ID   TSP1_XENLA              Reviewed;        1173 AA.
AC   P35448;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Thrombospondin-1;
DE   AltName: Full=Glycoprotein G {ECO:0000250|UniProtKB:P07996};
DE   Flags: Precursor;
GN   Name=thbs1; Synonyms=tsp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Urry L.A., Ramos J., Duquette M., Desimone D.W., Lawler J.;
RT   "Cloning, characterization and expression of thrombospondin-1 in Xenopus
RT   laevis embryos.";
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC       matrix interactions. Can bind to fibrinogen, fibronectin, laminin, type
CC       V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-
CC       IIb/beta-3 (By similarity). May play a role in ER stress response (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07996}. Cell
CC       surface {ECO:0000250|UniProtKB:P07996}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:P07996}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:P35441}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P35441}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR   EMBL; L04278; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P35448; -.
DR   SMR; P35448; -.
DR   GlyCosmos; P35448; 7 sites, No reported glycans.
DR   AGR; Xenbase:XB-GENE-6253120; -.
DR   Xenbase; XB-GENE-6253120; thbs1.S.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR   Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 6.
DR   Pfam; PF05735; TSP_C; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00209; TSP1; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal;
KW   Unfolded protein response.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1173
FT                   /note="Thrombospondin-1"
FT                   /id="PRO_0000035844"
FT   DOMAIN          22..224
FT                   /note="Laminin G-like"
FT   DOMAIN          319..376
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          382..432
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          438..493
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          495..550
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          550..590
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          649..693
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          694..729
FT                   /note="TSP type-3 1"
FT   REPEAT          730..765
FT                   /note="TSP type-3 2"
FT   REPEAT          766..788
FT                   /note="TSP type-3 3"
FT   REPEAT          789..824
FT                   /note="TSP type-3 4"
FT   REPEAT          825..847
FT                   /note="TSP type-3 5"
FT   REPEAT          848..885
FT                   /note="TSP type-3 6"
FT   REPEAT          886..921
FT                   /note="TSP type-3 7"
FT   REPEAT          922..957
FT                   /note="TSP type-3 8"
FT   DOMAIN          961..1173
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT   REGION          50..98
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          838..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           929..931
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        844..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..900
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        705
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        711
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1070
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        174..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        398..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        409..416
FT                   /evidence="ECO:0000250"
FT   DISULFID        450..487
FT                   /evidence="ECO:0000250"
FT   DISULFID        454..492
FT                   /evidence="ECO:0000250"
FT   DISULFID        465..477
FT                   /evidence="ECO:0000250"
FT   DISULFID        507..544
FT                   /evidence="ECO:0000250"
FT   DISULFID        511..549
FT                   /evidence="ECO:0000250"
FT   DISULFID        522..534
FT                   /evidence="ECO:0000250"
FT   DISULFID        554..565
FT                   /evidence="ECO:0000250"
FT   DISULFID        559..575
FT                   /evidence="ECO:0000250"
FT   DISULFID        578..589
FT                   /evidence="ECO:0000250"
FT   DISULFID        595..611
FT                   /evidence="ECO:0000250"
FT   DISULFID        602..620
FT                   /evidence="ECO:0000250"
FT   DISULFID        623..647
FT                   /evidence="ECO:0000250"
FT   DISULFID        653..666
FT                   /evidence="ECO:0000250"
FT   DISULFID        660..679
FT                   /evidence="ECO:0000250"
FT   DISULFID        681..692
FT                   /evidence="ECO:0000250"
FT   DISULFID        708..716
FT                   /evidence="ECO:0000250"
FT   DISULFID        721..741
FT                   /evidence="ECO:0000250"
FT   DISULFID        757..777
FT                   /evidence="ECO:0000250"
FT   DISULFID        780..800
FT                   /evidence="ECO:0000250"
FT   DISULFID        816..836
FT                   /evidence="ECO:0000250"
FT   DISULFID        839..859
FT                   /evidence="ECO:0000250"
FT   DISULFID        877..897
FT                   /evidence="ECO:0000250"
FT   DISULFID        913..933
FT                   /evidence="ECO:0000250"
FT   DISULFID        949..1170
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1173 AA;  130020 MW;  A9F036D6516C0F24 CRC64;
     MKGIFLLLML VMPQTHQAAE SGNDDNSVFD LFELTGYNRK AGSRKPQGLH LVKGPDPSSP
     AYRIEDADLI PPLPEDKFQD LLDAIRADRG FILLATLRQA KKSRGALLSV ERKDGGGHIF
     SLISNGRART LDLSLSGERK QQVVSVEDAV LATGNWTNIT LFVQEDRAQL YVGCNKMENA
     ELDVPIQKIF TENLASTAHL RVAKGGVKDN FQGVLQNVRF VFGTTLEAIL RNKGCLSMTN
     SVITLDNPVN GSSPAIRTNY IGHKTKDLQA VCGFSCDDLS KLFAEMKGLR TLVTTLKDQV
     TKETEKNELI AQIVTRTPGV CLHNGVLHKN RDEWTVDSCT ECTCQNSATI CRKVSCPLMP
     CTNATIPDGE CCPRCWPSDS ADDDWSPWSD WTPCSVTCGH GIQQRGRSCD SLNNPCEGSS
     VQTRSCQIQD CDKRFKQDGG WSHWSPWSSC SVTCGSGQIT RIRLCNSPVP QLNGKQCEGE
     GRENKPCQKD PCPINGQWGP WSLWDTCTVT CGGGMQKRER LCNNPKPQYE GKDCIGEPTD
     SQICNKQDCP IDGCLSNPCF AGVKCTSFID GSWKCGSCPP GYRGNGITCK DIDECKEVPD
     ACFTLNGVHR CENTEPGYNC LPCPPRFTGT QPFGKGIEEA KANKQVCKPR NPCADGTHDC
     HKNARCIYLG HYSDPMFRCE CRPGYAGNGI ICGEDTDLDG WPNENLTCVD NATYHCLKDN
     CPNLPNSGQE DYDKDGMGDA CDKDDDNDGI LDDRDNCQFV YNPAQYDYDR DDVGDRCDNC
     PYNHNPDQAD TDRNGEGDAC SVDIDGDGIL NERDNCAYVY NVDQKDTDKD GVGDQCDNCP
     LEHNPEQTDS DSDLIGDKCD NNQDIDEDGH QNNLDNCPYI PNANQADHDK DGKGDACDHD
     DDNDGVPDDK DNCRLVPNPD QTDTNGDGRG DACQYDFDDD SIPDAEDVCP ENVEISTTDF
     RKFQMVPLDP KGTSQIDPNW VVRHQGKELV QTVNCDPGIA VGFDEFSAVD FSGTFFINTE
     RDDDYAGFVF GYQSSSRFYV VMWKQITQTY WDTTPTVAQG YSGLSIKVVN STSGPGEHLR
     NALWHTGNTP GQVRTLWHDP HQKGWKDFTA YRWHLTHRPK TGFIRVVMYE GKRVMADSGP
     IYDKTYAGGR LGLFVFSQEM VFFSDLKYEC RDS
//