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P08572

- CO4A2_HUMAN

UniProt

P08572 - CO4A2_HUMAN

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Protein

Collagen alpha-2(IV) chain

Gene
COL4A2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications
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.3 Publications

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. axon guidance Source: Reactome
  3. cellular response to transforming growth factor beta stimulus Source: Ensembl
  4. collagen catabolic process Source: Reactome
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: UniProtKB
  7. negative regulation of angiogenesis Source: UniProtKB
  8. transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_169262. Laminin interactions.
REACT_18312. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(IV) chain
Cleaved into the following chain:
Gene namesi
Name:COL4A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:2203. COL4A2.

Subcellular locationi

GO - Cellular componenti

  1. collagen type IV trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1037 – 10371G → E in POREN2. 1 Publication
VAR_067837
Natural varianti1152 – 11521G → D in POREN2; incomplete penetrance. 1 Publication
VAR_067838
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1123 – 11231E → 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. 1 Publication
Corresponds to variant rs117412802 [ dbSNP | Ensembl ].
VAR_067554
Natural varianti1150 – 11501Q → 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. 1 Publication
Corresponds to variant rs62621875 [ dbSNP | Ensembl ].
VAR_067555
Natural varianti1690 – 16901A → 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. 1 Publication
Corresponds to variant rs201105747 [ dbSNP | Ensembl ].
VAR_067558

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614483. phenotype.
614519. phenotype.
Orphaneti99810. Familial porencephaly.
PharmGKBiPA26718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Propeptidei26 – 183158N-terminal propeptide (7S domain)PRO_0000005824Add
BLAST
Chaini184 – 17121529Collagen alpha-2(IV) chainPRO_0000005825Add
BLAST
Chaini1486 – 1712227CanstatinPRO_0000283775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)1 Publication
Disulfide bondi1504 ↔ 1593
Disulfide bondi1537 ↔ 1590
Disulfide bondi1549 ↔ 1555
Disulfide bondi1612 ↔ 1708
Disulfide bondi1646 ↔ 1705
Disulfide bondi1658 ↔ 1665

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP08572.
PaxDbiP08572.
PeptideAtlasiP08572.
PRIDEiP08572.

PTM databases

PhosphoSiteiP08572.

Miscellaneous databases

PMAP-CutDBP08572.

Expressioni

Gene expression databases

ArrayExpressiP08572.
BgeeiP08572.
CleanExiHS_COL4A2.
GenevestigatoriP08572.

Organism-specific databases

HPAiCAB010751.
HPA029118.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
COL4A1P024622EBI-2432506,EBI-2432478

Protein-protein interaction databases

BioGridi107681. 11 interactions.
IntActiP08572. 19 interactions.
MINTiMINT-1180068.
STRINGi9606.ENSP00000353654.

Structurei

Secondary structure

1
1712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1490 – 14956
Beta strandi1497 – 15004
Beta strandi1509 – 152214
Beta strandi1525 – 15284
Helixi1534 – 15363
Beta strandi1537 – 15404
Beta strandi1546 – 15505
Turni1551 – 15533
Beta strandi1554 – 15585
Beta strandi1563 – 15686
Helixi1580 – 15867
Beta strandi1589 – 15979
Beta strandi1599 – 16035
Beta strandi1605 – 16084
Beta strandi1616 – 162914
Beta strandi1635 – 16373
Helixi1643 – 16453
Beta strandi1646 – 16494
Beta strandi1655 – 16595
Turni1660 – 16634
Beta strandi1664 – 16663
Beta strandi1672 – 16776
Beta strandi1680 – 16845
Beta strandi1691 – 16944
Helixi1699 – 17013
Beta strandi1704 – 17107

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90C/F1485-1712[»]
ProteinModelPortaliP08572.
SMRiP08572. Positions 1488-1712.

Miscellaneous databases

EvolutionaryTraceiP08572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1489 – 1712224Collagen IV NC1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 14841301Triple-helical regionAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the type IV collagen family.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiP08572.
KOiK06237.
OMAiGFKGMAG.
OrthoDBiEOG7RZ5P3.
PhylomeDBiP08572.
TreeFamiTF344135.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08572-1 [UniParc]FASTAAdd to Basket

