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)

P05997

- CO5A2_HUMAN

UniProt

P05997 - CO5A2_HUMAN

Protein

Collagen alpha-2(V) chain

Gene

COL5A2

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 166 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      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. Type V collagen is a key determinant in the assembly of tissue-specific matrices By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1314 – 13141CalciumBy similarity
    Metal bindingi1316 – 13161CalciumBy similarity
    Metal bindingi1317 – 13171Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1322 – 13221CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cellular response to amino acid stimulus 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. eye morphogenesis Source: UniProtKB
    8. skeletal system development Source: Ensembl
    9. skin development Source: UniProtKB

    Keywords - Ligandi

    Calcium, 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-2(V) chain
    Gene namesi
    Name:COL5A2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2210. COL5A2.

    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 matrix Source: UniProtKB
    4. extracellular region Source: Reactome

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 varianti963 – 9631G → R in EDS2. 1 Publication
    VAR_013588

    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.
    PharmGKBiPA26725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 12291203Collagen alpha-2(V) chainPRO_0000005830Add
    BLAST
    Propeptidei1230 – 1499270C-terminal propeptidePRO_0000005831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei290 – 2901Hydroxyproline1 Publication
    Modified residuei293 – 2931Hydroxyproline1 Publication
    Modified residuei296 – 2961Hydroxyproline1 Publication
    Modified residuei611 – 6111Hydroxyproline1 Publication
    Modified residuei617 – 6171Hydroxyproline1 Publication
    Modified residuei919 – 91913-hydroxyproline; partial1 Publication
    Modified residuei1156 – 115613-hydroxyproline; partial1 Publication
    Glycosylationi1262 – 12621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1296 ↔ 1328PROSITE-ProRule annotation
    Disulfide bondi1336 ↔ 1497PROSITE-ProRule annotation
    Glycosylationi1400 – 14001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1405 ↔ 1450PROSITE-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 Pro-919 and Pro-1156 by LEPREL1.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP05997.
    PaxDbiP05997.
    PRIDEiP05997.

    PTM databases

    PhosphoSiteiP05997.

    Miscellaneous databases

    PMAP-CutDBP05997.

    Expressioni

    Gene expression databases

    ArrayExpressiP05997.
    BgeeiP05997.
    GenevestigatoriP05997.

    Organism-specific databases

    HPAiHPA047922.

    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.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A9Amodel-B561-581[»]
    ProteinModelPortaliP05997.
    SMRiP05997. Positions 35-96, 1284-1499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 9759VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1266 – 1499234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi506 – 5083Cell attachment siteSequence Analysis
    Motifi944 – 9463Cell attachment siteSequence Analysis
    Motifi1067 – 10693Cell attachment siteSequence Analysis
    Motifi1070 – 10723Cell attachment siteSequence Analysis
    Motifi1100 – 11023Cell attachment siteSequence Analysis
    Motifi1127 – 11293Cell attachment siteSequence Analysis
    Motifi1136 – 11383Cell 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.
    HOVERGENiHBG004933.
    InParanoidiP05997.
    KOiK06236.
    OMAiIGIRGQP.
    OrthoDBiEOG7TJ3HH.
    PhylomeDBiP05997.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 9 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.

