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Q99715

- COCA1_HUMAN

UniProt

Q99715 - COCA1_HUMAN

Protein

Collagen alpha-1(XII) chain

Gene

COL12A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.By similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent conferring tensile strength Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. collagen catabolic process Source: Reactome
    3. collagen fibril organization Source: UniProtKB
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. skeletal system development Source: ProtInc

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_150401. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XII) chain
    Gene namesi
    Name:COL12A1
    Synonyms:COL12A1L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2188. COL12A1.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type XII trimer Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26704.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 30633040Collagen alpha-1(XII) chainPRO_0000005783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi798 – 7981O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi889 – 8891O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi981 – 9811O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2206 – 22061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2528 – 25281N-linked (GlcNAc...)1 Publication
    Glycosylationi2679 – 26791N-linked (GlcNAc...)1 Publication
    Modified residuei2944 – 294414-hydroxyprolineBy similarity
    Modified residuei2947 – 294714-hydroxyprolineBy similarity
    Modified residuei2950 – 295014-hydroxyprolineBy similarity
    Modified residuei2959 – 295914-hydroxyprolineBy similarity
    Modified residuei2965 – 296514-hydroxyprolineBy similarity
    Modified residuei2968 – 296814-hydroxyprolineBy similarity
    Modified residuei2971 – 297114-hydroxyprolineBy similarity
    Modified residuei2983 – 298314-hydroxyprolineBy similarity
    Modified residuei3000 – 300014-hydroxyprolineBy similarity
    Modified residuei3003 – 300314-hydroxyprolineBy similarity
    Modified residuei3014 – 301414-hydroxyprolineBy similarity
    Modified residuei3023 – 302314-hydroxyprolineBy similarity
    Modified residuei3026 – 302614-hydroxyprolineBy similarity
    Modified residuei3029 – 302914-hydroxyprolineBy similarity

    Post-translational modificationi

    The triple-helical tail is stabilized by disulfide bonds at each end.By similarity
    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
    Isoform 1 O-glycosylation; glycosaminoglycan of chondroitin-sulfate type.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ99715.
    PaxDbiQ99715.
    PRIDEiQ99715.

    PTM databases

    PhosphoSiteiQ99715.

    Expressioni

    Tissue specificityi

    Found in collagen I-containing tissues: both isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle, small intestine, and in cell culture of dermal fibroblasts, keratinocytes and endothelial cells. Only isoform 2 is found in lung, placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is also present in the corneal epithelial Bowman's membrane (BM) and the interfibrillar matrix of the corneal stroma, but it is not detected in the limbal BM.1 Publication

    Gene expression databases

    ArrayExpressiQ99715.
    BgeeiQ99715.
    CleanExiHS_COL12A1.
    GenevestigatoriQ99715.

    Organism-specific databases

    HPAiHPA009143.

    Interactioni

    Subunit structurei

    Trimer of identical chains each containing 190 kDa of non-triple-helical sequences.

    Protein-protein interaction databases

    BioGridi107700. 1 interaction.
    IntActiQ99715. 6 interactions.
    STRINGi9606.ENSP00000325146.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99715.
    SMRiQ99715. Positions 25-1179, 1196-1367, 1385-2310, 2317-2724.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 11791Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 316177VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini336 – 42691Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini440 – 616177VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini634 – 72289Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini725 – 81692Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini817 – 90589Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 99892Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini999 – 108789Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1089 – 117991Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1199 – 1371173VWFA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1387 – 147690Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1477 – 156791Fibronectin type-III 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1568 – 165891Fibronectin type-III 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1659 – 175496Fibronectin type-III 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1755 – 184995Fibronectin type-III 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1850 – 193586Fibronectin type-III 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1936 – 202691Fibronectin type-III 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2027 – 211791Fibronectin type-III 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2118 – 220689Fibronectin type-III 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2207 – 229488Fibronectin type-III 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2323 – 2496174VWFA 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2520 – 2712193Laminin G-likeAdd
    BLAST
    Domaini2747 – 279852Collagen-like 1Add
    BLAST
    Domaini2802 – 285251Collagen-like 2Add
    BLAST
    Domaini2853 – 289846Collagen-like 3Add
    BLAST
    Domaini2941 – 299050Collagen-like 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2451 – 2746296Nonhelical region (NC3)Add
    BLAST
    Regioni2747 – 2898152Triple-helical region (COL2) with 1 imperfectionAdd
    BLAST
    Regioni2899 – 294143Nonhelical region (NC2)Add
    BLAST
    Regioni2942 – 3044103Triple-helical region (COL1) with 2 imperfectionsAdd
    BLAST
    Regioni3045 – 306319Nonhelical region (NC1)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi862 – 8643Cell attachment siteSequence Analysis
    Motifi2779 – 27813Cell attachment siteSequence Analysis
    Motifi2895 – 28973Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 4 collagen-like domains.Curated
    Contains 18 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated
    Contains 4 VWFA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG051060.
    InParanoidiQ99715.
    KOiK08132.
    OMAiNRFNQML.
    PhylomeDBiQ99715.
    TreeFamiTF329914.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    2.60.40.10. 18 hits.
    3.40.50.410. 4 hits.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR001791. Laminin_G.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01391. Collagen. 4 hits.
    PF00041. fn3. 18 hits.
    PF00092. VWA. 4 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 18 hits.
    SM00210. TSPN. 1 hit.
    SM00327. VWA. 4 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 11 hits.
    SSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 4 hits.
    PROSITEiPS50853. FN3. 18 hits.
    PS50234. VWFA. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: The final tissue form of collagen XII may contain homotrimers of either isoform 1 or isoform 2 or any combination of isoform 1 and isoform 2.

