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P35448

- TSP1_XENLA

UniProt

P35448 - TSP1_XENLA

Protein

Thrombospondin-1

Gene

thbs1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3 By similarity. May play a role in ER stress response By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. extracellular matrix binding Source: InterPro
    3. heparin binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. inflammatory response Source: InterPro
    3. negative regulation of angiogenesis Source: InterPro
    4. response to unfolded protein Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Unfolded protein response

    Keywords - Ligandi

    Calcium, Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thrombospondin-1
    Gene namesi
    Name:thbs1
    Synonyms:tsp1
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-865586. thbs1.

    Subcellular locationi

    Endoplasmic reticulum By similarity. Sarcoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. extracellular space Source: InterPro
    3. sarcoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 11731155Thrombospondin-1PRO_0000035844Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi174 ↔ 235By similarity
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi394 ↔ 426By similarity
    Disulfide bondi398 ↔ 431By similarity
    Disulfide bondi409 ↔ 416By similarity
    Disulfide bondi450 ↔ 487By similarity
    Disulfide bondi454 ↔ 492By similarity
    Disulfide bondi465 ↔ 477By similarity
    Disulfide bondi507 ↔ 544By similarity
    Disulfide bondi511 ↔ 549By similarity
    Disulfide bondi522 ↔ 534By similarity
    Disulfide bondi554 ↔ 565By similarity
    Disulfide bondi559 ↔ 575By similarity
    Disulfide bondi578 ↔ 589By similarity
    Disulfide bondi595 ↔ 611By similarity
    Disulfide bondi602 ↔ 620By similarity
    Disulfide bondi623 ↔ 647By similarity
    Disulfide bondi653 ↔ 666By similarity
    Disulfide bondi660 ↔ 679By similarity
    Disulfide bondi681 ↔ 692By similarity
    Glycosylationi705 – 7051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi708 ↔ 716By similarity
    Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi721 ↔ 741By similarity
    Disulfide bondi757 ↔ 777By similarity
    Disulfide bondi780 ↔ 800By similarity
    Disulfide bondi816 ↔ 836By similarity
    Disulfide bondi839 ↔ 859By similarity
    Disulfide bondi877 ↔ 897By similarity
    Disulfide bondi913 ↔ 933By similarity
    Disulfide bondi949 ↔ 1170By similarity
    Glycosylationi1070 – 10701N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotrimer; disulfide-linked.

    Structurei

    3D structure databases

    ProteinModelPortaliP35448.
    SMRiP35448. Positions 25-235, 552-1172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 224203Laminin G-likeAdd
    BLAST
    Domaini319 – 37658VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini382 – 43251TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 49356TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini495 – 55056TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini550 – 59041EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini649 – 69345EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati694 – 72936TSP type-3 1Add
    BLAST
    Repeati730 – 76536TSP type-3 2Add
    BLAST
    Repeati766 – 78823TSP type-3 3Add
    BLAST
    Repeati789 – 82436TSP type-3 4Add
    BLAST
    Repeati825 – 84723TSP type-3 5Add
    BLAST
    Repeati848 – 88538TSP type-3 6Add
    BLAST
    Repeati886 – 92136TSP type-3 7Add
    BLAST
    Repeati922 – 95736TSP type-3 8Add
    BLAST
    Domaini961 – 1173213TSP C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 9849Heparin-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi929 – 9313Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the thrombospondin family.Curated
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated
    Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
    Contains 3 TSP type-1 domains.PROSITE-ProRule annotation
    Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    HOVERGENiHBG018006.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    4.10.1080.10. 2 hits.
    InterProiIPR026823. cEGF.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR001791. Laminin_G.
    IPR028499. Thrombospondin-1.
    IPR000884. Thrombospondin_1_rpt.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR017897. Thrombospondin_3_rpt.
    IPR008859. Thrombospondin_C.
    IPR028974. TSP_type-3_rpt.
    IPR001007. VWF_C.
    [Graphical view]
    PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
    PfamiPF12662. cEGF. 1 hit.
    PF12947. EGF_3. 1 hit.
    PF00090. TSP_1. 3 hits.
    PF02412. TSP_3. 7 hits.
    PF05735. TSP_C. 1 hit.
    PF00093. VWC. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 2 hits.
    SM00209. TSP1. 3 hits.
    SM00210. TSPN. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    SUPFAMiSSF103647. SSF103647. 3 hits.
    SSF49899. SSF49899. 2 hits.
    SSF82895. SSF82895. 3 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS50092. TSP1. 3 hits.
    PS51234. TSP3. 8 hits.
    PS51236. TSP_CTER. 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.

