ID M3VYG6_FELCA Unreviewed; 1136 AA.
AC M3VYG6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSFCAP00000002227.4};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSFCAP00000002227.4,
GN ECO:0000313|VGNC:VGNC:66155};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000002227.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000002227.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002227.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000002227.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002227.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000002227.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002227.4};
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 EMBL; AANG04004686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VYG6; -.
DR Ensembl; ENSFCAT00000002420.6; ENSFCAP00000002227.4; ENSFCAG00000002420.6.
DR VGNC; VGNC:66155; THBS2.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000002420; Expressed in eyeball of camera-type eye and 11 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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 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; 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; 2.
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; 3.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
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..1136
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014198095"
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 752..787
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 849..884
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 DOMAIN 924..1136
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 810..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125735 MW; 9319A1E5FA67CABE CRC64;
MLWDLVLLAL WAASGARAGD QDEDTAFNLF SISNINRKTI GAKQFRGPDP NVPAYRFVRF
DYIPPVSADY LSKIAKIVRQ KEGFFLTASL KQDPKSRGTL LALEGPGASQ RQFEIVSNGP
ADTLDLTYWI DGAQHVISLE DVGLADSQWK NITVQVTGET YSLYVGCDLI DSFTLDEPFY
EQLRTEKSRM YVAKGSARDN HFRGLLQNIY LVFENSVEDV LSKKGCQQSQ GAEANAISEN
TETLHLSPQV ATEYAGPGAH RRPEVCERSC EELGTMITEL SGLHVIVNQL HENLRKVSND
NQVLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTK CTCKKFKTVC HQITCPPATC
ANPSFVEGEC CPSCFHSLDG EEGWSPWAEW TQCSATCGSG TQQRGRSCDV TSNTCLGPSI
QTRACSLGKC DHRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG
RETKGCQGTP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQHGG KDCVGDVQER
QMCNKRSCPV DGCLSNPCFP GAECSSFPDG SWSCGACPVG FLGNGTHCED LDECAVVTDV
CFAVGKAQRC VNTNPGFHCL PCPPRYKGTQ PFGVGLEAAR TEKQVCEPEN PCKDKTHACH
KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNKNLVCSTN ATYHCIKDNC
QLLFNPRQFD YDKDEVGDRC DNCPYVHNPA QIDTDNNGEG DACSVDIDGD DVFNERDNCP
YVYNTDQRDT DGDGVGDHCD NCPLVHNPDQ TDIDNDLVGD QCDNNDDIDD DGHQNNQDNC
PYIPNANQAD HDHDGQGDAC DSDDDNDGVP DDRDNCRLVS NPGQEDSDGD GRGDACKDDF
DNDSIPDIDD VCPENSAISE TDFRNFQMVH LDPKGTTQID PNWVIRHQGK ELVQTANSDP
GIAVGFDEFG SVDFSGTFYV NTDRDDDYAG FVFGYQSSSR FYVVMWKQVT QTYWEEQPTR
AYGYSGVSLK VVNSTTGTGE HLRNALWHTG NTQGQVRTLW HDPKNIGWKD YTAYRWHLTH
RPKTGYIRVL VHEGKQVMAD SGPIYDQTYA GGRLGLFVFS QEMVYFSDLK YECRDV
//