    Isoform 1 (identifier: Q99715-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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    MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD     50
    PIVGYRITVD PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV 100
    EESVPVIGQL TIQTGSSTKP VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS 150
    VGRNNFKYIL DFIAALVSAF DIGEEKTRVG VVQYSSDTRT EFNLNQYYQR 200
    DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG FPKVAIIITD 250
    GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA 300
    NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV 350
    KLNWNPSPSP VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY 400
    QISVSAMKGM TSSEPISIME KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS 450
    IGIANFVKVR AFLEVLVKSF EISPNRVQIS LVQYSRDPHT EFTLKKFTKV 500
    EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN VPKVMILITD 550
    GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE 600
    DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT 650
    NWSPAGENVF SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN 700
    VTAEYEDGFS IPLAGEETTE EVKGAPRNLK VTDETTDSFK ITWTQAPGRV 750
    LRYRIIYRPV AGGESREVTT PPNQRRRTLE NLIPDTKYEV SVIPEYFSGP 800
    GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK VKQYLVTYTP 850
    VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT 900
    TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE 950
    KNLPEDAIHT MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK 1000
    TLKVDEETEN TMRVTWKPAP GKVVNYRVVY RPHGRGKQMV AKVPPTVTST 1050
    VLKRLQPQTT YDITVLPIYK MGEGKLRQGS GTTASRFKSP RNLKTSDPTM 1100
    SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN TVVLEELRAG 1150
    TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI 1200
    VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE 1250
    WQLNAHRDKK SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA 1300
    RKIGVLITDG KSQDDVEAPS KKLKDEGVEL FAIGIKNADE VELKMIATDP 1350
    DDTHAYNVAD FESLSRIVDD LTINLCNSVK GPGDLEAPSN LVISERTHRS 1400
    FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV LKDLKPETEY 1450
    VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA 1500
    TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH 1550
    DLTSEPVTVR EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY 1600
    KTPEEDVKEV EVDRSETSTS LKDLFSQTLY TVSVSAVHDE GESPPVTAQE 1650
    TTRPVPAPTN LKITEVTSEG FRGTWDHGAS DVSLYRITWA PFGSSDKMET 1700
    ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS ERTLPILTTQ 1750
    APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT 1800
    IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL 1850
    RVYDPSTSTL NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL 1900
    RNLQPDTSYT VTVVPVYTEG DGGRTSDTGR TLMRGLARNV QVYNPTPNSL 1950
    DVRWDPAPGP VLQYRVVYSP VDGTRPSESI VVPGNTRMVH LERLIPDTLY 2000
    SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS LSVAWDHADG 2050
    PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE 2100
    DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY 2150
    KPVGSNEPME AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG 2200
    TTLYLNVTDL KTYQIGWDTF CVKWSPHRAA TSYRLKLSPA DGTRGQEITV 2250
    RGSETSHCFT GLSPDTDYGV TVFVQTPNLE GPGVSVKEHT TVKPTEAPTE 2300
    PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN KVVKFIFNTV 2350
    GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN 2400
    TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ 2450
    SGFSVFVVGV ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV 2500
    CETATSSCPL IYLDGYTSPG FKMLEAYNLT EKNFASVQGV SLESGSFPSY 2550
    SAYRIQKNAF VNQPTADLHP NGLPPSYTII LLFRLLPETP SDPFAIWQIT 2600
    DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV KTLFYGSFHK 2650
    VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA 2700
    FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG 2750
    PPGPAGGPGA KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS 2800
    IPGEQGRQGM KGDAGEPGLP GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM 2850
    GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH GRPGPSGLKG EKGDRGDIAS 2900
    QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ PGPPGPPGPP 2950
    GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP 3000
    GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA 3050
    SIPYNGQGYP GSG 3063
    Length:3,063
    Mass (Da):333,147
    Last modified:May 1, 2007 - v2
    Checksum:iEA38CAFECE8393D2
    GO
    Isoform 2 (identifier: Q99715-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         25-1188: Missing.

