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P08122

- CO4A2_MOUSE

UniProt

P08122 - CO4A2_MOUSE

Protein

Collagen alpha-2(IV) chain

Gene

Col4a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (20 Feb 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.1 Publication
    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 By similarity.By similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    3. negative regulation of angiogenesis Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.
    REACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_202342. Laminin interactions.
    REACT_206066. Extracellular matrix organization.
    REACT_209041. Scavenging by Class A Receptors.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(IV) chain
    Cleaved into the following chain:
    Gene namesi
    Name:Col4a2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:88455. Col4a2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane PROSITE-ProRule annotation

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. collagen type IV trimer Source: MGI
    3. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Propeptidei26 – 183158N-terminal propeptide (7S domain)PRO_0000005826Add
    BLAST
    Chaini184 – 17071524Collagen alpha-2(IV) chainPRO_0000005827Add
    BLAST
    Chaini1481 – 1707227CanstatinPRO_0000390487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1270 – 12701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1499 ↔ 1588PROSITE-ProRule annotation
    Disulfide bondi1532 ↔ 1585PROSITE-ProRule annotation
    Disulfide bondi1544 ↔ 1550PROSITE-ProRule annotation
    Disulfide bondi1607 ↔ 1703PROSITE-ProRule annotation
    Disulfide bondi1641 ↔ 1700PROSITE-ProRule annotation
    Disulfide bondi1653 ↔ 1660PROSITE-ProRule annotation

    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.
    Proteolytic processing produces the C-terminal NC1 peptide, canstatin.By similarity
    The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP08122.
    PaxDbiP08122.
    PRIDEiP08122.

    PTM databases

    PhosphoSiteiP08122.

    Expressioni

    Gene expression databases

    ArrayExpressiP08122.
    BgeeiP08122.
    CleanExiMM_COL4A2.
    GenevestigatoriP08122.

    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.

    Protein-protein interaction databases

    BioGridi198817. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP08122.
    SMRiP08122. Positions 1482-1706.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1484 – 1707224Collagen IV NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 14791296Triple-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.
    GeneTreeiENSGT00730000110538.
    HOVERGENiHBG004933.
    InParanoidiP08122.
    KOiK06237.
    OMAiGFKGMAG.
    OrthoDBiEOG7RZ5P3.
    PhylomeDBiP08122.
    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. 19 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.