« Hide

MGRDQRAVAG PALRRWLLLG TVTVGFLAQS VLAGVKKFDV PCGGRDCSGG     50
CQCYPEKGGR GQPGPVGPQG YNGPPGLQGF PGLQGRKGDK GERGAPGVTG 100
PKGDVGARGV SGFPGADGIP GHPGQGGPRG RPGYDGCNGT QGDSGPQGPP 150
GSEGFTGPPG PQGPKGQKGE PYALPKEERD RYRGEPGEPG LVGFQGPPGR 200
PGHVGQMGPV GAPGRPGPPG PPGPKGQQGN RGLGFYGVKG EKGDVGQPGP 250
NGIPSDTLHP IIAPTGVTFH PDQYKGEKGS EGEPGIRGIS LKGEEGIMGF 300
PGLRGYPGLS GEKGSPGQKG SRGLDGYQGP DGPRGPKGEA GDPGPPGLPA 350
YSPHPSLAKG ARGDPGFPGA QGEPGSQGEP GDPGLPGPPG LSIGDGDQRR 400
GLPGEMGPKG FIGDPGIPAL YGGPPGPDGK RGPPGPPGLP GPPGPDGFLF 450
GLKGAKGRAG FPGLPGSPGA RGPKGWKGDA GECRCTEGDE AIKGLPGLPG 500
PKGFAGINGE PGRKGDRGDP GQHGLPGFPG LKGVPGNIGA PGPKGAKGDS 550
RTITTKGERG QPGVPGVPGM KGDDGSPGRD GLDGFPGLPG PPGDGIKGPP 600
GDPGYPGIPG TKGTPGEMGP PGLGLPGLKG QRGFPGDAGL PGPPGFLGPP 650
GPAGTPGQID CDTDVKRAVG GDRQEAIQPG CIGGPKGLPG LPGPPGPTGA 700
KGLRGIPGFA GADGGPGPRG LPGDAGREGF PGPPGFIGPR GSKGAVGLPG 750
PDGSPGPIGL PGPDGPPGER GLPGEVLGAQ PGPRGDAGVP GQPGLKGLPG 800
DRGPPGFRGS QGMPGMPGLK GQPGLPGPSG QPGLYGPPGL HGFPGAPGQE 850
GPLGLPGIPG REGLPGDRGD PGDTGAPGPV GMKGLSGDRG DAGFTGEQGH 900
PGSPGFKGID GMPGTPGLKG DRGSPGMDGF QGMPGLKGRP GFPGSKGEAG 950
FFGIPGLKGL AGEPGFKGSR GDPGPPGPPP VILPGMKDIK GEKGDEGPMG 1000
LKGYLGAKGI QGMPGIPGLS GIPGLPGRPG HIKGVKGDIG VPGIPGLPGF 1050
PGVAGPPGIT GFPGFIGSRG DKGAPGRAGL YGEIGATGDF GDIGDTINLP 1100
GRPGLKGERG TTGIPGLKGF FGEKGTEGDI GFPGITGVTG VQGPPGLKGQ 1150
TGFPGLTGPP GSQGELGRIG LPGGKGDDGW PGAPGLPGFP GLRGIRGLHG 1200
LPGTKGFPGS PGSDIHGDPG FPGPPGERGD PGEANTLPGP VGVPGQKGDQ 1250
GAPGERGPPG SPGLQGFPGI TPPSNISGAP GDKGAPGIFG LKGYRGPPGP 1300
PGSAALPGSK GDTGNPGAPG TPGTKGWAGD SGPQGRPGVF GLPGEKGPRG 1350
EQGFMGNTGP TGAVGDRGPK GPKGDPGFPG APGTVGAPGI AGIPQKIAVQ 1400
PGTVGPQGRR GPPGAPGEMG PQGPPGEPGF RGAPGKAGPQ GRGGVSAVPG 1450
FRGDEGPIGH QGPIGQEGAP GRPGSPGLPG MPGRSVSIGY LLVKHSQTDQ 1500
EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN 1550
PGDVCYYASR NDKSYWLSTT APLPMMPVAE DEIKPYISRC SVCEAPAIAI 1600
AVHSQDVSIP HCPAGWRSLW IGYSFLMHTA AGDEGGGQSL VSPGSCLEDF 1650
RATPFIECNG GRGTCHYYAN KYSFWLTTIP EQSFQGSPSA DTLKAGLIRT 1700
HISRCQVCMK NL 1712
Length:1,712
Mass (Da):167,553
Last modified:April 3, 2007 - v4
Checksum:iE0DABEEAB349D8AF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti192 – 1921V → F Polymorphism that does not affect COL4A2 and COL4A1 secretion. 2 Publications
Corresponds to variant rs62621885 [ dbSNP | Ensembl ].
VAR_067551
Natural varianti517 – 5171R → K.3 Publications
Corresponds to variant rs7990383 [ dbSNP | Ensembl ].
VAR_048796
Natural varianti683 – 6831G → A.3 Publications
Corresponds to variant rs3803230 [ dbSNP | Ensembl ].
VAR_048797
Natural varianti701 – 7011K → R Polymorphism that does not affect COL4A2 and COL4A1 secretion. 2 Publications
Corresponds to variant rs78829338 [ dbSNP | Ensembl ].
VAR_067552
Natural varianti718 – 7181P → S Polymorphism that does not affect COL4A2 and COL4A1 secretion. 2 Publications
Corresponds to variant rs9583500 [ dbSNP | Ensembl ].
VAR_067836
Natural varianti1037 – 10371G → E in POREN2. 1 Publication
VAR_067837
Natural varianti1109 – 11091R → Q Polymorphism that does not affect COL4A2 and COL4A1 secretion. 1 Publication
Corresponds to variant rs184812559 [ dbSNP | Ensembl ].
VAR_067553
Natural varianti1123 – 11231E → 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. 1 Publication
Corresponds to variant rs117412802 [ dbSNP | Ensembl ].
VAR_067554
Natural varianti1150 – 11501Q → 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. 1 Publication
Corresponds to variant rs62621875 [ dbSNP | Ensembl ].
VAR_067555
Natural varianti1152 – 11521G → D in POREN2; incomplete penetrance. 1 Publication
VAR_067838
Natural varianti1389 – 13891G → 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. 1 Publication
VAR_067556
Natural varianti1399 – 13991V → I.2 Publications
Corresponds to variant rs45520539 [ dbSNP | Ensembl ].
VAR_067557
Natural varianti1690 – 16901A → 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. 1 Publication
Corresponds to variant rs201105747 [ dbSNP | Ensembl ].
VAR_067558