    Show »
    Length:1,899
    Mass (Da):205,491
    Checksum:iECFB9F5436FF7B24
    GO
    Isoform 4 (identifier: Q99715-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2651-2726: Missing.

    Show »
    Length:2,987
    Mass (Da):324,570
    Checksum:iE5EEB57CBFB556E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471K → E in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti441 – 4422IV → M in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti581 – 5811R → D in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti689 – 6891S → N in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti743 – 7431W → S in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti749 – 7491R → K in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti753 – 7531Y → C in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti813 – 8131V → G in AAC01506. (PubMed:9344363)Curated
    Sequence conflicti1355 – 13551A → D in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti1690 – 16901A → G in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti1729 – 17291P → A in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti1949 – 19513SLD → RLG in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti2614 – 26141P → S in AAB23937. (PubMed:1427837)Curated
    Sequence conflicti2647 – 26482SF → RK in AAB23937. (PubMed:1427837)Curated
    Sequence conflicti2848 – 28481G → S in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti2858 – 28581P → R in AAC51244. (PubMed:9143499)Curated
    Sequence conflicti3035 – 30351R → Q in AAC51244. (PubMed:9143499)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti461 – 4611A → P.
    Corresponds to variant rs34730529 [ dbSNP | Ensembl ].
    VAR_048768
    Natural varianti1738 – 17381I → T.
    Corresponds to variant rs240736 [ dbSNP | Ensembl ].
    VAR_048769
    Natural varianti2021 – 20211R → Q.
    Corresponds to variant rs34438461 [ dbSNP | Ensembl ].
    VAR_061111
    Natural varianti2160 – 21601E → V.
    Corresponds to variant rs35523808 [ dbSNP | Ensembl ].
    VAR_048770
    Natural varianti2596 – 25961I → V.
    Corresponds to variant rs35710072 [ dbSNP | Ensembl ].
    VAR_048771
    Natural varianti3048 – 30481Q → H.
    Corresponds to variant rs57396313 [ dbSNP | Ensembl ].
    VAR_061112
    Natural varianti3058 – 30581G → S.1 Publication
    Corresponds to variant rs970547 [ dbSNP | Ensembl ].
    VAR_032059

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 11881164Missing in isoform 2. 1 PublicationVSP_001149Add
    BLAST
    Alternative sequencei2651 – 272676Missing in isoform 4. CuratedVSP_024942Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73778 mRNA. Translation: AAC51244.1.
    U73779 mRNA. Translation: AAD40483.1.
    AL080250, AL096771, AL354664 Genomic DNA. Translation: CAI19898.1.
    AL354664, AL080250, AL096771 Genomic DNA. Translation: CAH71310.1.
    AL096771, AL354664, AL080250 Genomic DNA. Translation: CAI19908.1.
    AF061871 Genomic DNA. Translation: AAC83578.1.
    U68139 mRNA. Translation: AAC01506.1.
    AH004088 Genomic DNA. Translation: AAB23937.2.
    CCDSiCCDS43481.1. [Q99715-2]
    CCDS43482.1. [Q99715-1]
    PIRiA44479.
    RefSeqiNP_004361.3. NM_004370.5. [Q99715-1]
    NP_542376.2. NM_080645.2. [Q99715-2]
    UniGeneiHs.101302.

    Genome annotation databases

    EnsembliENST00000322507; ENSP00000325146; ENSG00000111799. [Q99715-1]
    ENST00000345356; ENSP00000305147; ENSG00000111799. [Q99715-2]
    ENST00000416123; ENSP00000412864; ENSG00000111799. [Q99715-4]
    GeneIDi1303.
    KEGGihsa:1303.
    UCSCiuc003phs.3. human. [Q99715-1]
    uc003pht.3. human. [Q99715-2]

