ID A0A4D9E0A2_9SAUR Unreviewed; 1464 AA.
AC A0A4D9E0A2;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Leucine zipper putative tumor suppressor 3 {ECO:0000313|EMBL:TFK00783.1};
GN ORFNames=DR999_PMT17052 {ECO:0000313|EMBL:TFK00783.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK00783.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK00783.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK00783.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK00783.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK00783.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK00783.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK00783.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:TFK00783.1}.
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DR EMBL; QXTE01000256; TFK00783.1; -; Genomic_DNA.
DR STRING; 55544.A0A4D9E0A2; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd16005; 7tmB2_Latrophilin-3; 1.
DR CDD; cd22846; Gal_Rha_Lectin_LPHN3; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 2.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020023897"
FT TRANSMEM 879..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1065..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..124
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 498..554
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 877..1118
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 412..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1464 AA; 163393 MW; DC9659CCD3BCD162 CRC64;
MWSSQLLFFT MLLAPAVHAF SRAPVPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDSDP AQMENIRCYL PDAYKIMTQR CSNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGLLK GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKDD FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGKIVISQL NPYTLRIEGT
WDTAYDKRSA SNAFMICGIL YVVKSVYEDD DNEATGNKID YIYNTDQSKD SLVDVPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGPLDSRSGQ AHHGQVSYIA PPIHLDSDPE
RPPSKVSTSG AHGMGSTTTS TPLLLTATST GRTTTTSAAG RRNRSTSTPS LVVDVPDEMT
TPLPPASSQL PAVGAESCEA VEAREIMWFR TRQGQMAKQP CPMGTVGVST FLCLAPDGIW
DPQGPDLSNC SSPWVNHITQ KLKSGETAAN IARELAEQTK NHLNAGDITY SVRAMDQLVG
LLDVQLRNLT PGGKDSAARS LNKLQKRERS CRAYVQAMVE TVNNLLQPQA LNAWRDLTAS
DQLRAATMLL DTVEESAFVL ADNLLKSDIV RENTDNIQLE VARLSTDGNL EDLKFPQNLG
HGSAIQLSAN TLKQNARNGE IRVAFVLYNN LGHYLSTENA SMKLGTEAMS TNHSVIVNSP
VITAAINKEF SNKVYLADPV VFTVKHIKQS EEIFNPNCSF WNYSKHTMTG YWSKQGCRLL
TTNKTHTTCS CNHLTNFAVL MAHVEVKHSD TVHDLLLDVI TWVGILLSLV CLLICIFTFC
FFRGLQSDRN TIHKNLCISL FVAELLFLIG INRTDQPIAC AVFAALLHFF FLAAFTWMFL
EGVQLYIMLV EVFESEHSRR KYFYLVGYGM PALIVAVSAA VDYRSYGTDK VCWLRLDTYF
IWSFIGPATL IIMLNVIFLG IALYKMFHHT AILKPESGCL DNIKSWVIGA IALLCLLGLT
WAFGLMYINE STVIMAYLFT IFNSLQGMFI FIFHCVLQKK VRKEYGKCLR THCCSGKSTE
SSIGSGKTSG SRTPGRYSTG SQVNHSRIRR MWNDTVRKQS ESSFITGDIN SSASLNREGL
LNNARDTSVM DTLPLNGNHG NSYSIASGEY LSNCVQIIDR GYNNHTETAL EKKILKELTS
NYIPSYLNNH ERSSEQNRNL VNKLVNNIGS ATEDDAIVLD DATSFNHEES LGLELIHEES
DAPLLPPRVY SAENHQPHHY TRRRIPQDNS ESFFPLLTNE HTEDHQSPNR DSLYTSMPAL
AGMPVTESVT TSTQTDPPTA KSGDADDVYY KSMPNLGSRN HVHQLHTYYQ LGRGSSDGFI
VPPSKDGTSP EGSSKGPAHL VTSL
//
