TSP1_BOVIN
ID TSP1_BOVIN Reviewed; 1170 AA.
AC Q28178; Q28179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Thrombospondin-1;
DE AltName: Full=Glycoprotein G {ECO:0000250|UniProtKB:P07996};
DE Flags: Precursor;
GN Name=THBS1; Synonyms=TSP-1, TSP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Holstein; TISSUE=Tooth;
RX PubMed=9507054; DOI=10.1016/s0167-4838(97)00188-x;
RA Ueno A., Yamashita K., Nagata T., Tsurumi C., Miwa Y., Kitamura S.,
RA Inoue H.;
RT "cDNA cloning of bovine thrombospondin 1 and its expression in odontoblasts
RT and predentin.";
RL Biochim. Biophys. Acta 1382:17-22(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-18 AND 710-1170.
RC TISSUE=Aortic endothelium;
RA Zafar R.S., Moll Y.D., Womack J.F., Walz D.A.;
RT "Cloning and sequencing of bovine thrombospondin stimulatory effect of TGF-
RT beta.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Ligand for CD36 mediating antiangiogenic
CC properties (By similarity). May play a role in dentinogenesis and/or
CC maintenance of dentin and dental pulp. Plays a role in ER stress
CC response, via its interaction with the activating transcription factor
CC 6 alpha (ATF6) which produces adaptive ER stress response factors (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (By similarity). Can bind to
CC fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-
CC V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Interacts
CC (via the TSP type I repeats) with CD36; the interaction conveys an
CC antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG;
CC the interaction blocks the antiangiogenic effect of THBS1 with CD36 (By
CC similarity). Interacts with ATF6 (via lumenal domain) (By similarity).
CC Interacts with FN1; this interaction is enhanced by TNFAIP6, which may
CC act as a bridging molecule between FN1 and THBS1. {ECO:0000250,
CC ECO:0000250|UniProtKB:P07996}.
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}. Note=Secreted by thrombin-activated
CC platelets and binds to the cell surface in the presence of
CC extracellular Ca(2+). Incorporated into the extracellular matrix of
CC fibroblasts. Also detected in the endoplasmic reticulum and
CC sarcoplasmic reticulum where it plays a role in the ER stress response.
CC {ECO:0000250|UniProtKB:P07996, ECO:0000250|UniProtKB:P35441}.
CC -!- TISSUE SPECIFICITY: Odontoblasts. {ECO:0000269|PubMed:9507054}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; AB005287; BAA21115.1; -; mRNA.
DR EMBL; X87618; CAA60950.1; -; mRNA.
DR EMBL; X87619; CAA60951.1; -; mRNA.
DR PIR; S55501; S55501.
DR RefSeq; NP_776621.1; NM_174196.1.
DR AlphaFoldDB; Q28178; -.
DR SMR; Q28178; -.
DR ComplexPortal; CPX-4107; Thrombospondin 1 complex.
DR IntAct; Q28178; 1.
DR STRING; 9913.ENSBTAP00000002600; -.
DR GlyConnect; 593; 2 O-Linked glycans.
DR PaxDb; Q28178; -.
DR PeptideAtlas; Q28178; -.
DR PRIDE; Q28178; -.
DR GeneID; 281530; -.
DR KEGG; bta:281530; -.
DR CTD; 7057; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; Q28178; -.