    P05997-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN     50
    RDIWKPAPCQ ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP 100
    GGGNTNFGRG RKGQKGEPGL VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG 150
    RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS HPGPDGLSRP FSAQMAGLDE 200
    KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG EPGDPGPMGP 250
    IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG 300
    HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ 350
    GAPGQRGAHG MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP 400
    QGQRGETGPP GPVGSPGLPG AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG 450
    SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG PKGEPGPHGI QGPIGPPGEE 500
    GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG AQGERGPVGS 550
    SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG 600
    PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV 650
    GPSGPVGPPG LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD 700
    PGAVGPLGPR GERGNPGERG EPGITGLPGE KGMAGGHGPD GPKGSPGPSG 750
    TPGDTGPPGL QGMPGERGIA GTPGPKGDRG GIGEKGAEGT AGNDGARGLP 800
    GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG PTGAVGFAGP 850
    QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG 900
    TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH 950
    GRVGDRGPAG PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ 1000
    RGERGMPGLP GPAGTPGKVG PTGATGDKGP PGPVGPPGSN GPVGEPGPEG 1050
    PAGNDGTPGR DGAVGERGDR GDPGPAGLPG SQGAPGTPGP VGAPGDAGQR 1100
    GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG QKGHRGFTGL 1150
    QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG 1200
    VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE 1250
    FTEDQAAPDD KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK 1300
    LCHSAKQSGE YWIDPNQGSV EDAIKVYCNM ETGETCISAN PSSVPRKTWW 1350
    ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP NTAITQMTFL RLLSKEASQN 1400
    ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR FRYIVLQDTC 1450
    SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV 1499
    Length:1,499
    Mass (Da):144,910
    Last modified:April 3, 2007 - v3
    Checksum:iE8C92BF5E749EC97
    GO

    Sequence cautioni

    The sequence AAH43613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD92282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAY24185.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti292 – 2921A → P AA sequence (PubMed:8181482)Curated
    Sequence conflicti361 – 3611M → L in AAL13166. (PubMed:11566270)Curated
    Sequence conflicti430 – 4301A → P in CAA75002. 1 PublicationCurated
    Sequence conflicti430 – 4301A → P in AAA51859. (PubMed:2914927)Curated
    Sequence conflicti430 – 4301A → P in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti463 – 4664IRGQ → NSGL in CAA75002. 1 PublicationCurated
    Sequence conflicti463 – 4664IRGQ → NSGL in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti463 – 4631I → N in AAA51859. (PubMed:2914927)Curated
    Sequence conflicti472 – 4743Missing in CAA75002. 1 PublicationCurated
    Sequence conflicti472 – 4743Missing in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti512 – 5121V → L in CAA75002. 1 PublicationCurated
    Sequence conflicti512 – 5121V → L in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti608 – 6081R → K in CAA75002. 1 PublicationCurated
    Sequence conflicti608 – 6081R → K in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti613 – 6131S → T in CAA75002. 1 PublicationCurated
    Sequence conflicti613 – 6131S → T in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti623 – 6231S → N in CAA75002. 1 PublicationCurated
    Sequence conflicti623 – 6231S → N in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti635 – 6351A → P in CAA75002. 1 PublicationCurated
    Sequence conflicti635 – 6351A → P in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti649 – 6491E → K in CAA75002. 1 PublicationCurated
    Sequence conflicti649 – 6491E → K in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti653 – 6531S → Y in CAA75002. 1 PublicationCurated
    Sequence conflicti653 – 6531S → Y in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti656 – 6561V → P in CAA75002. 1 PublicationCurated
    Sequence conflicti656 – 6561V → P in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti662 – 6621A → R in CAA75002. 1 PublicationCurated
    Sequence conflicti662 – 6621A → R in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti679 – 6791L → H in CAA75002. 1 PublicationCurated
    Sequence conflicti679 – 6791L → H in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti700 – 7001D → G in CAA75002. 1 PublicationCurated
    Sequence conflicti700 – 7001D → G in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti797 – 7971R → G in CAA75002. 1 PublicationCurated
    Sequence conflicti797 – 7971R → G in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti811 – 8122PT → LL in CAA75002. 1 PublicationCurated
    Sequence conflicti811 – 8122PT → LL in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti853 – 8531P → S in CAA75002. 1 PublicationCurated
    Sequence conflicti853 – 8531P → S in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti943 – 9431L → P in CAA75002. 1 PublicationCurated
    Sequence conflicti943 – 9431L → P in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti955 – 9551D → V in CAA75002. 1 PublicationCurated
    Sequence conflicti955 – 9551D → V in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti1111 – 11122PP → HL in CAA75002. 1 PublicationCurated
    Sequence conflicti1111 – 11122PP → HL in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti1111 – 11122PP → HL in AAA52007. (PubMed:2985598)Curated
    Sequence conflicti1196 – 11961I → L in CAA75002. 1 PublicationCurated
    Sequence conflicti1196 – 11961I → L in CAA28454. (PubMed:3029669)Curated
    Sequence conflicti1196 – 11961I → L in AAA52007. (PubMed:2985598)Curated
    Sequence conflicti1421 – 14211K → T in AAA52058. (PubMed:2411731)Curated
    Sequence conflicti1441 – 14411F → S in AAA52058. (PubMed:2411731)Curated
    Sequence conflicti1467 – 14671Q → E in AAA51858. (PubMed:3224983)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti460 – 4601P → S.
    Corresponds to variant rs35830636 [ dbSNP | Ensembl ].
    VAR_048799
    Natural varianti512 – 5121V → A.1 Publication
    Corresponds to variant rs35852101 [ dbSNP | Ensembl ].
    VAR_057910
    Natural varianti833 – 8331P → L.1 Publication
    Corresponds to variant rs116298748 [ dbSNP | Ensembl ].
    VAR_057911
    Natural varianti956 – 9561R → P.
    Corresponds to variant rs6434313 [ dbSNP | Ensembl ].
    VAR_048800
    Natural varianti963 – 9631G → R in EDS2. 1 Publication
    VAR_013588
    Natural varianti1230 – 12301T → S.1 Publication
    VAR_057912
    Natural varianti1432 – 14321D → V.1 Publication
    VAR_057913

