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P20908

- CO5A1_HUMAN

UniProt

P20908 - CO5A1_HUMAN

Protein

Collagen alpha-1(V) chain

Gene

COL5A1

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 3 (13 Sep 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1657 – 16571CalciumBy similarity
    Metal bindingi1659 – 16591CalciumBy similarity
    Metal bindingi1660 – 16601Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1662 – 16621Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1665 – 16651CalciumBy similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: Ensembl
    2. heparin binding Source: UniProtKB
    3. integrin binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. platelet-derived growth factor binding Source: MGI
    6. proteoglycan binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. blood vessel development Source: Ensembl
    3. cell adhesion Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. collagen biosynthetic process Source: UniProtKB
    6. collagen catabolic process Source: Reactome
    7. collagen fibril organization Source: UniProtKB
    8. extracellular fibril organization Source: UniProtKB
    9. extracellular matrix disassembly Source: Reactome
    10. extracellular matrix organization Source: Reactome
    11. eye morphogenesis Source: UniProtKB
    12. heart morphogenesis Source: Ensembl
    13. integrin biosynthetic process Source: UniProtKB
    14. regulation of cellular component organization Source: Ensembl
    15. skin development Source: UniProtKB
    16. tendon development Source: Ensembl
    17. wound healing, spreading of epidermal cells Source: UniProtKB

    Keywords - Ligandi

    Calcium, Heparin-binding, Metal-binding

    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-1(V) chain
    Gene namesi
    Name:COL5A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2209. COL5A1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. collagen type V trimer Source: UniProtKB
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular matrix Source: UniProtKB
    5. extracellular region Source: Reactome
    6. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ehlers-Danlos syndrome 1 (EDS1) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057902
    Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057903
    Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
    Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
    VAR_015412
    Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
    VAR_057909
    Natural varianti1489 – 14891G → D in EDS1. 1 Publication
    VAR_015413
    Natural varianti1639 – 16391C → S in EDS1. 1 Publication
    VAR_001808
    Ehlers-Danlos syndrome 2 (EDS2) [MIM:130010]: Mild form of classic Ehlers-Danlos syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057902
    Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057903
    Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
    Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
    VAR_015412
    Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
    VAR_057909