    P08122-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRVRFKASG PPLRGWLLLA TVTVGLLAQS VLGGVKKLDV PCGGRDCSGG     50
    CQCYPEKGAR GQPGAVGPQG YNGPPGLQGF PGLQGRKGDK GERGVPGPTG 100
    PKGDVGARGV SGFPGADGIP GHPGQGGPRG RPGYDGCNGT RGDAGPQGPS 150
    GSGGFPGLPG PQGPKGQKGE PYALSKEDRD KYRGEPGEPG LVGYQGPPGR 200
    PGPIGQMGPM GAPGRPGPPG PPGPKGQPGN RGLGFYGQKG EKGDIGQPGP 250
    NGIPSDITLV GPTTSTIHPD LYKGEKGDEG EQGIPGVISK GEEGIMGFPG 300
    IRGFPGLDGE KGVVGQKGSR GLDGFQGPSG PRGPKGERGE QGPPGPSVYS 350
    PHPSLAKGAR GDPGFQGAHG EPGSRGEPGE PGTAGPPGPS VGDEDSMRGL 400
    PGEMGPKGFS GEPGSPARYL GPPGADGRPG PQGVPGPAGP PGPDGFLFGL 450
    KGSEGRVGYP GPSGFPGTRG QKGWKGEAGD CQCGQVIGGL PGLPGPKGFP 500
    GVNGELGKKG DQGDPGLHGI PGFPGFKGAP GVAGAPGPKG IKGDSRTITT 550
    KGERGQPGIP GVHGMKGDDG VPGRDGLDGF PGLPGPPGDG IKGPPGDAGL 600
    PGVPGTKGFP GDIGPPGQGL PGPKGERGFP GDAGLPGPPG FPGPPGPPGT 650
    PGQRDCDTGV KRPIGGGQQV VVQPGCIEGP TGSPGQPGPP GPTGAKGVRG 700
    MPGFPGASGE QGLKGFPGDP GREGFPGPPG FMGPRGSKGT TGLPGPDGPP 750
    GPIGLPGPAG PPGDRGIPGE VLGAQPGTRG DAGLPGQPGL KGLPGETGAP 800
    GFRGSQGMPG MPGLKGQPGF PGPSGQPGQS GPPGQHGFPG TPGREGPLGQ 850
    PGSPGLGGLP GDRGEPGDPG VPGPVGMKGL SGDRGDAGMS GERGHPGSPG 900
    FKGMAGMPGI PGQKGDRGSP GMDGFQGMLG LKGRQGFPGT KGEAGFFGVP 950
    GLKGLPGEPG VKGNRGDRGP PGPPPLILPG MKDIKGEKGD EGPMGLKGYL 1000
    GLKGIQGMPG VPGVSGFPGL PGRPGFIKGV KGDIGVPGTP GLPGFPGVSG 1050
    PPGITGFPGF TGSRGEKGTP GVAGVFGETG PTGDFGDIGD TVDLPGSPGL 1100
    KGERGITGIP GLKGFFGEKG AAGDIGFPGI TGMAGAQGSP GLKGQTGFPG 1150
    LTGLQGPQGE PGRIGIPGDK GDFGWPGVPG LPGFPGIRGI SGLHGLPGTK 1200
    GFPGSPGVDA HGDPGFPGPT GDRGDRGEAN TLPGPVGVPG QKGERGTPGE 1250
    RGPAGSPGLQ GFPGISPPSN ISGSPGDVGA PGIFGLQGYQ GPPGPPGPNA 1300
    LPGIKGDEGS SGAAGFPGQK GWVGDPGPQG QPGVLGLPGE KGPKGEQGFM 1350
    GNTGPSGAVG DRGPKGPKGD QGFPGAPGSM GSPGIPGIPQ KIAVQPGTLG 1400
    PQGRRGLPGA LGEIGPQGPP GDPGFRGAPG KAGPQGRGGV SAVPGFRGDQ 1450
    GPMGHQGPVG QEGEPGRPGS PGLPGMPGRS VSIGYLLVKH SQTDQEPMCP 1500
    VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG SCLARFSTMP FLYCNPGDVC 1550
    YYASRNDKSY WLSTTAPLPM MPVAEEEIKP YISRCSVCEA PAVAIAVHSQ 1600
    DTSIPHCPAG WRSLWIGYSF LMHTAAGDEG GGQSLVSPGS CLEDFRATPF 1650
    IECNGGRGTC HYFANKYSFW LTTIPEQNFQ STPSADTLKA GLIRTHISRC 1700
    QVCMKNL 1707
    Length:1,707
    Mass (Da):167,325
    Last modified:February 20, 2007 - v4
    Checksum:i67CB3E3CB2A5B1F6
    GO