    Polymorphism databases

    DMDMi146345397.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73778 mRNA. Translation: AAC51244.1 .
    U73779 mRNA. Translation: AAD40483.1 .
    AL080250 , AL096771 , AL354664 Genomic DNA. Translation: CAI19898.1 .
    AL354664 , AL080250 , AL096771 Genomic DNA. Translation: CAH71310.1 .
    AL096771 , AL354664 , AL080250 Genomic DNA. Translation: CAI19908.1 .
    AF061871 Genomic DNA. Translation: AAC83578.1 .
    U68139 mRNA. Translation: AAC01506.1 .
    AH004088 Genomic DNA. Translation: AAB23937.2 .
    CCDSi CCDS43481.1. [Q99715-2 ]
    CCDS43482.1. [Q99715-1 ]
    PIRi A44479.
    RefSeqi NP_004361.3. NM_004370.5. [Q99715-1 ]
    NP_542376.2. NM_080645.2. [Q99715-2 ]
    UniGenei Hs.101302.

    3D structure databases

    ProteinModelPortali Q99715.
    SMRi Q99715. Positions 25-1179, 1196-1367, 1385-2310, 2317-2724.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107700. 1 interaction.
    IntActi Q99715. 6 interactions.
    STRINGi 9606.ENSP00000325146.

    PTM databases

    PhosphoSitei Q99715.

    Polymorphism databases

    DMDMi 146345397.

    Proteomic databases

    MaxQBi Q99715.
    PaxDbi Q99715.
    PRIDEi Q99715.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322507 ; ENSP00000325146 ; ENSG00000111799 . [Q99715-1 ]
    ENST00000345356 ; ENSP00000305147 ; ENSG00000111799 . [Q99715-2 ]
    ENST00000416123 ; ENSP00000412864 ; ENSG00000111799 . [Q99715-4 ]
    GeneIDi 1303.
    KEGGi hsa:1303.
    UCSCi uc003phs.3. human. [Q99715-1 ]
    uc003pht.3. human. [Q99715-2 ]

    Organism-specific databases

    CTDi 1303.
    GeneCardsi GC06M075850.
    H-InvDB HIX0006013.
    HGNCi HGNC:2188. COL12A1.
    HPAi HPA009143.
    MIMi 120320. gene.
    neXtProti NX_Q99715.
    PharmGKBi PA26704.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG051060.
    InParanoidi Q99715.
    KOi K08132.
    OMAi NRFNQML.
    PhylomeDBi Q99715.
    TreeFami TF329914.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi COL12A1. human.
    GeneWikii Collagen,_type_XII,_alpha_1.
    GenomeRNAii 1303.
    NextBioi 5299.
    PROi Q99715.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99715.
    Bgeei Q99715.
    CleanExi HS_COL12A1.
    Genevestigatori Q99715.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    2.60.40.10. 18 hits.
    3.40.50.410. 4 hits.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR001791. Laminin_G.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01391. Collagen. 4 hits.
    PF00041. fn3. 18 hits.
    PF00092. VWA. 4 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 18 hits.
    SM00210. TSPN. 1 hit.
    SM00327. VWA. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 11 hits.
    SSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 4 hits.
    PROSITEi PS50853. FN3. 18 hits.
    PS50234. VWFA. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete primary structure of two splice variants of collagen XII, and assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13."
      Gerecke D.R., Olson P.F., Koch M., Knoll J.H.M., Taylor R., Hudson D.L., Champliaud M.-F., Olsen B.R., Burgeson R.E.
      Genomics 41:236-242(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1280-1295; 1782-1801 AND 2906-2916, VARIANT SER-3058.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The chick and human collagen alpha1(XII) gene promoter -- activity of highly conserved regions around the first exon and in the first intron."
      Chiquet M., Mumenthaler U., Wittwer M., Jin W., Koch M.
      Eur. J. Biochem. 257:362-371(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    4. "Type XII collagen contributes to diversities in human corneal and limbal extracellular matrices."
      Wessel H., Anderson S., Fite D., Halvas E., Hempel J., SundarRaj N.
      Invest. Ophthalmol. Vis. Sci. 38:2408-2422(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-816 (ISOFORMS 1/4), TISSUE SPECIFICITY.
      Tissue: Cornea.
    5. "The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes are localized on mouse chromosome 9 and human chromosome 6."
      Oh S.P., Taylor R.W., Gerecke D.R., Rochelle J.M., Seldin M.F., Olsen B.R.
      Genomics 14:225-231(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2567-2755 (ISOFORM 4).
    6. "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-2528 AND ASN-2679.
      Tissue: Liver.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCOCA1_HUMAN
    AccessioniPrimary (citable) accession number: Q99715
    Secondary accession number(s): O43853
    , Q15955, Q5VYK1, Q5VYK2, Q71UR3, Q99716
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 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 6
      Human chromosome 6: 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