    Keywords - Diseasei

    Disease mutation, Ehlers-Danlos syndrome

    Organism-specific databases

    MIMi130000. phenotype.
    130010. phenotype.
    Orphaneti90309. Ehlers-Danlos syndrome type 1.
    90318. Ehlers-Danlos syndrome type 2.
    PharmGKBiPA26724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3737Sequence AnalysisAdd
    BLAST
    Chaini38 – 16051568Collagen alpha-1(V) chainPRO_0000005756Add
    BLAST
    Propeptidei1606 – 1838233C-terminal propeptidePRO_0000005757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341SulfotyrosineSequence Analysis
    Modified residuei236 – 2361SulfotyrosineSequence Analysis
    Modified residuei240 – 2401SulfotyrosineSequence Analysis
    Modified residuei262 – 2621SulfotyrosineSequence Analysis
    Modified residuei263 – 2631SulfotyrosineSequence Analysis
    Modified residuei338 – 3381SulfotyrosineSequence Analysis
    Modified residuei340 – 3401SulfotyrosineSequence Analysis
    Modified residuei346 – 3461SulfotyrosineSequence Analysis
    Modified residuei347 – 3471SulfotyrosineSequence Analysis
    Modified residuei416 – 4161SulfotyrosineSequence Analysis
    Modified residuei417 – 4171SulfotyrosineSequence Analysis
    Modified residuei420 – 4201SulfotyrosineSequence Analysis
    Modified residuei421 – 4211SulfotyrosineSequence Analysis
    Modified residuei570 – 5701Hydroxyproline1 Publication
    Modified residuei576 – 5761Hydroxyproline1 Publication
    Modified residuei621 – 6211Hydroxyproline1 Publication
    Modified residuei627 – 62715-hydroxylysine1 Publication
    Modified residuei639 – 6391Hydroxyproline1 Publication
    Modified residuei642 – 64215-hydroxylysine1 Publication
    Modified residuei648 – 6481Hydroxyproline1 Publication
    Modified residuei654 – 6541Hydroxyproline1 Publication
    Modified residuei657 – 6571Hydroxyproline1 Publication
    Modified residuei675 – 6751Hydroxyproline1 Publication
    Modified residuei678 – 6781Hydroxyproline1 Publication
    Modified residuei680 – 6801Hydroxyproline1 Publication
    Modified residuei686 – 6861Hydroxyproline1 Publication
    Modified residuei690 – 6901Hydroxyproline1 Publication
    Modified residuei696 – 6961Hydroxyproline1 Publication
    Modified residuei705 – 7051Hydroxyproline1 Publication
    Modified residuei708 – 70815-hydroxylysine1 Publication
    Modified residuei717 – 7171Hydroxyproline1 Publication
    Modified residuei720 – 7201Hydroxyproline1 Publication
    Modified residuei726 – 7261Hydroxyproline1 Publication
    Modified residuei732 – 7321Hydroxyproline1 Publication
    Modified residuei744 – 74415-hydroxylysine1 Publication
    Modified residuei750 – 7501Hydroxyproline1 Publication
    Modified residuei756 – 7561Hydroxyproline1 Publication
    Modified residuei762 – 7621Hydroxyproline1 Publication
    Modified residuei765 – 7651Hydroxyproline1 Publication
    Modified residuei771 – 7711Hydroxyproline1 Publication
    Modified residuei774 – 77415-hydroxylysine1 Publication
    Modified residuei780 – 7801Hydroxyproline1 Publication
    Modified residuei789 – 7891Hydroxyproline1 Publication
    Modified residuei795 – 79515-hydroxylysine1 Publication
    Modified residuei804 – 80415-hydroxylysine1 Publication
    Modified residuei807 – 80715-hydroxylysine1 Publication
    Modified residuei810 – 81015-hydroxylysine1 Publication
    Modified residuei816 – 8161Hydroxyproline1 Publication
    Modified residuei819 – 81915-hydroxylysine1 Publication
    Modified residuei834 – 8341Hydroxyproline1 Publication
    Modified residuei846 – 84615-hydroxylysine1 Publication
    Modified residuei861 – 8611Hydroxyproline1 Publication
    Modified residuei864 – 86415-hydroxylysine1 Publication
    Modified residuei870 – 8701Hydroxyproline1 Publication
    Modified residuei873 – 8731Hydroxyproline1 Publication
    Modified residuei876 – 8761Hydroxyproline1 Publication
    Modified residuei882 – 88215-hydroxylysine1 Publication
    Modified residuei888 – 8881Hydroxyproline1 Publication
    Modified residuei891 – 8911Hydroxyproline1 Publication
    Modified residuei897 – 89715-hydroxylysine1 Publication
    Modified residuei903 – 9031Hydroxyproline1 Publication
    Modified residuei906 – 9061Hydroxyproline1 Publication
    Modified residuei930 – 9301Hydroxyproline1 Publication
    Modified residuei945 – 9451Hydroxyproline1 Publication
    Modified residuei1017 – 10171Hydroxyproline1 Publication
    Modified residuei1020 – 10201Hydroxyproline1 Publication
    Modified residuei1023 – 10231Hydroxyproline1 Publication
    Modified residuei1029 – 10291Hydroxyproline1 Publication
    Modified residuei1221 – 12211Hydroxyproline1 Publication
    Modified residuei1224 – 12241Hydroxyproline1 Publication
    Modified residuei1467 – 14671Hydroxyproline1 Publication
    Modified residuei1470 – 14701Hydroxyproline1 Publication
    Modified residuei1601 – 16011SulfotyrosineSequence Analysis
    Modified residuei1604 – 16041SulfotyrosineSequence Analysis
    Disulfide bondi1639 ↔ 1671PROSITE-ProRule annotation
    Disulfide bondi1645 – 1645Interchain (with C-1662)PROSITE-ProRule annotation
    Disulfide bondi1662 – 1662Interchain (with C-1645)PROSITE-ProRule annotation
    Disulfide bondi1680 ↔ 1835PROSITE-ProRule annotation
    Disulfide bondi1746 ↔ 1789PROSITE-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.1 Publication
    Sulfated on 40% of tyrosines.

    Keywords - PTMi

    Disulfide bond, Hydroxylation, Sulfation

    Proteomic databases

    MaxQBiP20908.
    PaxDbiP20908.
    PRIDEiP20908.

    PTM databases

    PhosphoSiteiP20908.

    Miscellaneous databases

    PMAP-CutDBP20908.

    Expressioni

    Gene expression databases

    ArrayExpressiP20908.
    BgeeiP20908.
    CleanExiHS_COL5A1.
    GenevestigatoriP20908.

