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Database: UniProt
Entry: Q95116
LinkDB: Q95116
Original site: Q95116 
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   13-FEB-2019, entry version 140.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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>3.3.CO;2-0;
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
RT   secreted protein/thrombospondin-2 expression by adrenocorticotropic
RT   hormone in 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
RT   TGF-beta.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and
CC       cell-to-matrix interactions. Ligand for CD36 mediating
CC       antiangiogenic 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
CC       type I repeats) with CD36; the interaction conveys an
CC       antiangiogenic effect. Interacts (via the TSP type I repeats) with
CC       HRG; the interaction blocks the antiangiogenic effect of THBS2
CC       with CD36 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
DR   EMBL; X96540; CAA65385.1; -; mRNA.
DR   EMBL; X87620; CAA60952.1; -; mRNA.
DR   RefSeq; NP_789861.1; NM_176872.1.
DR   UniGene; Bt.5522; -.
DR   ProteinModelPortal; Q95116; -.
DR   SMR; Q95116; -.
DR   STRING; 9913.ENSBTAP00000042078; -.
DR   PaxDb; Q95116; -.
DR   PRIDE; Q95116; -.
DR   GeneID; 338092; -.
DR   KEGG; bta:338092; -.
DR   CTD; 7058; -.
DR   eggNOG; ENOG410IFQQ; Eukaryota.
DR   eggNOG; ENOG410XQKE; LUCA.
DR   HOGENOM; HOG000007542; -.
DR   HOVERGEN; HBG018006; -.
DR   InParanoid; Q95116; -.
DR   KO; K04659; -.
DR   OrthoDB; 120983at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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; 2.20.100.10; -; 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; 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; IPR015455; TSP2.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR10199; PTHR10199; 2.
DR   PANTHER; PTHR10199:SF10; PTHR10199:SF10; 2.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Heparin-binding; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1170       Thrombospondin-2.
FT                                /FTId=PRO_0000035845.
FT   DOMAIN       19    215       Laminin G-like.
FT   DOMAIN      318    375       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      379    429       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      435    490       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      492    547       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      547    587       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      646    690       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      691    726       TSP type-3 1.
FT   REPEAT      727    762       TSP type-3 2.
FT   REPEAT      763    785       TSP type-3 3.
FT   REPEAT      786    821       TSP type-3 4.
FT   REPEAT      822    844       TSP type-3 5.
FT   REPEAT      845    882       TSP type-3 6.
FT   REPEAT      883    918       TSP type-3 7.
FT   REPEAT      919    954       TSP type-3 8.
FT   DOMAIN      958   1170       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION       19    232       Heparin-binding. {ECO:0000255}.
FT   MOTIF       926    928       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    316    316       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    582    582       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    708    708       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    936    936       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    266    266       Interchain. {ECO:0000305}.
FT   DISULFID    270    270       Interchain. {ECO:0000305}.
FT   DISULFID    391    423       {ECO:0000250}.
FT   DISULFID    395    428       {ECO:0000250}.
FT   DISULFID    406    413       {ECO:0000250}.
FT   DISULFID    447    484       {ECO:0000250}.
FT   DISULFID    451    489       {ECO:0000250}.
FT   DISULFID    462    474       {ECO:0000250}.
FT   DISULFID    504    541       {ECO:0000250}.
FT   DISULFID    508    546       {ECO:0000250}.
FT   DISULFID    519    531       {ECO:0000250}.
FT   DISULFID    551    562       {ECO:0000250}.
FT   DISULFID    556    572       {ECO:0000250}.
FT   DISULFID    575    586       {ECO:0000250}.
FT   DISULFID    592    608       {ECO:0000250}.
FT   DISULFID    599    617       {ECO:0000250}.
FT   DISULFID    620    644       {ECO:0000250}.
FT   DISULFID    650    663       {ECO:0000250}.
FT   DISULFID    657    676       {ECO:0000250}.
FT   DISULFID    678    689       {ECO:0000250}.
FT   DISULFID    705    713       {ECO:0000250}.
FT   DISULFID    718    738       {ECO:0000250}.
FT   DISULFID    754    774       {ECO:0000250}.
FT   DISULFID    777    797       {ECO:0000250}.
FT   DISULFID    813    833       {ECO:0000250}.
FT   DISULFID    836    856       {ECO:0000250}.
FT   DISULFID    874    894       {ECO:0000250}.
FT   DISULFID    910    930       {ECO:0000250}.
FT   DISULFID    946   1167       {ECO:0000250}.
FT   CONFLICT    535    535       A -> V (in Ref. 3; CAA60952).
FT                                {ECO:0000305}.
FT   CONFLICT    748    748       S -> T (in Ref. 3; CAA60952).
FT                                {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
//
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