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Q3U962

- CO5A2_MOUSE

UniProt

Q3U962 - CO5A2_MOUSE

Protein

Collagen alpha-2(V) chain

Gene

Col5a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices.By similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1312 – 13121CalciumBy similarity
    Metal bindingi1314 – 13141CalciumBy similarity
    Metal bindingi1315 – 13151Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1320 – 13201CalciumBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. SMAD binding Source: MGI

    GO - Biological processi

    1. cellular response to amino acid stimulus Source: MGI
    2. collagen fibril organization Source: UniProtKB
    3. eye morphogenesis Source: Ensembl
    4. skeletal system development Source: MGI
    5. skin development Source: UniProtKB

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(V) chain
    Gene namesi
    Name:Col5a2Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:88458. Col5a2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen trimer Source: MGI
    2. collagen type V trimer Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 12271201Collagen alpha-2(V) chainSequence AnalysisPRO_0000283768Add
    BLAST
    Propeptidei1228 – 1497270C-terminal propeptideSequence AnalysisPRO_0000283769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei288 – 28814-hydroxyprolineBy similarity
    Modified residuei291 – 29114-hydroxyprolineBy similarity
    Modified residuei294 – 29414-hydroxyprolineBy similarity
    Modified residuei609 – 60914-hydroxyprolineBy similarity
    Modified residuei615 – 61514-hydroxyprolineBy similarity
    Glycosylationi1260 – 12601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1294 ↔ 1326PROSITE-ProRule annotation
    Disulfide bondi1334 ↔ 1495PROSITE-ProRule annotation
    Glycosylationi1398 – 13981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1403 ↔ 1448PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on prolines by LEPREL1.
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiQ3U962.
    PRIDEiQ3U962.

    PTM databases

    PhosphoSiteiQ3U962.

    Expressioni

    Developmental stagei

    Expressed in embryos from 9 days of gestation onward. In 12.5 dpc embryos, low and diffuse level of expression was observed in the peritoneal membranes and intestinal and craniofacial mesenchymes. By 16.5 dpc, expression is higher and exhibits a more restricted accumulation in primary ossified regions, perichondrium, joints, tendon, atrioventricular valve of heart, and in selected portions of the head.1 Publication

    Gene expression databases

    BgeeiQ3U962.
    CleanExiMM_COL5A2.
    GenevestigatoriQ3U962.

    Interactioni

    Subunit structurei

    Trimers of two alpha 1(V) and one alpha 2(V) chains expressed in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains with a more limited distribution of expression.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000083620.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3U962.
    SMRiQ3U962. Positions 1282-1497.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 9659VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1264 – 1497234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi141 – 1433Cell attachment siteSequence Analysis
    Motifi504 – 5063Cell attachment siteSequence Analysis
    Motifi942 – 9443Cell attachment siteSequence Analysis
    Motifi1065 – 10673Cell attachment siteSequence Analysis
    Motifi1068 – 10703Cell attachment siteSequence Analysis
    Motifi1125 – 11273Cell attachment siteSequence Analysis
    Motifi1134 – 11363Cell attachment siteSequence Analysis

    Domaini

    The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.By similarity

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00740000114967.
    HOVERGENiHBG004933.
    InParanoidiQ3U962.
    KOiK06236.
    OMAiIGIRGQP.
    OrthoDBiEOG7TJ3HH.
    PhylomeDBiQ3U962.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    PROSITEiPS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q3U962-1 [UniParc]FASTAAdd to Basket

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    MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR     50
    DIWKPSPCQI CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG 100
    GDTSFGRGRK GQKGEPGLVP VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP 150
    GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP GPDGMSRPFS AQMAGLDEKS 200
    GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP GEPGPMGPIG 250
    SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR 300
    GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA 350
    PGKRGAHGMP GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG 400
    QRGETGPPGP AGSQGLPGAV GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP 450
    GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK GEPGPHGIQG PIGPPGEEGK 500
    RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ GERGPVGSSG 550
    PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP 600
    GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP 650
    SGPVGPPGLA GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG 700
    AVGPLGPRGE RGNPGERGEP GITGLPGEKG MAGGHGPDGP KGNPGPTGTI 750
    GDTGPPGLQG MPGERGIAGT PGPKGDRGGI GEKGAEGTAG NDGARGLPGP 800
    LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT GAVGFAGPQG 850
    PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ 900
    GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR 950
    VGDRGPAGPP GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG 1000
    ERGMPGLPGP AGTPGKVGPT GATGDKGPPG PVGPPGSNGP VGEPGPEGPA 1050
    GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ GAPGTPGPVG APGDAGQRGE 1100
    PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK GHRGFTGLQG 1150
    LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR 1200
    GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT 1250
    EDQAAPDDTN KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC 1300
    HPTKQSGEYW IDPNQGSAED AIKVYCNMET GETCISANPA SVPRKTWWAS 1350
    KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT AITQMTFLRL LSKEASQNLT 1400
    YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR YTVLQDTCSK 1450
    RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM 1497
    Length:1,497
    Mass (Da):145,018
    Last modified:October 11, 2005 - v1
    Checksum:iCAAE15514984DB41
    GO