DR OrthoDB; 120983at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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:0001968; F:fibronectin binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
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; 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; 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:0000250"
FT CHAIN 19..1170
FT /note="Thrombospondin-1"
FT /id="PRO_0000035841"
FT DOMAIN 65..270
FT /note="Laminin G-like"
FT DOMAIN 316..373
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 379..429
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 435..490
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 492..547
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 547..587
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 646..690
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 691..726
FT /note="TSP type-3 1"
FT REPEAT 727..762
FT /note="TSP type-3 2"
FT REPEAT 763..785
FT /note="TSP type-3 3"
FT REPEAT 786..821
FT /note="TSP type-3 4"
FT REPEAT 822..844
FT /note="TSP type-3 5"
FT REPEAT 845..882
FT /note="TSP type-3 6"
FT REPEAT 883..918
FT /note="TSP type-3 7"
FT REPEAT 919..954
FT /note="TSP type-3 8"
FT DOMAIN 958..1170
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 47..95
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 839..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 926..928
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 841..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1085
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..232
FT /evidence="ECO:0000250"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 274
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 391..423
FT /evidence="ECO:0000250"
FT DISULFID 395..428
FT /evidence="ECO:0000250"
FT DISULFID 406..413
FT /evidence="ECO:0000250"
FT DISULFID 447..484
FT /evidence="ECO:0000250"
FT DISULFID 451..489
FT /evidence="ECO:0000250"
FT DISULFID 462..474
FT /evidence="ECO:0000250"
FT DISULFID 504..541
FT /evidence="ECO:0000250"
FT DISULFID 508..546
FT /evidence="ECO:0000250"
FT DISULFID 519..531
FT /evidence="ECO:0000250"
FT DISULFID 551..562
FT /evidence="ECO:0000250"
FT DISULFID 556..572
FT /evidence="ECO:0000250"
FT DISULFID 575..586
FT /evidence="ECO:0000250"
FT DISULFID 592..608
FT /evidence="ECO:0000250"
FT DISULFID 599..617
FT /evidence="ECO:0000250"
FT DISULFID 620..644
FT /evidence="ECO:0000250"
FT DISULFID 650..663
FT /evidence="ECO:0000250"
FT DISULFID 657..676
FT /evidence="ECO:0000250"
FT DISULFID 678..689
FT /evidence="ECO:0000250"
FT DISULFID 705..713
FT /evidence="ECO:0000250"
FT DISULFID 718..738
FT /evidence="ECO:0000250"
FT DISULFID 754..774
FT /evidence="ECO:0000250"
FT DISULFID 777..797
FT /evidence="ECO:0000250"
FT DISULFID 813..833
FT /evidence="ECO:0000250"
FT DISULFID 836..856
FT /evidence="ECO:0000250"
FT DISULFID 874..894
FT /evidence="ECO:0000250"
FT DISULFID 910..930
FT /evidence="ECO:0000250"
FT DISULFID 946..1167
FT /evidence="ECO:0000250"
FT CONFLICT 805
FT /note="S -> G (in Ref. 2; CAA60950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1170 AA; 129534 MW; 0DD6ADF3E5FA031A CRC64;
MGLAWGLGVL LLLHACGSNR IPESGGDNSV FDIFELTGAA RKRSGRRLVK GPDPSSPAFR
IEDANLIPPV PDKKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLAVERK DHSGQVFSVI
SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD
VPIQSIFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVFV
TLDNNVVNGS SPAIRTDYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK
VTEENKELAN ELRRPPLCYH NGVQYRTGDE WTVDSCTECR CQNSVTICKK VSCPIMPCSN
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSVTCGNGIQ QRGRSCDSLN NRCEGSSVQT
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGKARE
TKACQKDSCP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPKPQFGGKD CVGDVTENQI
CNKQDCPIDG CLSNPCFAGV QCTSYPDGSW KCGACPPGYS GDGVECKDVD ECKEVPDACF
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GRGVEHATAN KQVCKPRNPC TDGTHDCNKN
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN EDLLCVANAT YHCRKDNCPN
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
HNPDQADTDN NGEGDACAAD IDGDSILNER DNCQYVYNVD QKDTDMDGVG DQCDNCPLEH
NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDQDKVP DIDDICPENV DISETDFRRF
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
WHTGNTSGQV RTLWHDPRHI GWKDFTAYRW HLSHRPKTGF IRVVMYEGKK IMADSGPIYD
KTYAGGRLGL FVFSQEMVFF SDLKYECRDS
