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Database: UniProt
Entry: A0A493T8D7_ANAPP
LinkDB: A0A493T8D7_ANAPP
Original site: A0A493T8D7_ANAPP 
ID   A0A493T8D7_ANAPP        Unreviewed;       999 AA.
AC   A0A493T8D7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Thrombospondin 4 {ECO:0008006|Google:ProtNLM};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000022121.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000022121.1, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000022121.1}
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; A0A493T8D7; -.
DR   Ensembl; ENSAPLT00000035377.1; ENSAPLP00000022121.1; ENSAPLG00000006149.2.
DR   GeneTree; ENSGT00940000167074; -.
DR   Proteomes; UP000016666; Chromosome Z.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; 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; SSF57184; Growth factor receptor domain; 1.
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:UP000016666};
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          410..447
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          463..506
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          583..618
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          642..677
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          779..814
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          818..999
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   999 AA;  108857 MW;  1FBC43E4CD2B94CF CRC64;
     MTPWGGVIAP TRGLLRDPHR PRGRTQPAPC GRTPTPSAPQ RPSPAPARPL RPRAARRRPS
     PLNSGPGAEQ LAVLPCLLPS SPFPSPPLPG PALAAMGWDG GAALLLLPLA LQLCPGRAAP
     PAPRVIDLLS YSNKRVVTNF LQQALGDPTL NEVFLLSTFK LQPKSTATIF GLYSSTGNSK
     YFEFTVVGRM NKVVLRYLKS DGRLNSVIFS NIQLADGKPH AVILWLSGLQ QESSTIELYL
     DCLQVGAIQD LPKAFSTLPE RSAAVELHIF QKKPQDTLDE LKLVTGGTLA QVGNLQDCFL
     QQIEPASQYN GDFNRQLMSQ MMQMNQILGD VKDLLRQQVK ETTFLRNTLA ECQACGLGTV
     NFPTPIPRRS KPKCEPSSCF RGVRCMETAE GFQCGPCPEG LTGNGVTCSD IDECRYSPCF
     PGVRCVNTVP GFRCETCPPG YTGQTVQGVG LSYAKSNKQI CLDIDECQNG GHGLCVPNSH
     CINTLGSYHC GQCKSGYTGD QVRGCQAERS CRSRALNPCS VHARCIEERR GEVTCICGIG
     WAGDGYICGK DVDIDGYPNE ELSCPAESCR KDNCKFVPNS GQEDADGDGV GDACDEDADG
     DGIPNDQDNC VLTPNVNQRN SDQDIFGDAC DNCRNVLNND QRDTDGDGKG DACDDDMDGD
     GIKNLLDNCQ RIPNQDQEDK DNDGVGDACD SCPTVSNPNQ SDIDNDLVGD SCDTNQDSDG
     DGHQDSTDNC PTIINSSQLD TDKDGLGDEC DEDDDNDGIP DLLPPGPDNC RLVPNPGQED
     DNGDGVGDIC ESDFDQDTVI DRIDVCPENA EITLTDFRAY QTVVLDPEGD AQIDPNWVVL
     NQGMEIVQTM NSDPGLAVGY TAFNGVDFEG TFHVNTVTDD DYAGFIFGYQ DSSSFYVVMW
     KQTEQTYWQA TPFRAVAEPG IQLKAVKSKT GPGEHLRNSL WHTGDTSDQV RLLWKDPRNV
     GWKDKVSYRW FLQHRPQIGY IRKDNCKPTL FCDSVLYHV
//
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