    Organism-specific databases

    HPAiCAB002743.
    HPA030769.

    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. Interacts with CSPG4.1 Publication

    Protein-protein interaction databases

    BioGridi107686. 8 interactions.
    IntActiP20908. 1 interaction.
    STRINGi9606.ENSP00000360882.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A89model-A/B/C904-924[»]
    1A9Amodel-A/C904-924[»]
    ProteinModelPortaliP20908.
    SMRiP20908. Positions 73-208, 1628-1837.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 244173Laminin G-likeAdd
    BLAST
    Domaini1609 – 1837229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 443213Nonhelical regionAdd
    BLAST
    Regioni444 – 558115Interrupted collagenous regionAdd
    BLAST
    Regioni559 – 15701012Triple-helical regionAdd
    BLAST
    Regioni1571 – 160535Nonhelical regionAdd
    BLAST

    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 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000085654.
    HOVERGENiHBG004933.
    KOiK06236.
    OMAiPIGVVQM.
    OrthoDBiEOG7XPZ4W.
    PhylomeDBiP20908.
    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. 5 hits.
    PF02210. Laminin_G_2. 1 hit.
    [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.

    P20908-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN     50
    LPDGITKTTG FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF 100
    SILTTVKAKK GSQAFLVSIY NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE 150
    DYPLFRGINL SDGKWHRIAL SVHKKNVTLI LDCKKKTTKF LDRSDHPMID 200
    INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD 250
    TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA 300
    KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS 350
    PYDDLTYGEG EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL 400
    EGEFTEETIR NLDENYYDPY YDPTSSPSEI GPGMPANQDT IYEGIGGPRG 450
    EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP GPPGTMGPTG QVGDPGERGP 500
    PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS AQESQAQAIL 550
    QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP 600
    GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP 650
    SGPPGPPGDD GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG 700
    MDGQPGPKGN VGPQGEPGPP GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP 750
    GLPGMPGADG PPGHPGKEGP PGEKGGQGPP GPQGPIGYPG PRGVKGADGI 800
    RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED GPEGPKGRGG 850
    PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR 900
    GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP 950
    NGPQGPTGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG 1000
    PQGPTGETGP MGERGHPGPP GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD 1050
    GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP GPPGPAGSPG ERGPAGAAGP 1100
    IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV GLPGPAGPVG 1150
    PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP 1200
    GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP 1250
    PGPPGPRGPS GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG 1300
    PPGPKGERGE KGESGPSGAA GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP 1350
    GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT GEPGPSGPPG KRGPPGPAGP 1400
    EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR GIPGPVGEQG 1450
    LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK 1500
    GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP 1550
    TGPKGEAGHP GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN 1600
    YVDYADGMEE IFGSLNSLKL EIEQMKRPLG TQQNPARTCK DLQLCHPDFP 1650
    DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC VFPDKKSEGA RITSWPKENP 1700
    GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ NVTYHCYQSV 1750
    AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL 1800
    EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG 1838
    Length:1,838
    Mass (Da):183,560
    Last modified:September 13, 2005 - v3
    Checksum:i8F18AB0B91B3A0C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 832QL → HV in AAA59993. (PubMed:1722213)Curated
    Sequence conflicti390 – 3901A → R in AAA59993. (PubMed:1722213)Curated
    Sequence conflicti641 – 6411E → G AA sequence (PubMed:2496661)Curated
    Sequence conflicti650 – 6501P → L AA sequence (PubMed:2496661)Curated
    Sequence conflicti663 – 6631R → E AA sequence (PubMed:2496661)Curated
    Sequence conflicti668 – 6681E → Q AA sequence (PubMed:2496661)Curated
    Sequence conflicti677 – 6771E → K in BAA14323. (PubMed:2071595)Curated
    Sequence conflicti677 – 6771E → Q AA sequence (PubMed:2496661)Curated
    Sequence conflicti684 – 6841L → P AA sequence (PubMed:2496661)Curated
    Sequence conflicti692 – 6998PPGPPGVT → VTGEPGAP AA sequence (PubMed:2496661)Curated
    Sequence conflicti727 – 7271G → Q AA sequence (PubMed:2496661)Curated
    Sequence conflicti741 – 7411P → L AA sequence (PubMed:2496661)Curated
    Sequence conflicti747 – 7471L → Q AA sequence (PubMed:2496661)Curated
    Sequence conflicti753 – 7531P → A AA sequence (PubMed:2496661)Curated
    Sequence conflicti759 – 7591D → N AA sequence (PubMed:2496661)Curated
    Sequence conflicti776 – 7772GQ → QK AA sequence (PubMed:2496661)Curated
    Sequence conflicti849 – 8557GGPNGDP → IGPPGPR AA sequence (PubMed:2203476)Curated
    Sequence conflicti894 – 8941N → D AA sequence (PubMed:2203476)Curated
    Sequence conflicti1295 – 12995LPGEG → PSGRS in BAA14323. (PubMed:2071595)Curated
    Sequence conflicti1554 – 15541K → R in BAA14323. (PubMed:2071595)Curated
    Sequence conflicti1813 – 18131V → A in AAA59993. (PubMed:1722213)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057902
    Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
    VAR_057903
    Natural varianti114 – 1141A → D Unclassified mutation. 1 Publication
    VAR_057904
    Natural varianti192 – 1921D → N Unclassified mutation. 1 Publication
    Corresponds to variant rs138579182 [ dbSNP | Ensembl ].
    VAR_057905
    Natural varianti229 – 2291D → N Associated with increased risk of cervical artery dissection. 1 Publication
    VAR_057906
    Natural varianti393 – 3931P → S Unclassified mutation. 1 Publication
    VAR_057907
    Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
    Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
    VAR_015412
    Natural varianti908 – 9081P → L Found in a renal cell carcinoma case; somatic mutation. 1 Publication
    VAR_064702
    Natural varianti951 – 9511N → S Unclassified mutation. 1 Publication
    Corresponds to variant rs61736966 [ dbSNP | Ensembl ].
    VAR_057908
    Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
    VAR_057909
    Natural varianti1489 – 14891G → D in EDS1. 1 Publication
    VAR_015413
    Natural varianti1639 – 16391C → S in EDS1. 1 Publication
    VAR_001808