    Sequence cautioni

    The sequence AAH80789.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 277.
    The sequence AAI07686.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 277.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2751E → K in AAH80789. (PubMed:15489334)Curated
    Sequence conflicti626 – 6261E → R in AAA50293. (PubMed:2703491)Curated
    Sequence conflicti837 – 8371G → A in AAA50293. (PubMed:2703491)Curated
    Sequence conflicti1051 – 10511P → R in CAA27998. (PubMed:3758345)Curated
    Sequence conflicti1097 – 10971S → G in CAA26655. (PubMed:3839908)Curated
    Sequence conflicti1171 – 11711G → S in CAA27998. (PubMed:3758345)Curated
    Sequence conflicti1179 – 11791P → R in CAA27998. (PubMed:3758345)Curated
    Sequence conflicti1241 – 12411Q → E in CAA27998. (PubMed:3758345)Curated
    Sequence conflicti1328 – 13281P → A in CAA27998. (PubMed:3758345)Curated
    Sequence conflicti1573 – 15731V → L in CAA28308. (PubMed:3780963)Curated
    Sequence conflicti1583 – 15831S → I in AAR89902. (PubMed:15592653)Curated
    Sequence conflicti1583 – 15831S → I in AAQ83370. (PubMed:15592653)Curated
    Sequence conflicti1623 – 16231H → Y in AAA50293. (PubMed:2703491)Curated
    Sequence conflicti1623 – 16231H → Y in AAA37341. (PubMed:3597383)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04695 mRNA. Translation: AAA50293.1.
    AK053858 mRNA. Translation: BAC35559.1.
    AK075619 mRNA. Translation: BAC35863.1.
    AK164096 mRNA. Translation: BAE37626.1.
    BC013560 mRNA. Translation: AAH13560.2.
    BC080789 mRNA. Translation: AAH80789.1. Sequence problems.
    BC107685 mRNA. Translation: AAI07686.1. Sequence problems.
    M23334, M23333 Genomic DNA. Translation: AAA51626.1.
    J04448 Genomic DNA. Translation: AAA37438.1.
    X02896 mRNA. Translation: CAA26655.1.
    X02897 Genomic DNA. Translation: CAB51614.1.
    X02898 Genomic DNA. Translation: CAA26657.1.
    X02899 Genomic DNA. Translation: CAA26658.1.
    X04410 mRNA. Translation: CAA27998.1.
    X04647 mRNA. Translation: CAA28308.1.
    M15833 mRNA. Translation: AAA37341.1.
    AY375463 mRNA. Translation: AAQ83370.1.
    AY502946 mRNA. Translation: AAR89901.1.
    AY502947 mRNA. Translation: AAR89902.1.
    CCDSiCCDS40220.1.
    PIRiA33526.
    RefSeqiNP_034062.3. NM_009932.3.
    UniGeneiMm.181021.

    Genome annotation databases

    EnsembliENSMUST00000033899; ENSMUSP00000033899; ENSMUSG00000031503.
    GeneIDi12827.
    KEGGimmu:12827.
    UCSCiuc009kvc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04695 mRNA. Translation: AAA50293.1 .
    AK053858 mRNA. Translation: BAC35559.1 .
    AK075619 mRNA. Translation: BAC35863.1 .
    AK164096 mRNA. Translation: BAE37626.1 .
    BC013560 mRNA. Translation: AAH13560.2 .
    BC080789 mRNA. Translation: AAH80789.1 . Sequence problems.
    BC107685 mRNA. Translation: AAI07686.1 . Sequence problems.
    M23334 , M23333 Genomic DNA. Translation: AAA51626.1 .
    J04448 Genomic DNA. Translation: AAA37438.1 .
    X02896 mRNA. Translation: CAA26655.1 .
    X02897 Genomic DNA. Translation: CAB51614.1 .
    X02898 Genomic DNA. Translation: CAA26657.1 .
    X02899 Genomic DNA. Translation: CAA26658.1 .
    X04410 mRNA. Translation: CAA27998.1 .
    X04647 mRNA. Translation: CAA28308.1 .
    M15833 mRNA. Translation: AAA37341.1 .
    AY375463 mRNA. Translation: AAQ83370.1 .
    AY502946 mRNA. Translation: AAR89901.1 .
    AY502947 mRNA. Translation: AAR89902.1 .
    CCDSi CCDS40220.1.
    PIRi A33526.
    RefSeqi NP_034062.3. NM_009932.3.
    UniGenei Mm.181021.

    3D structure databases

    ProteinModelPortali P08122.
    SMRi P08122. Positions 1482-1706.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198817. 1 interaction.

    PTM databases

    PhosphoSitei P08122.

    Proteomic databases

    MaxQBi P08122.
    PaxDbi P08122.
    PRIDEi P08122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033899 ; ENSMUSP00000033899 ; ENSMUSG00000031503 .
    GeneIDi 12827.
    KEGGi mmu:12827.
    UCSCi uc009kvc.2. mouse.

