Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25940

- CO5A3_HUMAN

UniProt

P25940 - CO5A3_HUMAN

Protein

Collagen alpha-3(V) chain

Gene

COL5A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (15 Dec 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    GO - Molecular functioni

    1. collagen binding Source: UniProtKB
    2. extracellular matrix structural constituent Source: UniProtKB
    3. heparin binding Source: Ensembl

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell-matrix adhesion Source: Ensembl
    3. collagen catabolic process Source: Reactome
    4. collagen fibril organization Source: UniProtKB
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. skin development Source: UniProtKB

    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_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.
    REACT_197897. Syndecan interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-3(V) chain
    Gene namesi
    Name:COL5A3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:14864. COL5A3.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type V trimer Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26726.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 17451716Collagen alpha-3(V) chainPRO_0000005845Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi102 – 1021N-linked (GlcNAc...)1 Publication
    Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication
    Disulfide bondi1544 – 1544InterchainPROSITE-ProRule annotation
    Disulfide bondi1567 – 1567InterchainPROSITE-ProRule annotation
    Disulfide bondi1576 – 1576InterchainPROSITE-ProRule annotation
    Disulfide bondi1585 ↔ 1742PROSITE-ProRule annotation
    Disulfide bondi1651 ↔ 1696PROSITE-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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP25940.
    PRIDEiP25940.

    PTM databases

    PhosphoSiteiP25940.

    Expressioni

    Gene expression databases

    BgeeiP25940.
    CleanExiHS_COL5A3.
    GenevestigatoriP25940.

    Organism-specific databases

    HPAiHPA048256.

    Interactioni

    Subunit structurei

    Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta.

    Protein-protein interaction databases

    STRINGi9606.ENSP00000264828.

