TSP2_BOVIN
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 25-MAY-2022, entry version 148.
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}.
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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.ENSBTAP00000042078; -.
DR PaxDb; Q95116; -.
DR GeneID; 338092; -.
DR KEGG; bta:338092; -.
DR CTD; 7058; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; Q95116; -.
DR OrthoDB; 120983at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:InterPro.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR001791; Laminin_G.
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:SF10; PTHR10199:SF10; 1.
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; 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