    Organism-specific databases

    CTDi 1284.
    MGIi MGI:88455. Col4a2.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00730000110538.
    HOVERGENi HBG004933.
    InParanoidi P08122.
    KOi K06237.
    OMAi GFKGMAG.
    OrthoDBi EOG7RZ5P3.
    PhylomeDBi P08122.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.
    REACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_202342. Laminin interactions.
    REACT_206066. Extracellular matrix organization.
    REACT_209041. Scavenging by Class A Receptors.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi COL4A2. mouse.
    NextBioi 282318.
    PROi P08122.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08122.
    Bgeei P08122.
    CleanExi MM_COL4A2.
    Genevestigatori P08122.

    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. 19 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 mouse alpha 2(IV) collagen. Alignment with mouse alpha 1(IV) collagen."
      Saus J., Quinones S., Mackrell A., Blumberg B., Muthukumaran G., Pihlajaniemi T., Kurkinen M.
      J. Biol. Chem. 264:6318-6324(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-538 AND 1649-1707.
      Strain: C57BL/6J.
      Tissue: Eye and Spinal cord.
    3. "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 1-276 AND 1339-1707.
      Tissue: Mammary gland.
    4. "Alpha 1(IV) and alpha 2(IV) collagen genes are regulated by a bidirectional promoter and a shared enhancer."
      Burbelo P.D., Martin G.R., Yamada Y.
      Proc. Natl. Acad. Sci. U.S.A. 85:9679-9682(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-60.
    5. "Head-to-head arrangement of murine type IV collagen genes."
      Kaytes P., Wood L., Theriault N., Kurkinen M., Vogeli G.
      J. Biol. Chem. 263:19274-19277(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    6. "Characterization of 64-, 123- and 182-base-pair exons in the mouse alpha 2(IV) collagen gene."
      Kurkinen M., Bernard M.P., Barlow D.P., Chow L.T.
      Nature 317:177-179(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 964-1003; 1005-1085 AND 1087-1109.
    7. "Structure of mouse type IV collagen. Amino-acid sequence of the C-terminal 511-residue-long triple-helical segment of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain."
      Schwarz U., Schuppan D., Oberbaeumer I., Glanville R.W., Deutzmann R., Timpl R., Kuehn K.
      Eur. J. Biochem. 157:49-56(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 970-1480.
    8. "Proposed alignment of helical interruptions in the two subunits of the basement membrane (type IV) collagen."
      Vogeli G., Horn E., Carter J., Kaytes P.S.
      FEBS Lett. 206:29-32(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1041-1489.
    9. "cDNA and protein sequence of the NC1 domain of the alpha 2-chain of collagen IV and its comparison with alpha 1(IV)."
      Schwarz-Magdolen U., Oberbaeumer I., Kuehn K.
      FEBS Lett. 208:203-207(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1480-1707.
    10. "Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen."
      Kurkinen M., Condon M.R., Blumberg B., Barlow D., Quinones S., Saus J., Pihlajaniemi T.
      J. Biol. Chem. 262:8496-8499(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707, FUNCTION OF CANSTATIN.
    11. "Recombinant mouse canstatin inhibits chicken embryo chorioallantoic membrane angiogenesis and endothelial cell proliferation."
      Hou W.H., Wang T.Y., Yuan B.M., Chai Y.R., Jia Y.L., Tian F., Wang J.M., Xue L.X.
      Acta Biochim. Biophys. Sin. 36:845-850(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707.
      Strain: BALB/c.

    Entry informationi

    Entry nameiCO4A2_MOUSE
    AccessioniPrimary (citable) accession number: P08122
    Secondary accession number(s): Q3B7C2
    , Q3TPV9, Q61375, Q66JS5, Q6RCT6, Q6RCT7, Q6U9X1, Q8BPI9, Q8BPK3, Q91VI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3