ID A0A452SCY4_URSAM Unreviewed; 877 AA.
AC A0A452SCY4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thrombospondin 4 {ECO:0000313|Ensembl:ENSUAMP00000030195.1};
GN Name=THBS4 {ECO:0000313|Ensembl:ENSUAMP00000030195.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000030195.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000030195.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Sarcoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004369}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
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; A0A452SCY4; -.
DR Ensembl; ENSUAMT00000033680.1; ENSUAMP00000030195.1; ENSUAMG00000020082.1.
DR GeneTree; ENSGT00940000155227; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
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; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF92; THROMBOSPONDIN-4; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT DOMAIN 242..279
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 295..332
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 336..378
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 412..447
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 471..506
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 608..643
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 647..861
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 518..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 96987 MW; 8CC9FDB470192329 CRC64;
LHVCHPELLQ FATQGSPEPP RVVLSTCLVN QGRSILRYLK NDGKIHLVVF NNLQLADGRR
HRVLLRLSNL QRGAGSVELY VDCAQVDSVH NLPRAFSRSS QSPEPVELRT FQRKAQVGTH
KPFSKVERWI ATREFFHSWI MYQILLFHLV FPFPFLKVKE TTFLRNTVAE CQACGPLSFQ
SPTANTLVPP APPAPATSPM PPVRRCDSNS CFRGVRCTDT RDGFQCGPCP DGYTGNGITC
SDIDECKYHP CYPGVRCVNL APGFRCEACP VGFTGPIVQG VGISFAKSNK QVCTDIDECR
NGACVLNSIC INTLGSYRCG PCKPGYTGDQ TRGCKTERSC RNPELNPCSV NAQCIEERQG
DVTCVCGVGW AGDGYICGRD VDIDSYPDEE LPCSARNCKK DNCKYVPNSG QEDADRDGIG
DACDEDADGD GIVNEQDNCV LTHNVDQRNS DKDIFGDACD NCRNVLNNDQ KDTDGDGKGD
ACDDDMDGDG IKNILDNCPK VPNRDQWDKD GDGVGDVCDS CPDVSNPNQS DVDNDLVGDS
CDTNQDSDGD GHQDSTDNCP TVINSAQLDT DKDGIGDECD DDDDNDGIPD LVPPGPDNCR
LVPNPAQEDS NSDGVGDICE TDFDQDQVID RIDVCPENAE VTLTDFRAYQ TVVLDPEGDA
QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT FHVNTQTDDD YAGFIFGYQD
SSSFYVVMWK QTEQTYWQAT PFRAVAEPGI QLKAVKSKTG PGEHLRNSLW HTGDTSDQVR
LLWKDSRNVG WKDKVSYRWF LQHRPQVGYI RVRFYEGSDL VADSGVTIDT TMRGGRLGVF
CFSQENIIWS NLKYRCNDTI PEDFQEFQTQ NFDRLDN
//
