ID A0A1S3F310_DIPOR Unreviewed; 918 AA.
AC A0A1S3F310;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Thrombospondin-3 {ECO:0000313|RefSeq:XP_012870494.1};
GN Name=Thbs3 {ECO:0000313|RefSeq:XP_012870494.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870494.1};
RN [1] {ECO:0000313|RefSeq:XP_012870494.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870494.1};
RG RefSeq;
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 RefSeq; XP_012870494.1; XM_013015040.1.
DR AlphaFoldDB; A0A1S3F310; -.
DR STRING; 10020.ENSDORP00000010919; -.
DR GeneID; 105984769; -.
DR KEGG; dord:105984769; -.
DR CTD; 7059; -.
DR InParanoid; A0A1S3F310; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000081671; Unplaced.
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:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16079; TSP-3cc; 1.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028507; TSP3_coiled-coil.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF89; THROMBOSPONDIN-3; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 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}; Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 278..316
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 454..489
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 513..548
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 650..685
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 689..903
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 480..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 99970 MW; CD27D71A182A844D CRC64;
MVAVAEKIRT ALLTAGDIYL LSTFRLPPKQ GGVLFGLYSR QDNTRWLEAS VVGKINKVLV
RYQREDGKVH AVNLQQAGLA DGRTHTALLR LRGPSRPSPG LQLYVDCKLG DQYAGLPALA
PIPPAEVSGL EIRTGQKAYL RMQGFVESMK IILGGSMARV GALSECPFQG DESIHSAVAN
ALQSILGEQT KALVTQLTIF NQILVELRDD IRDQVKEMSL IRNTIMECQV CGFHEQRSHC
SPNPCFRGVD CMEVYEYPGY RCGPCPPGLQ GNGTHCDDIN ECAHADPCFP GSSCINTMPG
FHCEACPRGY KGTQVSGVGI DYARASKQVC NDIDECNDGN NGGCDPNSIC TNTVGSFKCG
PCRLGFLGNQ SQGCLPARTC HSPTHSPCHV HAHCLFERNG AVSCQCNVGW AGNGNVCGPD
TDIDGYPDQA LPCMDNNKHC KQDNCLLTPN SGQEDADNDG VGDQCDDDAD GDGIKNVEDN
CRLFPNKDQQ NSDTDSFGDA CDNCPNVPNN DQKDTDGNGE GDACDNDVDG DGIPNGLDNC
PKVPNPLQTD RDEDGVGDAC DSCPEMSNPT QTDADSDLVG DVCDTNEDSD GDGHQDTKDN
CPQLPNSSQL DSDNDGLGDE CDGDDDNDGI PDYVPPGPDN CRLVPNPNQK DSDGNGVGDV
CEDDFDNDAV VDPLDVCPES AEVTLTDFRA YQTVVLDPEG DAQIDPNWVV LNQGMEIVQT
MNSDPGLAVG YTAFNGVDFE GTFHVNTVTD DDYAGFLFSY QDSGRFYVVM WKQTEQTYWQ
ATPFRAVAQP GLQLKAVTSV TGPGEHLRNA LWHTGHTPDQ VRLLWTDPRN VGWRDKTSYR
WQLLHRPQVG YIRVKLYEGP QLVADSGVII DTSMRGGRLG VFCFSQENII WSNLQYRCND
TVPEDFEPFR RQLLQGRV
//