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P08572

- CO4A2_HUMAN

UniProt

P08572 - CO4A2_HUMAN

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
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 4 (03 Apr 2007)
      Previous versions | rss
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    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.
    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.

    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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08572.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1489 – 1712224Collagen IV NC1PROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti471 – 4711R → P in CAA29076. (PubMed:3345760)Curated
    Sequence conflicti1041 – 10411V → L in AAA52043. (PubMed:3692475)Curated
    Sequence conflicti1419 – 14191M → I in CAA29098. (PubMed:3582677)Curated
    Sequence conflicti1575 – 15751M → I in AAA58422. (PubMed:2439508)Curated
    Sequence conflicti1636 – 16361G → V in AAA52043. (PubMed:3692475)Curated
    Sequence conflicti1663 – 16631G → H AA sequence (PubMed:2844531)Curated
    Sequence conflicti1701 – 17011H → G AA sequence (PubMed:2844531)Curated

    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 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

    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: October 1, 2014
    This is version 163 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