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P39059

- COFA1_HUMAN

UniProt

P39059 - COFA1_HUMAN

Protein

Collagen alpha-1(XV) chain

Gene

COL15A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.1 Publication
    Restin potently inhibits angiogenesis.By similarity

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. collagen catabolic process Source: Reactome
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Angiogenesis, Cell adhesion, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XV) chain
    Cleaved into the following 4 chains:
    Alternative name(s):
    Endostatin-XV
    Related to endostatin
    Restin-I
    Alternative name(s):
    Restin-II
    Alternative name(s):
    Restin-III
    Alternative name(s):
    Restin-IV
    Gene namesi
    Name:COL15A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2192. COL15A1.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type XV 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: UniProt
    6. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26708.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 13881361Collagen alpha-1(XV) chainPRO_0000005788Add
    BLAST
    Chaini1198 – 1386189RestinPRO_0000005789Add
    BLAST
    Chaini1207 – 1386180Restin-2PRO_0000423014Add
    BLAST
    Chaini1213 – 1386174Restin-3PRO_0000423015Add
    BLAST
    Chaini1221 – 1386166Restin-4PRO_0000423016Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi265 – 2651O-linked (GalNAc...)2 Publications
    Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1046 – 10461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1237 ↔ 13771 Publication
    Disulfide bondi1339 ↔ 13691 Publication

    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.
    O-glycosylated; with core 1 or possibly core 8 glycans. An N-terminal peptide contains chondroitin sulfate.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP39059.
    PaxDbiP39059.
    PRIDEiP39059.

    PTM databases

    PhosphoSiteiP39059.

    Expressioni

    Tissue specificityi

    Expressed predominantly in internal organs such as adrenal gland, pancreas and kidney.

    Gene expression databases

    BgeeiP39059.
    CleanExiHS_COL15A1.
    GenevestigatoriP39059.

    Organism-specific databases

    HPAiHPA017913.
    HPA017915.

    Interactioni

    Subunit structurei

    Trimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi107702. 2 interactions.
    IntActiP39059. 2 interactions.
    STRINGi9606.ENSP00000364140.

    Structurei

    Secondary structure

    1
    1388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1135 – 11406
    Helixi1141 – 11455
    Helixi1146 – 11505
    Beta strandi1155 – 11595
    Turni1160 – 11634
    Beta strandi1164 – 11696
    Beta strandi1172 – 11754

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N3FX-ray2.00A/B1133-1186[»]
    ProteinModelPortaliP39059.
    SMRiP39059. Positions 1133-1186, 1215-1382.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 249184Laminin G-likeAdd
    BLAST
    Repeati358 – 408511Add
    BLAST
    Repeati409 – 459512Add
    BLAST
    Repeati460 – 509503Add
    BLAST
    Repeati510 – 555464Add
    BLAST
    Domaini619 – 68062Collagen-like 1Add
    BLAST
    Domaini681 – 73151Collagen-like 2Add
    BLAST
    Domaini823 – 86543Collagen-like 3Add
    BLAST
    Domaini879 – 92749Collagen-like 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 555327Nonhelical region 1 (NC1)Add
    BLAST
    Regioni358 – 5551984 X tandem repeatsAdd
    BLAST
    Regioni556 – 57318Triple-helical region 1 (COL1)Add
    BLAST
    Regioni574 – 61845Nonhelical region 2 (NC2)Add
    BLAST
    Regioni619 – 732114Triple-helical region 2 (COL2)Add
    BLAST
    Regioni733 – 76331Nonhelical region 3 (NC3)Add
    BLAST
    Regioni764 – 79835Triple-helical region 3 (COL3)Add
    BLAST
    Regioni799 – 82224Nonhelical region 4 (NC4)Add
    BLAST
    Regioni823 – 86745Triple-helical region 4 (COL4)Add
    BLAST
    Regioni868 – 87811Nonhelical region 5 (NC5)Add
    BLAST
    Regioni879 – 94971Triple-helical region 5 (COL5)Add
    BLAST
    Regioni950 – 98334Nonhelical region 6 (NC6)Add
    BLAST
    Regioni984 – 101330Triple-helical region 6 (COL6)Add
    BLAST
    Regioni1014 – 102714Nonhelical region 7 (NC7)Add
    BLAST
    Regioni1028 – 104518Triple-helical region 7 (COL7)Add
    BLAST
    Regioni1046 – 10527Nonhelical region 8 (NC8)
    Regioni1053 – 110755Triple-helical region 8 (COL8)Add
    BLAST
    Regioni1108 – 111710Nonhelical region 9 (NC9)
    Regioni1118 – 113215Triple-helical region 9 (COL9)Add
    BLAST
    Regioni1133 – 1388256Nonhelical region 10 (NC10)Add
    BLAST