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14690 mRNA. Translation: CAA75002.1.
    AB209045 mRNA. Translation: BAD92282.1. Different initiation.
    AC064833 Genomic DNA. No translation available.
    AC133106 Genomic DNA. Translation: AAY24185.1. Sequence problems.
    J04478 mRNA. Translation: AAA51859.1.
    AY016288, AY016287 Genomic DNA. Translation: AAL13165.1.
    AY016295
    , AY016289, AY016290, AY016291, AY016292, AY016293, AY016294 Genomic DNA. Translation: AAL13166.1.
    M58529 Genomic DNA. Translation: AAC41699.1.
    X04758 mRNA. Translation: CAA28454.1.
    BC043613 mRNA. Translation: AAH43613.1. Different initiation.
    M10956 mRNA. Translation: AAA52007.1.
    M11135 mRNA. Translation: AAA51857.1.
    M11718 mRNA. Translation: AAA52058.1.
    J03051 Genomic DNA. Translation: AAA51858.1.
    CCDSiCCDS33350.1.
    PIRiA31427. CGHU2V.
    RefSeqiNP_000384.2. NM_000393.3.
    UniGeneiHs.445827.

    Genome annotation databases

    EnsembliENST00000374866; ENSP00000364000; ENSG00000204262.
    GeneIDi1290.
    KEGGihsa:1290.
    UCSCiuc002uqk.3. human.

    Polymorphism databases

    DMDMi143811378.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14690 mRNA. Translation: CAA75002.1 .
    AB209045 mRNA. Translation: BAD92282.1 . Different initiation.
    AC064833 Genomic DNA. No translation available.
    AC133106 Genomic DNA. Translation: AAY24185.1 . Sequence problems.
    J04478 mRNA. Translation: AAA51859.1 .
    AY016288 , AY016287 Genomic DNA. Translation: AAL13165.1 .
    AY016295
    , AY016289 , AY016290 , AY016291 , AY016292 , AY016293 , AY016294 Genomic DNA. Translation: AAL13166.1 .
    M58529 Genomic DNA. Translation: AAC41699.1 .
    X04758 mRNA. Translation: CAA28454.1 .
    BC043613 mRNA. Translation: AAH43613.1 . Different initiation.
    M10956 mRNA. Translation: AAA52007.1 .
    M11135 mRNA. Translation: AAA51857.1 .
    M11718 mRNA. Translation: AAA52058.1 .
    J03051 Genomic DNA. Translation: AAA51858.1 .
    CCDSi CCDS33350.1.
    PIRi A31427. CGHU2V.
    RefSeqi NP_000384.2. NM_000393.3.
    UniGenei Hs.445827.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A9A model - B 561-581 [» ]
    ProteinModelPortali P05997.
    SMRi P05997. Positions 35-96, 1284-1499.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P05997.