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti471 – 4711R → P in CAA29076. 1 Publication
Sequence conflicti1041 – 10411V → L in AAA52043. 1 Publication
Sequence conflicti1419 – 14191M → I in CAA29098. 1 Publication
Sequence conflicti1575 – 15751M → I in AAA58422. 1 Publication
Sequence conflicti1636 – 16361G → V in AAA52043. 1 Publication
Sequence conflicti1663 – 16631G → H AA sequence 1 Publication
Sequence conflicti1701 – 17011H → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41907.1.
PIRiA32024. CGHU2B.
RefSeqiNP_001837.2. NM_001846.2.
UniGeneiHs.508716.

Genome annotation databases

EnsembliENST00000360467; ENSP00000353654; ENSG00000134871.
GeneIDi1284.
KEGGihsa:1284.
UCSCiuc001vqx.3. human.

Polymorphism databases

DMDMi143811377.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41907.1.
PIRi A32024. CGHU2B.
RefSeqi NP_001837.2. NM_001846.2.
UniGenei Hs.508716.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LI1 X-ray 1.90 C/F 1485-1712 [» ]
ProteinModelPortali P08572.
SMRi P08572. Positions 1488-1712.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107681. 11 interactions.
IntActi P08572. 19 interactions.
MINTi MINT-1180068.
STRINGi 9606.ENSP00000353654.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P08572.

Polymorphism databases

DMDMi 143811377.

Proteomic databases

MaxQBi P08572.
PaxDbi P08572.
PeptideAtlasi P08572.
PRIDEi P08572.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360467 ; ENSP00000353654 ; ENSG00000134871 .
GeneIDi 1284.
KEGGi hsa:1284.
UCSCi uc001vqx.3. human.

Organism-specific databases

CTDi 1284.
GeneCardsi GC13P110958.
H-InvDB HIX0011454.
HGNCi HGNC:2203. COL4A2.
HPAi CAB010751.
HPA029118.
MIMi 120090. gene.
614483. phenotype.
614519. phenotype.
neXtProti NX_P08572.
Orphaneti 99810. Familial porencephaly.
PharmGKBi PA26718.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085652.
HOVERGENi HBG004933.
InParanoidi P08572.
KOi K06237.
OMAi GFKGMAG.
OrthoDBi EOG7RZ5P3.
PhylomeDBi P08572.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_169262. Laminin interactions.
REACT_18312. NCAM1 interactions.

Miscellaneous databases

ChiTaRSi COL4A2. human.
EvolutionaryTracei P08572.
GeneWikii COL4A2.
GenomeRNAii 1284.
NextBioi 5187.
PMAP-CutDB P08572.
PROi P08572.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08572.
Bgeei P08572.
CleanExi HS_COL4A2.
Genevestigatori P08572.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: VARIANT ARG-1389.

Entry informationi

Entry nameiCO4A2_HUMAN
AccessioniPrimary (citable) accession number: P08572
Secondary accession number(s): Q14052
, Q548C3, Q5VZA9, Q66K23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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