement Ref.4Ref.3. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

   Molecular_functionextracellular matrix structural constituent

Traceable author statement Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COL4A1P024622EBI-2432506,EBI-2432478

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Propeptide26 – 183158N-terminal propeptide (7S domain)
PRO_0000005824
Chain184 – 17121529Collagen alpha-2(IV) chain
PRO_0000005825
Chain1486 – 1712227Canstatin
PRO_0000283775

Regions

Domain1489 – 1712224Collagen IV NC1
Region184 – 14841301Triple-helical region

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Ref.1
Disulfide bond1504 ↔ 1593
Disulfide bond1537 ↔ 1590
Disulfide bond1549 ↔ 1555
Disulfide bond1612 ↔ 1708
Disulfide bond1646 ↔ 1705
Disulfide bond1658 ↔ 1665

Natural variations

Natural variant1921V → F Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs62621885 [ dbSNP | Ensembl ].
VAR_067551
Natural variant5171R → K. Ref.3 Ref.21 Ref.23
Corresponds to variant rs7990383 [ dbSNP | Ensembl ].
VAR_048796
Natural variant6831G → A. Ref.3 Ref.21 Ref.23
Corresponds to variant rs3803230 [ dbSNP | Ensembl ].
VAR_048797
Natural variant7011K → R Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs78829338 [ dbSNP | Ensembl ].
VAR_067552
Natural variant7181P → S Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.21 Ref.23
Corresponds to variant rs9583500 [ dbSNP | Ensembl ].
VAR_067836
Natural variant10371G → E in POREN2. Ref.22
VAR_067837
Natural variant11091R → Q Polymorphism that does not affect COL4A2 and COL4A1 secretion. Ref.23
Corresponds to variant rs184812559 [ dbSNP | Ensembl ].
VAR_067553
Natural variant11231E → 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
Corresponds to variant rs117412802 [ dbSNP | Ensembl ].
VAR_067554
Natural variant11501Q → 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
Corresponds to variant rs62621875 [ dbSNP | Ensembl ].
VAR_067555
Natural variant11521G → D in POREN2; incomplete penetrance. Ref.22
VAR_067838
Natural variant13891G → 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 variant13991V → I. Ref.8 Ref.23
Corresponds to variant rs45520539 [ dbSNP | Ensembl ].
VAR_067557
Natural variant16901A → 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
Corresponds to variant rs201105747 [ dbSNP | Ensembl ].
VAR_067558

Experimental info

Sequence conflict4711R → P in CAA29076. Ref.3
Sequence conflict10411V → L in AAA52043. Ref.7
Sequence conflict14191M → I in CAA29098. Ref.8
Sequence conflict15751M → I in AAA58422. Ref.12
Sequence conflict16361G → V in AAA52043. Ref.7
Sequence conflict16631G → H AA sequence Ref.11
Sequence conflict17011H → G AA sequence Ref.11

Secondary structure

............................................... 1712
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08572 [UniParc].

Last modified April 3, 2007. Version 4.
Checksum: E0DABEEAB349D8AF

FASTA1,712167,553
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS41907.1.
PIRCGHU2B. A32024.
RefSeqNP_001837.2. NM_001846.2.
UniGeneHs.508716.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90C/F1485-1712[»]
ProteinModelPortalP08572.
SMRP08572. Positions 1488-1712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107681. 11 interactions.
IntActP08572. 19 interactions.
MINTMINT-1180068.
STRING9606.ENSP00000353654.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP08572.

Polymorphism databases

DMDM143811377.

Proteomic databases

MaxQBP08572.
PaxDbP08572.
PeptideAtlasP08572.
PRIDEP08572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360467; ENSP00000353654; ENSG00000134871.
GeneID1284.
KEGGhsa:1284.
UCSCuc001vqx.3. human.

Organism-specific databases

CTD1284.
GeneCardsGC13P110958.
H-InvDBHIX0011454.
HGNCHGNC:2203. COL4A2.
HPACAB010751.
HPA029118.
MIM120090. gene.
614483. phenotype.
614519. phenotype.
neXtProtNX_P08572.
Orphanet99810. Familial porencephaly.
PharmGKBPA26718.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085652.
HOVERGENHBG004933.
InParanoidP08572.
KOK06237.
OMAGFKGMAG.
OrthoDBEOG7RZ5P3.
PhylomeDBP08572.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP08572.
BgeeP08572.
CleanExHS_COL4A2.
GenevestigatorP08572.

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

Other

ChiTaRSCOL4A2. human.
EvolutionaryTraceP08572.
GeneWikiCOL4A2.
GenomeRNAi1284.
NextBio5187.
PMAP-CutDBP08572.
PROP08572.
SOURCESearch...

Entry information

Entry nameCO4A2_HUMAN
AccessionPrimary (citable) accession number: P08572
Secondary accession number(s): Q14052 expand/collapse secondary AC list , Q548C3, Q5VZA9, Q66K23
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 161 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 13

Human chromosome 13: entries, gene names and cross-references to MIM