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Database: UniProt
Entry: P35448
LinkDB: P35448
Original site: P35448 
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   18-JUL-2018, entry version 119.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
RT   Xenopus laevis embryos.";
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and
CC       cell-to-matrix interactions. Can bind to fibrinogen, fibronectin,
CC       laminin, type V collagen and integrins alpha-V/beta-1, alpha-
CC       V/beta-3 and alpha-IIb/beta-3 (By similarity). May play a role in
CC       ER stress response (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07996}.
CC       Cell surface {ECO:0000250|UniProtKB:P07996}. Secreted,
CC       extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:P07996}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P35441}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P35441}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
DR   EMBL; L04278; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniGene; Xl.57138; -.
DR   ProteinModelPortal; P35448; -.
DR   SMR; P35448; -.
DR   PRIDE; P35448; -.
DR   Xenbase; XB-GENE-865586; thbs1.
DR   HOVERGEN; HBG018006; -.
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:0006954; P:inflammatory response; IEA:InterPro.
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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR037349; Thrombospondin.
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; PTHR10199; 2.
DR   PANTHER; PTHR10199:SF78; PTHR10199:SF78; 2.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 7.
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;
KW   Heparin-binding; Repeat; Sarcoplasmic reticulum; Secreted; Signal;
KW   Unfolded protein response.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1173       Thrombospondin-1.
FT                                /FTId=PRO_0000035844.
FT   DOMAIN       22    224       Laminin G-like.
FT   DOMAIN      319    376       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      382    432       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      438    493       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      495    550       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      550    590       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      649    693       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      694    729       TSP type-3 1.
FT   REPEAT      730    765       TSP type-3 2.
FT   REPEAT      766    788       TSP type-3 3.
FT   REPEAT      789    824       TSP type-3 4.
FT   REPEAT      825    847       TSP type-3 5.
FT   REPEAT      848    885       TSP type-3 6.
FT   REPEAT      886    921       TSP type-3 7.
FT   REPEAT      922    957       TSP type-3 8.
FT   DOMAIN      961   1173       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION       50     98       Heparin-binding. {ECO:0000250}.
FT   MOTIF       929    931       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    250    250       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    705    705       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    711    711       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1070   1070       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    174    235       {ECO:0000250}.
FT   DISULFID    394    426       {ECO:0000250}.
FT   DISULFID    398    431       {ECO:0000250}.
FT   DISULFID    409    416       {ECO:0000250}.
FT   DISULFID    450    487       {ECO:0000250}.
FT   DISULFID    454    492       {ECO:0000250}.
FT   DISULFID    465    477       {ECO:0000250}.
FT   DISULFID    507    544       {ECO:0000250}.
FT   DISULFID    511    549       {ECO:0000250}.
FT   DISULFID    522    534       {ECO:0000250}.
FT   DISULFID    554    565       {ECO:0000250}.
FT   DISULFID    559    575       {ECO:0000250}.
FT   DISULFID    578    589       {ECO:0000250}.
FT   DISULFID    595    611       {ECO:0000250}.
FT   DISULFID    602    620       {ECO:0000250}.
FT   DISULFID    623    647       {ECO:0000250}.
FT   DISULFID    653    666       {ECO:0000250}.
FT   DISULFID    660    679       {ECO:0000250}.
FT   DISULFID    681    692       {ECO:0000250}.
FT   DISULFID    708    716       {ECO:0000250}.
FT   DISULFID    721    741       {ECO:0000250}.
FT   DISULFID    757    777       {ECO:0000250}.
FT   DISULFID    780    800       {ECO:0000250}.
FT   DISULFID    816    836       {ECO:0000250}.
FT   DISULFID    839    859       {ECO:0000250}.
FT   DISULFID    877    897       {ECO:0000250}.
FT   DISULFID    913    933       {ECO:0000250}.
FT   DISULFID    949   1170       {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
//
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