    Sequence similaritiesi

    Belongs to the multiplexin collagen family.Curated
    Contains 4 collagen-like domains.Curated
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231591.
    HOVERGENiHBG080337.
    InParanoidiP39059.
    KOiK08135.
    OMAiPELITFH.
    OrthoDBiEOG7NSB2B.
    PhylomeDBiP39059.
    TreeFamiTF315821.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01391. Collagen. 4 hits.
    PF06482. Endostatin. 2 hits.
    [Graphical view]
    SMARTiSM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P39059-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRRNNGQC WCLLMLLSVS TPLPAVTQTR GATETASQGH LDLTQLIGVP     50
    LPSSVSFVTG YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVVVKPS 100
    STRGGVLFAI TDAFQKVIYL GLRLSGVEDG HQRIILYYTE PGSHVSQEAA 150
    AFSVPVMTHR WNRFAMIVQG EEVTLLVNCE EHSRIPFQRS SQALAFESSA 200
    GIFMGNAGAT GLERFTGSLQ QLTVHPDPRT PEELCDPEES SASGETSGLQ 250
    EADGVAEILE AVTYTQASPK EAKVEPINTP PTPSSPFEDM ELSGEPVPEG 300
    TLETTNMSII QHSSPKQGSG EILNDTLEGV HSVDGDPITD SGSGAGAFLD 350
    IAEEKNLAAT AAGLAEVPIS TAGEAEASSV PTGGPTLSMS TENPEEGVTP 400
    GPDNEERLAA TAAGEAEALA SMPGEVEASG VAPGELDLSM SAQSLGEEAT 450
    VGPSSEDSLT TAAAATEVSL STFEDEEASG VPTDGLAPLT ATMAPERAVT 500
    SGPGDEEDLA AATTEEPLIT AGGEESGSPP PDGPPLPLPT VAPERWITPA 550
    QREHVGMKGQ AGPKGEKGDA GEELPGPPEP SGPVGPTAGA EAEGSGLGWG 600
    SDVGSGSGDL VGSEQLLRGP PGPPGPPGLP GIPGKPGTDV FMGPPGSPGE 650
    DGPAGEPGPP GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG 700
    LPGPPGKKGQ AGPPGVMGPP GPPGPPGPPG PGCTMGLGFE DTEGSGSTQL 750
    LNEPKLSRPT AAIGLKGEKG DRGPKGERGM DGASIVGPPG PRGPPGHIKV 800
    LSNSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR GPKGDTGLPG 850
    FPGLKGEQGE KGEPGAILTE DIPLERLMGK KGEPGMHGAP GPMGPKGPPG 900
    HKGEFGLPGR PGRPGLNGLK GTKGDPGVIM QGPPGLPGPP GPPGPPGAVI 950
    NIKGAIFPIP VRPHCKMPVD TAHPGSPELI TFHGVKGEKG SWGLPGSKGE 1000
    KGDQGAQGPP GPPLDLAYLR HFLNNLKGEN GDKGFKGEKG EKGDINGSFL 1050
    MSGPPGLPGN PGPAGQKGET VVGPQGPPGA PGLPGPPGFG RPGDPGPPGP 1100
    PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN MDDMLQKAHL 1150
    VIEGTFIYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ 1200
    LLPPPNPISS ANYEKPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY 1250
    RAFLSSHLQD LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNM 1300
    HIPIYSFDGR DIMTDPSWPQ KVIWHGSSPH GVRLVDNYCE AWRTADTAVT 1350
    GLASPLSTGK ILDQKAYSCA NRLIVLCIEN SFMTDARK 1388
    Length:1,388
    Mass (Da):141,720
    Last modified:July 5, 2005 - v2
    Checksum:iAF54DDCC136C3745
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101C → S in BAA04762. (PubMed:8307960)Curated
    Sequence conflicti49 – 491V → D in AAA58429. (PubMed:8106446)Curated
    Sequence conflicti94 – 952SV → RA in AAA58429. (PubMed:8106446)Curated
    Sequence conflicti94 – 952SV → RA in BAA04762. (PubMed:8307960)Curated
    Sequence conflicti150 – 1501A → P in AAA58429. (PubMed:8106446)Curated
    Sequence conflicti409 – 4091A → R in AAA58429. (PubMed:8106446)Curated
    Sequence conflicti409 – 4091A → R in AAC78500. (PubMed:9651385)Curated
    Sequence conflicti1134 – 11341L → LLGELIPIPADSPPPPALSS N in AAC78500. (PubMed:9651385)Curated
    Sequence conflicti1178 – 119720Missing in AAC78500. (PubMed:9651385)CuratedAdd
    BLAST
    Sequence conflicti1227 – 12271F → V in AAC78500. (PubMed:9651385)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti163 – 1631R → H.
    Corresponds to variant rs2075662 [ dbSNP | Ensembl ].
    VAR_033787
    Natural varianti204 – 2041M → V.1 Publication
    Corresponds to variant rs2075663 [ dbSNP | Ensembl ].
    VAR_033788
    Natural varianti391 – 3911T → M.
    Corresponds to variant rs10988532 [ dbSNP | Ensembl ].
    VAR_033789
    Natural varianti442 – 4421A → T.
    Corresponds to variant rs16918128 [ dbSNP | Ensembl ].
    VAR_033790
    Natural varianti446 – 4461G → R.
    Corresponds to variant rs35934703 [ dbSNP | Ensembl ].
    VAR_033791
    Natural varianti504 – 5041G → V.
    Corresponds to variant rs2297603 [ dbSNP | Ensembl ].
    VAR_048776
    Natural varianti506 – 5061E → D.
    Corresponds to variant rs35250850 [ dbSNP | Ensembl ].
    VAR_033792
    Natural varianti531 – 5311P → R.
    Corresponds to variant rs35529307 [ dbSNP | Ensembl ].
    VAR_033793
    Natural varianti705 – 7051P → L.
    Corresponds to variant rs41308900 [ dbSNP | Ensembl ].
    VAR_061114
    Natural varianti989 – 9891K → R.
    Corresponds to variant rs35642150 [ dbSNP | Ensembl ].
    VAR_033794
    Natural varianti1001 – 10011K → R.
    Corresponds to variant rs35544077 [ dbSNP | Ensembl ].
    VAR_033795
    Natural varianti1332 – 13321V → I.
    Corresponds to variant rs10519 [ dbSNP | Ensembl ].
    VAR_033796

