ID M3Y5J6_MUSPF Unreviewed; 1173 AA.
AC M3Y5J6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSMPUP00000006597.1};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSMPUP00000006597.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000006597.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000006597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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}.
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; AEYP01073679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y5J6; -.
DR STRING; 9669.ENSMPUP00000006597; -.
DR Ensembl; ENSMPUT00000006710.1; ENSMPUP00000006597.1; ENSMPUG00000006651.1.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; M3Y5J6; -.
DR OMA; MPGVMLQ; -.
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; -; 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; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 319..376
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 550..590
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 649..693
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 730..765
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 789..824
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 886..921
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 922..957
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 961..1173
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 728..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 129665 MW; 0DA58D6FE95B5F52 CRC64;
NALWACARPV CWQSLCSVPT AAGAQDEDMA FDLFSISNIN RKTIGAKQFR GPDPSVPAYR
FVRFDYIPPV NADYLSKIAK IMRQKEGFFL TASLKQDPKS RGTLLALEGP GASQRQFEIV
SNGPADTLDL TYWTDGTQHV ISLEDVGLAD SQWKNITVQV TGETYSLYVG CDLIDSFTLD
EPFYEQLRTE KSRMYVAKGS ARESHFRGLL QNVYLVFENS AEDVLSQKGC QQSQGGYVPL
SNQQAGGAPK VAPEYAGPGA PRKPEVCEQS CEELGTMMAE LAGLRVVVNE LHENLRKVSN
DNQFLWELIG GPPKTRNMSA CWQDGRFFAE NETWVVDSCT KCTCKKFKTV CHQITCPPAT
CANPSFVEGE CCPSCFRSLD GEEGWSPWAE WTECSATCGS GTQQRGRSCD VTSNTCLGPS
IQTRACSLGK CDHRIRQHGG WSHWSPWSSC SVTCGSGNIT RIRLCNSPVP QMGGKNCKGS
GRETKGCQGV PCPIDGRWSP WSPWSACTVT CAGGIRERTR VCNSPEPQHG GKDCAGDVRE
HQMCNRRSCP IDGCLSNPCF PGAQCNSFPD GSWSCGSCPV GFLGNGTHCE DLDECAVVTD
VCFTTSKAHR CVNTNPGFHC LPCPPRYKGT QPFGVGLEAA RTEKQVCEPE NPCKDKTHSC
HRHAECIYLG HFSDPMYKCE CQTGYAGDGL ICGEDSDLDG WPNKNLVCAT NATYHCIRDN
CPLLPNSGQE DFDKDGTGDA CDDDDDNDGV DDEKDNCQLL FNPRQFDYDK DEVGDRCDNC
PYVHNPAQID TDDNGEGDAC SVDIDGDDVF NERDNCPYVY NTDQRDTDGD GVGDHCDNCP
LVHNPDQTDV DNDLVGDQCD NNEDIDEDGH QNNQDNCPYI SNANQADHDH DGQGDACDSD
DDNDGVPDDR DNCRLVSNPD QEDSDGDGRG DACRDDFDND SVPDIDDVCP ENSAISETDF
RNFQMVHLDP KGTTQIDPNW VIRHQGKELV QTANSDPGIA VGFDEFGSVD FSGTFYVNTD
RDDDYAGFVF GYQSSSRFYV VMWKQVTQTY WEDQPTRAYG YSGVSLKVVN STTGTGEHLR
NALWHTGNTQ GQVRTLWHDP KNIGWKDYTA YRWHLTHRPK TGYMRVLVHE GKQVMADSGP
IYDQTYAGGR LGLFVFSQEM VYFSDLRYEC RGG
//