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90279 mRNA. Translation: BAA14323.1.
    M76729 mRNA. Translation: AAA59993.1.
    AL591890, AL603650, AL645768 Genomic DNA. Translation: CAI15483.1.
    AL645768, AL591890, AL603650 Genomic DNA. Translation: CAI17261.1.
    AL603650, AL591890, AL645768 Genomic DNA. Translation: CAI39859.1.
    CCDSiCCDS6982.1.
    PIRiS18802. CGHU1V.
    RefSeqiNP_000084.3. NM_000093.4.
    UniGeneiHs.210283.

    Genome annotation databases

    EnsembliENST00000371817; ENSP00000360882; ENSG00000130635.
    GeneIDi1289.
    KEGGihsa:1289.
    UCSCiuc004cfe.4. human.

    Polymorphism databases

    DMDMi85687376.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90279 mRNA. Translation: BAA14323.1 .
    M76729 mRNA. Translation: AAA59993.1 .
    AL591890 , AL603650 , AL645768 Genomic DNA. Translation: CAI15483.1 .
    AL645768 , AL591890 , AL603650 Genomic DNA. Translation: CAI17261.1 .
    AL603650 , AL591890 , AL645768 Genomic DNA. Translation: CAI39859.1 .
    CCDSi CCDS6982.1.
    PIRi S18802. CGHU1V.
    RefSeqi NP_000084.3. NM_000093.4.
    UniGenei Hs.210283.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A89 model - A/B/C 904-924 [» ]
    1A9A model - A/C 904-924 [» ]
    ProteinModelPortali P20908.
    SMRi P20908. Positions 73-208, 1628-1837.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107686. 8 interactions.
    IntActi P20908. 1 interaction.
    STRINGi 9606.ENSP00000360882.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P20908.

    Polymorphism databases

    DMDMi 85687376.

    Proteomic databases

    MaxQBi P20908.
    PaxDbi P20908.
    PRIDEi P20908.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371817 ; ENSP00000360882 ; ENSG00000130635 .
    GeneIDi 1289.
    KEGGi hsa:1289.
    UCSCi uc004cfe.4. human.