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25286 mRNA. Translation: AAA58429.1.
    L25280
    , L25281, L25282, L25283, L25284, L25285, AF052956, AF052957, AF052958, AF052959, AF052960, AF052961, AF052962, AF052963, AF052964, AF052965, AF052966, AF052967, AF052968, AF052969, AF052970, AF052971, AF052972, AF052973, AF052974, AF052975 Genomic DNA. Translation: AAC78500.1.
    AL136084, AL354923 Genomic DNA. Translation: CAI17044.2.
    AL354923, AL136084 Genomic DNA. Translation: CAI12548.2.
    D21230 mRNA. Translation: BAA04762.1.
    L01697 mRNA. No translation available.
    CCDSiCCDS35081.1.
    PIRiA53317.
    RefSeqiNP_001846.3. NM_001855.4.
    UniGeneiHs.409034.

    Genome annotation databases

    EnsembliENST00000375001; ENSP00000364140; ENSG00000204291.
    GeneIDi1306.
    KEGGihsa:1306.
    UCSCiuc004azb.2. human.

    Polymorphism databases

    DMDMi68839886.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25286 mRNA. Translation: AAA58429.1 .
    L25280
    , L25281 , L25282 , L25283 , L25284 , L25285 , AF052956 , AF052957 , AF052958 , AF052959 , AF052960 , AF052961 , AF052962 , AF052963 , AF052964 , AF052965 , AF052966 , AF052967 , AF052968 , AF052969 , AF052970 , AF052971 , AF052972 , AF052973 , AF052974 , AF052975 Genomic DNA. Translation: AAC78500.1 .
    AL136084 , AL354923 Genomic DNA. Translation: CAI17044.2 .
    AL354923 , AL136084 Genomic DNA. Translation: CAI12548.2 .
    D21230 mRNA. Translation: BAA04762.1 .
    L01697 mRNA. No translation available.
    CCDSi CCDS35081.1.
    PIRi A53317.
    RefSeqi NP_001846.3. NM_001855.4.
    UniGenei Hs.409034.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N3F X-ray 2.00 A/B 1133-1186 [» ]
    ProteinModelPortali P39059.
    SMRi P39059. Positions 1133-1186, 1215-1382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107702. 2 interactions.
    IntActi P39059. 2 interactions.
    STRINGi 9606.ENSP00000364140.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P39059.

