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Database: UniProt
Entry: A0A2K6KTD3_RHIBE
LinkDB: A0A2K6KTD3_RHIBE
Original site: A0A2K6KTD3_RHIBE 
ID   A0A2K6KTD3_RHIBE        Unreviewed;      1081 AA.
AC   A0A2K6KTD3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSRBIP00000014520.1};
GN   Name=THBS2 {ECO:0000313|Ensembl:ENSRBIP00000014520.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000014520.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000014520.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000014520.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the thrombospondin family.
CC       {ECO:0000256|ARBA:ARBA00009456}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A2K6KTD3; -.
DR   STRING; 61621.ENSRBIP00000014520; -.
DR   Ensembl; ENSRBIT00000038354.1; ENSRBIP00000014520.1; ENSRBIG00000031348.1.
DR   GeneTree; ENSGT00940000157846; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:Ensembl.
DR   Gene3D; 2.60.120.200; -; 3.
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; 6.
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; 4.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1081
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014432383"
FT   DOMAIN          318..375
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          549..589
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          648..692
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          729..764
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          788..823
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          885..920
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          921..956
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          960..1081
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          845..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..927
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  119527 MW;  677C9E594C40DB93 CRC64;
     MVWGLVLLAL WVWPSTQAGH QDKGTTFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF
     DYIPPVNAED LSKITRIMRQ KEGFFLTAQL KQDGKSRGTL LALEGPGLSQ RQFEIVSNGP
     ADTLDLTYWI DGTRHVVSLE DVGLADSQWK NVTVQVAGET YSLHVGCDLI DSFALDEPFY
     EHLQAEKSRM YVAKGSARES HFRGLLQNVH LVFENSVEDI LSKKGCQQAQ GAEINAISEN
     TETLRLGPHV TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND
     NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC HQITCPPATC
     ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TECSVTCGSG TQQRGRSCDV TSNTCLGPSI
     QTRACSLSKC DTRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG
     RETKACQGAP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER
     QMCNKRSCPV DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVSDI
     CFSTSKVPRC VNTQPGFHCL PCPPRYRGSQ PVGVGLEAAK TEKQVCEPEN PCKDKTHNCH
     RHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNLNLVCATN ATYHCIKDNC
     PHLPNSGQED FDKDGIGDAC DDDDDNDGVT DEKDNCQLLF NPRQADYDKD EVGDRCDNCP
     YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL
     VHNPDQTDMD NDLVGDQCDN NEDIDGDGHQ NNQDNCPYIS NANQADHDND GHGDACDPDD
     DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN VPDIDDVCPE NNAISETDFR
     NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV VRTLWHDPRN IGWKDYTAYR
     WHLTHRPKTG YIRVLVHEGK QIMADSGPIY DQTYAGGRLG LFVFSQEMVY FSDLKYECRD
     V
//
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