    Organism-specific databases

    CTDi 1289.
    GeneCardsi GC09P137533.
    GeneReviewsi COL5A1.
    H-InvDB HIX0008519.
    HGNCi HGNC:2209. COL5A1.
    HPAi CAB002743.
    HPA030769.
    MIMi 120215. gene.
    130000. phenotype.
    130010. phenotype.
    neXtProti NX_P20908.
    Orphaneti 90309. Ehlers-Danlos syndrome type 1.
    90318. Ehlers-Danlos syndrome type 2.
    PharmGKBi PA26724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000085654.
    HOVERGENi HBG004933.
    KOi K06236.
    OMAi PIGVVQM.
    OrthoDBi EOG7XPZ4W.
    PhylomeDBi P20908.
    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

    ChiTaRSi COL5A1. human.
    GeneWikii Collagen,_type_V,_alpha_1.
    GenomeRNAii 1289.
    NextBioi 5219.
    PMAP-CutDB P20908.
    PROi P20908.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20908.
    Bgeei P20908.
    CleanExi HS_COL5A1.
    Genevestigatori P20908.

    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. 5 hits.
    PF02210. Laminin_G_2. 1 hit.
    [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. "Complete primary structure of human collagen alpha 1 (V) chain."
      Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y., Kato I.
      J. Biol. Chem. 266:13124-13129(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 556-565.
    2. "The pro-alpha-1(V) collagen chain: complete primary structure, distribution of expression, and comparison with the pro-alpha-1(XI) collagen chain."
      Greenspan D.S., Cheng W., Hoffman G.G.
      J. Biol. Chem. 266:24727-24733(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from human alpha 1(V) collagen chain."
      Seyer J.M., Kang A.H.
      Arch. Biochem. Biophys. 271:120-129(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 621-822, HYDROXYLATION.
      Tissue: Chorioamniotic membrane.
    5. "Primary structure of the heparin-binding site of type V collagen."
      Yaoi Y., Hashimoto K., Koitabashi H., Takahara K., Ito M., Kato I.
      Biochim. Biophys. Acta 1035:139-145(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 823-950, HEPARIN-BINDING.
    6. "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: PROTEIN SEQUENCE OF 556-571.
      Tissue: Placenta.
    7. Cited for: PROTEIN SEQUENCE OF 565-576; 756-772; 1012-1029; 1219-1232 AND 1465-1477.
      Tissue: Chorioamniotic membrane.
    8. "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein."
      Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.
      J. Biol. Chem. 272:10769-10776(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4.
    9. "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II."
      de Paepe A., Nuytinck L., Hausser I., Anton-Lamprecht I., Naeyaert J.-M.
      Am. J. Hum. Genet. 60:547-554(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, VARIANT EDS1 SER-1639.
    10. "Mutations in the COL5A1 coding sequence are not common in patients with spontaneous cervical artery dissections."
      Grond-Ginsbach C., Weber R., Haas J., Orberk E., Kunz S., Busse O., Hausser I., Brandt T., Wildemann B.
      Stroke 30:1887-1890(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-229, ASSOCIATION WITH INCREASED RISK OF CERVICAL ARTERY DISSECTION.
    11. "Compound heterozygosity for a disease-causing G1489E and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability?"
      Giunta C., Steinmann B.
      Am. J. Med. Genet. 90:72-79(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS1 SER-530 AND ASP-1489.
    12. Erratum
      Giunta C., Steinmann B.
      Am. J. Med. Genet. 93:342-342(2000)
    13. "Homozygous Gly530Ser substitution in COL5A1 causes mild classical Ehlers-Danlos syndrome."
      Giunta C., Nuytinck L., Raghunath M., Hausser I., De Paepe A., Steinmann B.
      Am. J. Med. Genet. 109:284-290(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS2 SER-530.
    14. "The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive study of biochemical and molecular findings in 48 unrelated patients."
      Malfait F., Coucke P., Symoens S., Loeys B., Nuytinck L., De Paepe A.
      Hum. Mutat. 25:28-37(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS1/EDS2 SER-530 AND CYS-1486, VARIANTS ASP-114; ASN-192; SER-393 AND SER-951.
    15. "COL5A1 signal peptide mutations interfere with protein secretion and cause classic Ehlers-Danlos syndrome."
      Symoens S., Malfait F., Renard M., Andre J., Hausser I., Loeys B., Coucke P., De Paepe A.
      Hum. Mutat. 30:E395-E403(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS1/EDS2 ARG-25 AND PRO-25, CHARACTERIZATION OF VARIANTS EDS1/EDS2 ARG-25 AND PRO-25.
    16. Cited for: VARIANT LEU-908.

    Entry informationi

    Entry nameiCO5A1_HUMAN
    AccessioniPrimary (citable) accession number: P20908
    Secondary accession number(s): Q15094, Q5SUX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 163 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

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

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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