ID   TSP2_BOVIN              Reviewed;        1170 AA.
AC   Q95116; Q28180;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Thrombospondin-2;
DE   AltName: Full=Corticotropin-induced secreted protein;
DE            Short=CISP;
DE   Flags: Precursor;
GN   Name=THBS2; Synonyms=TSP-2, TSP2;
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].
RA   Danik M., Chinn A., Lafeuillade M., Keramidas M., Aguesse-Germon S.,
RA   Penhoat A., Chen H., Mosher D., Chambaz E.M., Feige J.J.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-522.
RX   PubMed=8698834;
RX   DOI=10.1002/(sici)1097-4652(199604)167:1<164::aid-jcp19>3.0.co;2-b;
RA   Lafeuillade B., Pellerin S., Keramidas M., Danik M., Chambaz E.M.,
RA   Feige J.J.;
RT   "Opposite regulation of thrombospondin-1 and corticotropin-induced secreted
RT   protein/thrombospondin-2 expression by adrenocorticotropic hormone in
RT   adrenocortical cells.";
RL   J. Cell. Physiol. 167:164-172(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 318-831.
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 (MAY-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). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. Can bind to fibrinogen,
CC       fibronectin, laminin and type V collagen. Interacts (via the TSP type I
CC       repeats) with CD36; the interaction conveys an antiangiogenic effect.
CC       Interacts (via the TSP type I repeats) with HRG; the interaction blocks
CC       the antiangiogenic effect of THBS2 with CD36 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X96540; CAA65385.1; -; mRNA.
DR   EMBL; X87620; CAA60952.1; -; mRNA.
DR   RefSeq; NP_789861.1; NM_176872.1.
DR   AlphaFoldDB; Q95116; -.
DR   SMR; Q95116; -.
DR   STRING; 9913.ENSBTAP00000071758; -.
DR   GlyCosmos; Q95116; 8 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000042078; -.
DR   GeneID; 338092; -.
DR   KEGG; bta:338092; -.
DR   CTD; 7058; -.
DR   eggNOG; ENOG502QRK8; Eukaryota.
DR   InParanoid; Q95116; -.
DR   OrthoDB; 5345349at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
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:SF10; THROMBOSPONDIN-2; 1.
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   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; Glycoprotein;
KW   Heparin-binding; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1170
FT                   /note="Thrombospondin-2"
FT                   /id="PRO_0000035845"
FT   DOMAIN          19..215
FT                   /note="Laminin G-like"
FT   DOMAIN          318..375
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          19..232
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          731..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..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        733..748
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..936
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        582
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        936
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1067
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        266
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        270
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        535
FT                   /note="A -> V (in Ref. 3; CAA60952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="S -> T (in Ref. 3; CAA60952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1170 AA;  129863 MW;  9CF1FBF55B89A051 CRC64;
     MLWPLLLLAL WAWPSAQAGD QDEDTAFDLF SISNINRKTI GAKQFRGPDP SVPAYRFVRF
     DYIPPVSAEH LGRITEAMRR KEGFFLTASM KQDRRSRGTL LALEGPGATH RQFEIVSNGP
     ADTLDLTYWV DGTQHVISLE DVGLADSQWK NVTVQVTGET YSLYVGCDLM DSFALDEPFY
     EHLQTERSRM YVTKGAARES HFRGLLQNVY LVFENSVEDL LSKKGCQQSQ GAETNAISEN
     TETLHLSPMV TMEHVGPSAE KSPEVCEHSC EELGSMIREL SGLHVIVNQL HENLRKVSND
     NQFLWELIGG PPKTRNVSAC WQDGRFFAEN ETWVVDSCTK CTCKKFKTVC HQISCPPATC
     ADPWFVEGEC CPSCVHDGEE GWSPWAEWTE CSATCGSGTQ QRGRSCDVTS NTCLGPSIQT
     RACSLGRCDH RIRQDGGWSH WSPWSSCSVT CGVGNVTRIR LCNSPVPQMG GRSCKGSGRE
     TKACQGPPCP VDGRWSPWSP WSACTVTCAG GIRERTRVCN SPEPQHGGKD CVGGAKEQQM
     CNRKSCPIDG CLSNPCFPGA ECSSFPDGSW SCGSCPGGFL GNGTHCEDLD ECAVVTDVCF
     ATSKAHRCVN TNPGYHCLPC PPRYKGNQPF GVGLEAARTE KQVCEPENPC KDKTHSCHRH
     AECIYLGHFS DPMYKCECQT GYAGDGLICG EDSDLDGWPN KNLVCATNAT YHCVKDNCPL
     LPNSGQEDFD KDGIGDACDD DDDNDGVSDE KDNCQLLFNP RQFDYDKDEV GDRCDNCPYV
     HNPAQIDTDN NGEGDACSVD IDGDDVFNER DNCPYVYNTD QRDTDGDGVG DHCDNCPLVH
     NPDQTDVDND LVGDQCDNNE DIDEDGHQNN QDNCPHIPNA NQADHDRDGQ GDACDSDDDN
     DGIPDDRDNC RLVANPDQED SDGDRRGDAC KDDFDNDSIP DIDDVCPENN AISETDFRNF
     QMVHLDPKGT TQIDPNWVIR HQGKELVQTA NSDPGIAVGF DEFGSVDFSG TFYVNTDRDD
     DYAGFVFGYQ SSSRFYVVMW KQVTQTYWED QPTRAYGYSG VSLKVVNSTT GTGEHLRNAL
     WHTGNTEGQV RTLWHDPKNI GWKDYTAYRW HLTHRPKTGY IRVLVHEGKQ VMADSGPIYD
     QTYAGGRLGL FVFSQEMVYF SDLKYECRDV
//