    Polymorphism databases

    DMDMi 68839886.

    Proteomic databases

    MaxQBi P39059.
    PaxDbi P39059.
    PRIDEi P39059.

    Protocols and materials databases

    DNASUi 1306.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375001 ; ENSP00000364140 ; ENSG00000204291 .
    GeneIDi 1306.
    KEGGi hsa:1306.
    UCSCi uc004azb.2. human.

    Organism-specific databases

    CTDi 1306.
    GeneCardsi GC09P101705.
    H-InvDB HIX0008227.
    HGNCi HGNC:2192. COL15A1.
    HPAi HPA017913.
    HPA017915.
    MIMi 120325. gene.
    neXtProti NX_P39059.
    PharmGKBi PA26708.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231591.
    HOVERGENi HBG080337.
    InParanoidi P39059.
    KOi K08135.
    OMAi PELITFH.
    OrthoDBi EOG7NSB2B.
    PhylomeDBi P39059.
    TreeFami TF315821.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi COL15A1. human.
    GeneWikii Collagen,_type_XV,_alpha_1.
    GenomeRNAii 1306.
    NextBioi 5345.
    PROi P39059.
    SOURCEi Search...

    Gene expression databases

    Bgeei P39059.
    CleanExi HS_COL15A1.
    Genevestigatori P39059.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01391. Collagen. 4 hits.
    PF06482. Endostatin. 2 hits.
    [Graphical view ]
    SMARTi SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the alpha 1 chain of human type XV collagen and exon-intron organization in the 3' region of the corresponding gene."
      Kivirikko S., Heinamaki P., Rehn M.V., Honkanen N., Myers J.C., Pihlajaniemi T.
      J. Biol. Chem. 269:4773-4779(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Umbilical cord.
    2. "Complete exon-intron organization of the human gene for the alpha1 chain of type XV collagen (COL15A1) and comparison with the homologous COL18A1 gene."
      Haegg P.M., Muona A., Lietard J., Kivirikko S., Pihlajaniemi T.
      J. Biol. Chem. 273:17824-17831(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen."
      Muragaki Y., Abe N., Ninomiya Y., Olsen B.R., Ooshima A.
      J. Biol. Chem. 269:4042-4046(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-569, VARIANT VAL-204.
      Tissue: Placenta.
    5. "Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region."
      Myers J.C., Kivirikko S., Gordon M.K., Dion A.S., Pihlajaniemi T.
      Proc. Natl. Acad. Sci. U.S.A. 89:10144-10148(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 544-1252.
    6. "Chromosomal assignment of a gene encoding a new collagen type (COL15A1) to 9q21 --> q22."
      Huebner K., Cannizzaro L.A., Jabs E.W., Kivirikko S., Manzone H., Pihlajaniemi T., Myers J.C.
      Genomics 14:220-224(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1145, CHROMOSOMAL LOCATION.
      Tissue: Placenta.
    7. "Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin."
      John H., Radtke K., Staendker L., Forssmann W.G.
      Biochim. Biophys. Acta 1747:161-170(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1198-1210; 1207-1219; 1213-1225 AND 1221-1233, IDENTIFICATION OF RESTIN-RELATED PEPTIDES, DISULFIDE BOND.
    8. "Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin."
      Ramchandran R., Dhanabal M., Volk R., Waterman M.J.F., Segal M., Lu H., Knebelmann B., Sukhatme V.P.
      Biochem. Biophys. Res. Commun. 255:735-739(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells."
      Li D., Clark C.C., Myers J.C.
      J. Biol. Chem. 275:22339-22347(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, INTERCHAIN DISULFIDE BONDS.
    10. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-265, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCOFA1_HUMAN
    AccessioniPrimary (citable) accession number: P39059
    Secondary accession number(s): Q5T6J4, Q9UDC5, Q9Y4W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 134 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

    Caution

    The name restin has also been used for CAP-Gly domain-containing linker protein 1 the product of the CLIP1 gene.Curated

    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