    Structurei

    3D structure databases

    ProteinModelPortaliP25940.
    SMRiP25940. Positions 1533-1743.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 224163Laminin G-likeAdd
    BLAST
    Domaini391 – 44050Collagen-like 1Add
    BLAST
    Domaini482 – 53857Collagen-like 2Add
    BLAST
    Domaini824 – 87754Collagen-like 3Add
    BLAST
    Domaini905 – 95046Collagen-like 4Add
    BLAST
    Domaini951 – 98939Collagen-like 5Add
    BLAST
    Domaini1430 – 148859Collagen-like 6Add
    BLAST
    Domaini1514 – 1744231Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni211 – 391181Nonhelical regionAdd
    BLAST
    Regioni392 – 14891098Triple-helical regionAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 6 collagen-like domains.Curated
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    InParanoidiP25940.
    KOiK06236.
    OMAiKGDVGQD.
    OrthoDBiEOG7XPZ4W.
    PhylomeDBiP25940.
    TreeFamiTF323987.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51461. NC1_FIB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P25940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNRRDLGQP RAGLCLLLAA LQLLPGTQAD PVDVLKALGV QGGQAGVPEG     50
    PGFCPQRTPE GDRAFRIGQA STLGIPTWEL FPEGHFPENF SLLITLRGQP 100
    ANQSVLLSIY DERGARQLGL ALGPALGLLG DPFRPLPQQV NLTDGRWHRV 150
    AVSIDGEMVT LVADCEAQPP VLGHGPRFIS IAGLTVLGTQ DLGEKTFEGD 200
    IQELLISPDP QAAFQACERY LPDCDNLAPA ATVAPQGEPE TPRPRRKGKG 250
    KGRKKGRGRK GKGRKKNKEI WTSSPPPDSA ENQTSTDIPK TETPAPNLPP 300
    TPTPLVVTST VTTGLNATIL ERSLDPDSGT ELGTLETKAA REDEEGDDST 350
    MGPDFRAAEY PSRTQFQIFP GAGEKGAKGE PAVIEKGQQF EGPPGAPGPQ 400
    GVVGPSGPPG PPGFPGDPGP PGPAGLPGIP GIDGIRGPPG TVIMMPFQFA 450
    GGSFKGPPVS FQQAQAQAVL QQTQLSMKGP PGPVGLTGRP GPVGLPGHPG 500
    LKGEEGAEGP QGPRGLQGPH GPPGRVGKMG RPGADGARGL PGDTGPKGDR 550
    GFDGLPGLPG EKGQRGDFGH VGQPGPPGED GERGAEGPPG PTGQAGEPGP 600
    RGLLGPRGSP GPTGRPGVTG IDGAPGAKGN VGPPGEPGPP GQQGNHGSQG 650
    LPGPQGLIGT PGEKGPPGNP GIPGLPGSDG PLGHPGHEGP TGEKGAQGPP 700
    GSAGPPGYPG PRGVKGTSGN RGLQGEKGEK GEDGFPGFKG DVGLKGDQGK 750
    PGAPGPRGED GPEGPKGQAG QAGEEGPPGS AGEKGKLGVP GLPGYPGRPG 800
    PKGSIGFPGP LGPIGEKGKS GKTGQPGLEG ERGPPGSRGE RGQPGATGQP 850
    GPKGDVGQDG APGIPGEKGL PGLQGPPGFP GPKGPPGHQG KDGRPGHPGQ 900
    RGELGFQGQT GPPGPAGVLG PQGKTGEVGP LGERGPPGPP GPPGEQGLPG 950
    LEGREGAKGE LGPPGPLGKE GPAGLRGFPG PKGGPGDPGP TGLKGDKGPP 1000
    GPVGANGSPG ERGPLGPAGG IGLPGQSGSE GPVGPAGKKG SRGERGPPGP 1050
    TGKDGIPGPL GPLGPPGAAG PSGEEGDKGD VGAPGHKGSK GDKGDAGPPG 1100
    QPGIRGPAGH PGPPGADGAQ GRRGPPGLFG QKGDDGVRGF VGVIGPPGLQ 1150
    GLPGPPGEKG EVGDVGSMGP HGAPGPRGPQ GPTGSEGTPG LPGGVGQPGA 1200
    VGEKGERGDA GDPGPPGAPG IPGPKGDIGE KGDSGPSGAA GPPGKKGPPG 1250
    EDGAKGSVGP TGLPGDLGPP GDPGVSGIDG SPGEKGDPGD VGGPGPPGAS 1300
    GEPGAPGPPG KRGPSGHMGR EGREGEKGAK GEPGPDGPPG RTGPMGARGP 1350
    PGRVGPEGLR GIPGPVGEPG LLGAPGQMGP PGPLGPSGLP GLKGDTGPKG 1400
    EKGHIGLIGL IGPPGEAGEK GDQGLPGVQG PPGPKGDPGP PGPIGSLGHP 1450
    GPPGVAGPLG QKGSKGSPGS MGPRGDTGPA GPPGPPGAPA ELHGLRRRRR 1500
    FVPVPLPVVE GGLEEVLASL TSLSLELEQL RRPPGTAERP GLVCHELHRN 1550
    HPHLPDGEYW IDPNQGCARD SFRVFCNFTA GGETCLYPDK KFEIVKLASW 1600
    SKEKPGGWYS TFRRGKKFSY VDADGSPVNV VQLNFLKLLS ATARQNFTYS 1650
    CQNAAAWLDE ATGDYSHSAR FLGTNGEELS FNQTTAATVS VPQDGCRLRK 1700
    GQTKTLFEFS SSRAGFLPLW DVAATDFGQT NQKFGFELGP VCFSS 1745
    Length:1,745
    Mass (Da):172,121
    Last modified:December 15, 2009 - v3
    Checksum:i4F5644D2A919D864
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1687 – 16871A → T in AAF59902. (PubMed:10722718)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti134 – 1341R → H.
    Corresponds to variant rs2303098 [ dbSNP | Ensembl ].
    VAR_020015
    Natural varianti322 – 3221R → G.1 Publication
    Corresponds to variant rs2287803 [ dbSNP | Ensembl ].
    VAR_060789
    Natural varianti1042 – 10421R → P.
    Corresponds to variant rs2161468 [ dbSNP | Ensembl ].
    VAR_055678
    Natural varianti1207 – 12071R → P.
    Corresponds to variant rs2287813 [ dbSNP | Ensembl ].
    VAR_020016
    Natural varianti1428 – 14281V → M.
    Corresponds to variant rs3815746 [ dbSNP | Ensembl ].
    VAR_020017
    Natural varianti1488 – 14881A → P.
    Corresponds to variant rs3745584 [ dbSNP | Ensembl ].
    VAR_055679
    Natural varianti1594 – 15941I → M.
    Corresponds to variant rs3745581 [ dbSNP | Ensembl ].
    VAR_020018
    Natural varianti1691 – 16911V → I.
    Corresponds to variant rs2277969 [ dbSNP | Ensembl ].
    VAR_020019