    Polymorphism databases

    DMDMi 143811378.

    Proteomic databases

    MaxQBi P05997.
    PaxDbi P05997.
    PRIDEi P05997.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374866 ; ENSP00000364000 ; ENSG00000204262 .
    GeneIDi 1290.
    KEGGi hsa:1290.
    UCSCi uc002uqk.3. human.

    Organism-specific databases

    CTDi 1290.
    GeneCardsi GC02M189861.
    GeneReviewsi COL5A2.
    HGNCi HGNC:2210. COL5A2.
    HPAi HPA047922.
    MIMi 120190. gene.
    130000. phenotype.
    130010. phenotype.
    neXtProti NX_P05997.
    Orphaneti 90309. Ehlers-Danlos syndrome type 1.
    90318. Ehlers-Danlos syndrome type 2.
    PharmGKBi PA26725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    InParanoidi P05997.
    KOi K06236.
    OMAi IGIRGQP.
    OrthoDBi EOG7TJ3HH.
    PhylomeDBi P05997.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_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 COL5A2. human.
    GeneWikii COL5A2.
    GenomeRNAii 1290.
    NextBioi 5223.
    PMAP-CutDB P05997.
    PROi P05997.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05997.
    Bgeei P05997.
    Genevestigatori P05997.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 9 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. Richards A.J.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the structural criteria of a fibrillar procollagen molecule."
      Woodbury D., Benson-Chanda V., Ramirez F.
      J. Biol. Chem. 264:2735-2738(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-463.
    5. "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes."
      Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L.
      Matrix Biol. 20:357-366(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499.
    6. "Homology between alpha 2(V) and alpha 1(III) collagen promoters and evidence for negatively acting elements in the alpha 2(V) first intron and 5' flanking sequences."
      Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G.
      Gene Expr. 1:29-39(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
    7. "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 208-227.
      Tissue: Placenta.
    8. Cited for: PROTEIN SEQUENCE OF 288-297 AND 609-620, HYDROXYLATION AT PRO-290; PRO-293; PRO-296; PRO-611 AND PRO-617.
      Tissue: Bone.
    9. "The pro alpha 2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens."
      Weil D., Bernard M.P., Gargano S., Ramirez F.
      Nucleic Acids Res. 15:181-198(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499.
    10. "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 878-1499.
      Tissue: Skin.
    11. "Partial covalent structure of the human alpha 2 type V collagen chain."
      Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M.
      J. Biol. Chem. 260:5533-5541(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, PROTEIN SEQUENCE OF 1006-1036.
    12. "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2."
      Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.
      Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037.
    13. "Complete primary structure of the human alpha 2 type V procollagen COOH-terminal propeptide."
      Myers J.C., Loidl H.R., Seyer J.M., Dion A.S.
      J. Biol. Chem. 260:11216-11222(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499.
    14. "Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2."
      Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D., Ramirez F.
      Genomics 3:275-277(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499.
    15. "Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce Ehlers-Danlos syndrome type I."
      Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G.
      Hum. Mol. Genet. 7:249-255(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EDS1.
    16. "A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
      Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
      J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-919 AND PRO-1156, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II."
      Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M., Burrows N.P.
      J. Med. Genet. 35:846-848(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS2 ARG-963.
    18. "Sequence analysis of the COL5A2 gene in patients with spontaneous cervical artery dissections."
      Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., Hausser I., Brandt T.
      Neurology 58:1103-1105(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432.

    Entry informationi

    Entry nameiCO5A2_HUMAN
    AccessioniPrimary (citable) accession number: P05997
    Secondary accession number(s): P78440
    , Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 166 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 2
      Human chromosome 2: 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