    P35448-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGIFLLLML VMPQTHQAAE SGNDDNSVFD LFELTGYNRK AGSRKPQGLH     50
    LVKGPDPSSP AYRIEDADLI PPLPEDKFQD LLDAIRADRG FILLATLRQA 100
    KKSRGALLSV ERKDGGGHIF SLISNGRART LDLSLSGERK QQVVSVEDAV 150
    LATGNWTNIT LFVQEDRAQL YVGCNKMENA ELDVPIQKIF TENLASTAHL 200
    RVAKGGVKDN FQGVLQNVRF VFGTTLEAIL RNKGCLSMTN SVITLDNPVN 250
    GSSPAIRTNY IGHKTKDLQA VCGFSCDDLS KLFAEMKGLR TLVTTLKDQV 300
    TKETEKNELI AQIVTRTPGV CLHNGVLHKN RDEWTVDSCT ECTCQNSATI 350
    CRKVSCPLMP CTNATIPDGE CCPRCWPSDS ADDDWSPWSD WTPCSVTCGH 400
    GIQQRGRSCD SLNNPCEGSS VQTRSCQIQD CDKRFKQDGG WSHWSPWSSC 450
    SVTCGSGQIT RIRLCNSPVP QLNGKQCEGE GRENKPCQKD PCPINGQWGP 500
    WSLWDTCTVT CGGGMQKRER LCNNPKPQYE GKDCIGEPTD SQICNKQDCP 550
    IDGCLSNPCF AGVKCTSFID GSWKCGSCPP GYRGNGITCK DIDECKEVPD 600
    ACFTLNGVHR CENTEPGYNC LPCPPRFTGT QPFGKGIEEA KANKQVCKPR 650
    NPCADGTHDC HKNARCIYLG HYSDPMFRCE CRPGYAGNGI ICGEDTDLDG 700
    WPNENLTCVD NATYHCLKDN CPNLPNSGQE DYDKDGMGDA CDKDDDNDGI 750
    LDDRDNCQFV YNPAQYDYDR DDVGDRCDNC PYNHNPDQAD TDRNGEGDAC 800
    SVDIDGDGIL NERDNCAYVY NVDQKDTDKD GVGDQCDNCP LEHNPEQTDS 850
    DSDLIGDKCD NNQDIDEDGH QNNLDNCPYI PNANQADHDK DGKGDACDHD 900
    DDNDGVPDDK DNCRLVPNPD QTDTNGDGRG DACQYDFDDD SIPDAEDVCP 950
    ENVEISTTDF RKFQMVPLDP KGTSQIDPNW VVRHQGKELV QTVNCDPGIA 1000
    VGFDEFSAVD FSGTFFINTE RDDDYAGFVF GYQSSSRFYV VMWKQITQTY 1050
    WDTTPTVAQG YSGLSIKVVN STSGPGEHLR NALWHTGNTP GQVRTLWHDP 1100
    HQKGWKDFTA YRWHLTHRPK TGFIRVVMYE GKRVMADSGP IYDKTYAGGR 1150
    LGLFVFSQEM VFFSDLKYEC RDS 1173
    Length:1,173
    Mass (Da):130,020
    Last modified:June 1, 1994 - v1
    Checksum:iA9F036D6516C0F24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04278 mRNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04278 mRNA. No translation available.

    3D structure databases

    ProteinModelPortali P35448.
    SMRi P35448. Positions 25-235, 552-1172.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-865586. thbs1.

    Phylogenomic databases

    HOVERGENi HBG018006.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    4.10.1080.10. 2 hits.
    InterProi IPR026823. cEGF.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR001791. Laminin_G.
    IPR028499. Thrombospondin-1.
    IPR000884. Thrombospondin_1_rpt.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR017897. Thrombospondin_3_rpt.
    IPR008859. Thrombospondin_C.
    IPR028974. TSP_type-3_rpt.
    IPR001007. VWF_C.
    [Graphical view ]
    PANTHERi PTHR10199:SF78. PTHR10199:SF78. 1 hit.
    Pfami PF12662. cEGF. 1 hit.
    PF12947. EGF_3. 1 hit.
    PF00090. TSP_1. 3 hits.
    PF02412. TSP_3. 7 hits.
    PF05735. TSP_C. 1 hit.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 2 hits.
    SM00209. TSP1. 3 hits.
    SM00210. TSPN. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103647. SSF103647. 3 hits.
    SSF49899. SSF49899. 2 hits.
    SSF82895. SSF82895. 3 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS50092. TSP1. 3 hits.
    PS51234. TSP3. 8 hits.
    PS51236. TSP_CTER. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization and expression of thrombospondin-1 in Xenopus laevis embryos."
      Urry L.A., Ramos J., Duquette M., Desimone D.W., Lawler J.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiTSP1_XENLA
    AccessioniPrimary (citable) accession number: P35448
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3