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177941 mRNA. Translation: AAF59902.1.
    AC008742 Genomic DNA. No translation available.
    CCDSiCCDS12222.1.
    PIRiS20375.
    RefSeqiNP_056534.2. NM_015719.3.
    UniGeneiHs.235368.

    Genome annotation databases

    EnsembliENST00000264828; ENSP00000264828; ENSG00000080573.
    GeneIDi50509.
    KEGGihsa:50509.
    UCSCiuc002mmq.1. human.

    Polymorphism databases

    DMDMi281185497.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177941 mRNA. Translation: AAF59902.1 .
    AC008742 Genomic DNA. No translation available.
    CCDSi CCDS12222.1.
    PIRi S20375.
    RefSeqi NP_056534.2. NM_015719.3.
    UniGenei Hs.235368.

    3D structure databases

    ProteinModelPortali P25940.
    SMRi P25940. Positions 1533-1743.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000264828.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P25940.

    Polymorphism databases

    DMDMi 281185497.

    Proteomic databases

    PaxDbi P25940.
    PRIDEi P25940.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264828 ; ENSP00000264828 ; ENSG00000080573 .
    GeneIDi 50509.
    KEGGi hsa:50509.
    UCSCi uc002mmq.1. human.

    Organism-specific databases

    CTDi 50509.
    GeneCardsi GC19M010071.
    H-InvDB HIX0039977.
    HIX0040299.
    HGNCi HGNC:14864. COL5A3.
    HPAi HPA048256.
    MIMi 120216. gene.
    neXtProti NX_P25940.
    PharmGKBi PA26726.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    InParanoidi P25940.
    KOi K06236.
    OMAi KGDVGQD.
    OrthoDBi EOG7XPZ4W.
    PhylomeDBi P25940.
    TreeFami TF323987.

    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_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.
    REACT_197897. Syndecan interactions.

    Miscellaneous databases

    GeneWikii COL5A3.
    GenomeRNAii 50509.
    NextBioi 53078.
    PROi P25940.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25940.
    CleanExi HS_COL5A3.
    Genevestigatori P25940.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000885. Fib_collagen_C.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 6 hits.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51461. NC1_FIB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The pro-alpha3 (V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains."
      Imamura Y., Scott I.C., Greenspan D.S.
      J. Biol. Chem. 275:8749-8759(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-322.
      Tissue: Heart and Placenta.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing."
      Mann K.
      Biol. Chem. Hoppe-Seyler 373:69-75(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 479-564; 665-709; 723-758; 787-816; 922-1008; 1054-1088; 1248-1287 AND 1313-1334.
      Tissue: Placenta.
    4. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-141.
      Tissue: Liver.

    Entry informationi

    Entry nameiCO5A3_HUMAN
    AccessioniPrimary (citable) accession number: P25940
    Secondary accession number(s): Q9NZQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3