    Sequence cautioni

    The sequence BAE23896.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201Y → D in BAE23896. (PubMed:16141072)Curated
    Sequence conflicti88 – 881T → P in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti160 – 1601G → R in BAE27850. (PubMed:16141072)Curated
    Sequence conflicti164 – 1641V → M in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti222 – 2221Q → V in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti231 – 2311V → A in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti387 – 3871A → R in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti390 – 3901T → H in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti428 – 4281A → R in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti431 – 4311P → A in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti614 – 6141L → V in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti614 – 6141L → V in AAH55077. (PubMed:15489334)Curated
    Sequence conflicti666 – 6661Q → A in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti809 – 8135PTGEK → LLGAP in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti851 – 8511P → S in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti1001 – 10022ER → VT in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti1013 – 10131T → A in AAH55077. (PubMed:15489334)Curated
    Sequence conflicti1063 – 10631G → V in BAE21154. (PubMed:16141072)Curated
    Sequence conflicti1181 – 11811P → S in AAA37440. (PubMed:1297453)Curated
    Sequence conflicti1337 – 13371A → T in AAH55077. (PubMed:15489334)Curated
    Sequence conflicti1388 – 13881L → F in AAA37440. (PubMed:1297453)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02918 mRNA. Translation: AAA37440.1.
    AK132413 mRNA. Translation: BAE21154.1.
    AK139130 mRNA. Translation: BAE23896.1. Different initiation.
    AK147220 mRNA. Translation: BAE27775.1.
    AK147328 mRNA. Translation: BAE27850.1.
    AK151929 mRNA. Translation: BAE30805.1.
    AK160008 mRNA. Translation: BAE35556.1.
    BC043696 mRNA. Translation: AAH43696.1.
    BC055077 mRNA. Translation: AAH55077.1.
    CCDSiCCDS35555.1.
    PIRiI49607.
    RefSeqiNP_031763.2. NM_007737.2.
    UniGeneiMm.10299.

    Genome annotation databases

    EnsembliENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
    GeneIDi12832.
    KEGGimmu:12832.
    UCSCiuc007awr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02918 mRNA. Translation: AAA37440.1 .
    AK132413 mRNA. Translation: BAE21154.1 .
    AK139130 mRNA. Translation: BAE23896.1 . Different initiation.
    AK147220 mRNA. Translation: BAE27775.1 .
    AK147328 mRNA. Translation: BAE27850.1 .
    AK151929 mRNA. Translation: BAE30805.1 .
    AK160008 mRNA. Translation: BAE35556.1 .
    BC043696 mRNA. Translation: AAH43696.1 .
    BC055077 mRNA. Translation: AAH55077.1 .
    CCDSi CCDS35555.1.
    PIRi I49607.
    RefSeqi NP_031763.2. NM_007737.2.
    UniGenei Mm.10299.

    3D structure databases

    ProteinModelPortali Q3U962.
    SMRi Q3U962. Positions 1282-1497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000083620.

    PTM databases

    PhosphoSitei Q3U962.

    Proteomic databases

    PaxDbi Q3U962.
    PRIDEi Q3U962.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086430 ; ENSMUSP00000083620 ; ENSMUSG00000026042 .
    GeneIDi 12832.
    KEGGi mmu:12832.
    UCSCi uc007awr.1. mouse.

    Organism-specific databases

    CTDi 1290.
    MGIi MGI:88458. Col5a2.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00740000114967.
    HOVERGENi HBG004933.
    InParanoidi Q3U962.
    KOi K06236.
    OMAi IGIRGQP.
    OrthoDBi EOG7TJ3HH.
    PhylomeDBi Q3U962.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_196644. Syndecan interactions.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199046. Assembly of collagen fibrils and other multimeric structures.
    REACT_199055. Collagen degradation.
    REACT_206066. Extracellular matrix organization.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi COL5A2. mouse.
    NextBioi 282338.
    PROi Q3U962.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3U962.
    CleanExi MM_COL5A2.
    Genevestigatori Q3U962.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 7 hits.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    PROSITEi PS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Localization of pro-alpha 2(V) collagen transcripts in the tissues of the developing mouse embryo."
      Andrikopoulos K., Suzuki H.R., Solursh M., Ramirez F.
      Dev. Dyn. 195:113-120(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
      Strain: BALB/cImported.
    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].
      Strain: C57BL/6JImported.
      Tissue: Bone marrowImported, CerebellumImported, EmbryoImported, PlacentaImported and SkinImported.
    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].
      Strain: C3H/HeImported.
      Tissue: Mammary glandImported and Mesenchymal stem cellImported.
    4. "Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly."
      Andrikopoulos K., Liu X., Keene D.R., Jaenisch R., Ramirez F.
      Nat. Genet. 9:31-36(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Effect of targeted mutation in collagen V alpha 2 gene on development of cutaneous hyperplasia in tight skin mice."
      Phelps R.G., Murai C., Saito S., Hatakeyama A., Andrikopoulos K., Kasturi K.N., Bona C.A.
      Mol. Med. 4:356-360(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Development of a functional skin matrix requires deposition of collagen V heterotrimers."
      Chanut-Delalande H., Bonod-Bidaud C., Cogne S., Malbouyres M., Ramirez F., Fichard A., Ruggiero F.
      Mol. Cell. Biol. 24:6049-6057(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiCO5A2_MOUSE
    AccessioniPrimary (citable) accession number: Q3U962
    Secondary accession number(s): Q3TVR2
    , Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mice homozygous for the targeted deletion of the N-terminal telopeptide segment of the COL5A2 chain show poor survival rates, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils.3 Publications
    The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer makes a critical contribution to fibrillogenesis, basement membrane organization, and cell viability, and may play a possible role in the development of a functional skin matrix.1 Publication

    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