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Database: UniProt
Entry: A0A1V4L1H3_PATFA
LinkDB: A0A1V4L1H3_PATFA
Original site: A0A1V4L1H3_PATFA 
ID   A0A1V4L1H3_PATFA        Unreviewed;       913 AA.
AC   A0A1V4L1H3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Thrombospondin-4 {ECO:0000313|EMBL:OPJ90515.1};
GN   Name=THBS4 {ECO:0000313|EMBL:OPJ90515.1};
GN   ORFNames=AV530_008693 {ECO:0000313|EMBL:OPJ90515.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ90515.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ90515.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ90515.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ90515.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ90515.1}.
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DR   EMBL; LSYS01000242; OPJ90515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4L1H3; -.
DR   STRING; 372326.A0A1V4L1H3; -.
DR   Proteomes; UP000190648; 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   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; 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; 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:UP000190648};
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          275..312
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          328..371
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          448..483
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          507..542
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          644..679
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          683..897
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          556..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..624
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  100281 MW;  CC74CF42848C14E6 CRC64;
     MVTNFLQQAL GDSTLDDVYL LSTFKLQPKS TATVFGLYSS AENNKYFEFT VMGRMNKVVL
     RYLKSDGRLN SVIFSNIHLA DGKPHAVILW LSGLQQGSST MELYLDCLQV GAIQDVPKAF
     SALSLRSSAV ELRTFQEKPQ EALNELKLVT GGTLAEVGNL QDCFLQQIEP VSQYTGDFNR
     QLMGQMMQMN QILGDVKDLL RQQVKETTFL RNTIAECQAC GLGTVNFPTQ LPRRSKPKCE
     VNSCFRGVRC METADGFQCG PCPEGLTGNG VTCSDIDECR YSPCFPGVRC VNTAPGFRCE
     TCPPGYTGQT VQGVGLSYAK NNKQICLDID ECQNGGLGLC VPNSHCINTL GSYHCGQCKP
     GYTGDQVRGC QAERSCRNRA LNPCSVHARC IEEKRGEVTC ICGIGWAGDG YICGKDVDID
     GYPNEELSCS AENCRKDNCR FVPNSGQEDA DGDGIGDACD DDADGDGIPN EQDNCVLAPN
     VNQRNGDQDI FGDACDNCRN VLNNDQRDTD GDGKGDACDD DMDGDGIKNL LDNCQRIPNQ
     DQEDMDNDGV GDACDSCPTI SNPNQSDVDN DLVGDSCDTN QDSDGDGHQD STDNCPTIIN
     SSQLDTDKDG LGDECDEDDD NDGIPDLLPP GPDNCRLVPN PGQEDDNGDG VGDICESDFD
     QDTVIDRIDV CPENAEITLT DFRAYQTVVL DPEGDAQIDP NWVVLNQGME IVQTMNSDPG
     LAVGYTAFNG VDFEGTFHVN TVTDDDYAGF IFGYQDSSSF YVVMWKQTEQ TYWQATPFRA
     VAEPGIQLKA VKSKTGPGEH LRNSLWHTGD TSDQVRLLWK DPRNVGWKDK VSYRWFLQHR
     PQIGYIRARF YEGSDLVADS GVTIDTTMRG GRLGVFCFSQ ENIIWSNLKY RCNDTIPEDF
     QEFQAQQFGV GDI
//
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