Reviewed, UniProtKB/Swiss-Prot P08572 (CO4A2_HUMAN)

Names and origin

Protein names

Recommended name:
    Collagen alpha-2(IV) chain
Cleaved into the following chain:
    1- Recommended name:
            Canstatin

Gene names

Name:

COL4A2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Potently inhibits angiogenesis and tumor growth. Ref.13
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.
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
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	extracellular matrix organization Ref.6 Non-traceable author statement. Source: UniProtKB negative regulation of angiogenesis Ref.13 Inferred from direct assay. Source: UniProtKB
Cellular component	collagen type IV Ref.3 Ref.4 Traceable author statement. Source: UniProtKB
Molecular function	extracellular matrix structural constituent Ref.6 Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KLK6	Q92876	1	EBI-2432506,EBI-2432309

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

517

1

R → K: dbSNP rs7990383. Ref.3

VAR_048796

Natural variant

683

1

G → A: dbSNP rs3803230. Ref.3

VAR_048797

Natural variant

718

1

P → S: dbSNP rs9583500.

VAR_048798

Experimental info

Sequence conflict

471

1

R → P in CAA29076. Ref.3

Sequence conflict

1041

1

V → L in AAA52043. Ref.7

Sequence conflict

1399

1

V → I in CAA29098. Ref.8

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)
	P08572-1 [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: 3198637] [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: 15057823] [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: 3345760] [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: 2846280] [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: 3182844] [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: 8317999] [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: 3692475] [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: 3582677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1254-1712.
[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: 15489334] [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: 3025878] [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: 2844531] [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: 2439508] [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: 10625665] [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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"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: 12011424] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1485-1712.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.508716

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P08572. 2 interactions.

STRING

P08572.

PTM databases

PhosphoSite

P08572.

Proteomic databases

PeptideAtlas

P08572.

PRIDE

P08572.

Genome annotation databases

Ensembl

ENST00000257309; ENSP00000257309; ENSG00000134871; Homo sapiens. [Genome view]
ENST00000298721; ENSP00000298721; ENSG00000134871; Homo sapiens. [Genome view]
ENST00000360467; ENSP00000353654; ENSG00000134871; Homo sapiens. [Genome view]
ENST00000400163; ENSP00000383027; ENSG00000134871; Homo sapiens. [Genome view]

GeneID

1284.

KEGG

hsa:1284.

UCSC

uc001vqx.1. human.

Organism-specific databases

CTD

1284.

GeneCards

GC13P109757.

HGNC

HGNC:2203. COL4A2.

HPA

CAB010751.

MIM

120090. gene.

PharmGKB

PA26718.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P08572.

HOVERGEN

P08572.

OMA

GWVGDPG.

Enzyme and pathway databases

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P08572.

Bgee

P08572.

CleanEx

HS_COL4A2.

Genevestigator

P08572.

GermOnline

ENSG00000134871. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR001442. Procollagn4_C.
[Graphical view]

Gene3D

G3DSA:2.170.240.10. Procollagn4_C. 1 hit.

Pfam

PF01413. C4. 2 hits.
PF01391. Collagen. 24 hits.
[Graphical view]

ProDom

PD000007. Clg_helix. 11 hits.
PD003923. Procollagn4_C. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00111. C4. 2 hits.
[Graphical view]

PROSITE

PS51403. NC1_IV. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	November 3, 2009
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.