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Database: UniProt
Entry: A0A2Y9DHY5_TRIMA
LinkDB: A0A2Y9DHY5_TRIMA
Original site: A0A2Y9DHY5_TRIMA 
ID   A0A2Y9DHY5_TRIMA        Unreviewed;       964 AA.
AC   A0A2Y9DHY5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thrombospondin-4 {ECO:0000313|RefSeq:XP_004374519.1};
GN   Name=LOC101352874 {ECO:0000313|RefSeq:XP_004374519.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004374519.1};
RN   [1] {ECO:0000313|RefSeq:XP_004374519.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_004374519.1; XM_004374462.1.
DR   AlphaFoldDB; A0A2Y9DHY5; -.
DR   STRING; 127582.A0A2Y9DHY5; -.
DR   GeneID; 101352874; -.
DR   KEGG; tmu:101352874; -.
DR   InParanoid; A0A2Y9DHY5; -.
DR   OrthoDB; 5345349at2759; -.
DR   Proteomes; UP000248480; Unplaced.
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   CDD; cd16080; TSP-4cc; 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; 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; 5.
DR   Pfam; PF05735; TSP_C; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
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; 2.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
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}; Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
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, ECO:0000256|SAM:SignalP};
KW   Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..964
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016067849"
FT   DOMAIN          329..366
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          423..465
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          499..534
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          558..593
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          695..730
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          734..948
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          271..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..290
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..675
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  106239 MW;  5AD25A27EAF9019A CRC64;
     MLARHGAAFL LLHLVLQPWL GADAQATPQV FDLLPSSSQR LNPGILQPIL TDPTLNEIYV
     ISTFKLQTKS TATIFGLYSS TDNSKYFEFT VMGRLNKAIL RYLKTDGKIH LVVFNNLQLA
     DGRRHRILLR LTNWQRGAGS VELYLDCTQV DSIHNLPRAF SGLSQSPKSI ELRTFQRKAQ
     DFLEELKLVV RGSLIQVASL QDCFLQQSEP LATISTGDFN RQFLGQMTQL NHLLAEVKDL
     LRQQVKETSF LRNTIAECQA CGPLSVQSST TNTLVPPAPP APPTSPTPPV RRCDPNSCFR
     GVRCTDTRDG FQCGPCPVGY TGNGITCSDI DECKYHPCYP GVRCVNLAPG FRCDACPVGF
     TGSMVQGVGI TFANLNKQVC TDIDECQNGA CVLNSICINT WGSYRCGPCK SGYAGDQTRG
     CKAERSCKNP ELNPCSVNAQ CIEERQGDVT CVCGVGWAGD GYICGKDVDI DSYPDEELPC
     SARNCKKDNC KYVPNSGQED ADGDGIGDTC DEDADGDGIL NEQDNCVLTH NVDQRNSDKD
     IFGDACDNCR TVLNNDQKDT DGDGKGDACD DDMDGDGIKN VLDNCPKVPN HDQQDKDNDG
     VGDACDSCPD ISNPNQSDVD NDLVGDSCDT NQDSDGDGHQ DSTDNCPTVI NSAQLDTDKD
     GIGDECDDDD DNDGIPDLVP PGPDNCRLVP NPAQEDSNSD GVGDVCEMDF DQDQVIDRID
     VCPENAEVTL TDFRAYQTVV LDPEGDAQID PNWVVLNQGM EIVQTMNSDP GLAVGYTAFN
     GVDFEGTFHV NTQTDDDYAG FIFGYQDSSS FYVVMWKQTE QTYWQATPFR AVAEPGIQLK
     AVKSKTGPGE HLRNSLWHTG DTSDQVRLLW KDFRNVGWKD KVSYRWFLQH RPQVGYIRVR
     FYEGSELVAD SGVTVDTTMR GGRLGVFCFS QENIIWSNLK YRCNDTIPED FQEFQTHNFD
     QLDN
//
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