TSP1_XENLA
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 25-MAY-2022, entry version 127.
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 PRIDE; P35448; -.
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:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix 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:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 4.10.1080.10; -; 2.
DR InterPro; IPR026823; cEGF.
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; IPR001791; Laminin_G.
DR InterPro; IPR028499; Thrombospondin-1.
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; IPR001007; VWF_dom.
DR PANTHER; PTHR10199:SF78; PTHR10199:SF78; 1.
DR Pfam; PF12662; cEGF; 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 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; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF82895; SSF82895; 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
