ID A0A3Q1JCI8_ANATE Unreviewed; 1517 AA.
AC A0A3Q1JCI8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSATEP00000030715.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000030715.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000030715.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR STRING; 64144.ENSATEP00000030715; -.
DR Ensembl; ENSATET00000031176.2; ENSATEP00000030715.1; ENSATEG00000021184.2.
DR GeneTree; ENSGT00940000155527; -.
DR InParanoid; A0A3Q1JCI8; -.
DR OMA; NENTMIM; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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:UP000265040};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030080376"
FT TRANSMEM 871..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1086..1109
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 505..560
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 869..1110
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 398..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1517 AA; 168303 MW; 2C2AD07B801AA960 CRC64;
MWIRCLLFVS TLFAPIAIAH GRAPIPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDSDP AQMENTRCYL PDAYKIMSLR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGILR GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKED FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGRIVVSQL NPYTLRIEGS
WDTSYDKRSA SNAFMICGVL YVVKTVYEDD DNEGTGNKID YMYNTDKSKE MTINIPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGNNDFRPPP MIPPNRGGGG GPIGGGGSSS
SSTSRTTTTR SPPYYTTPRP LLTTSPGQRY RTTTTIRQPV LVPASGSSSD TNQIPDTNQK
AGGRSPPVQV PPAIPQAPVL PPQDFCSPRV TADISWPRTQ QGQTAKQPCP VGTLGVATYV
CRMGYWDPQG PDLSNCTSPW VNHIMQKLRS GETAAIVARE LAEQTKGLLR PGDVPSTVRA
MAQLVELLDV QLRNLTPGGK DSAARSLTKA MVETVNNLLQ PRAEAAWGEL PTSEKLHSAT
LLLDTVETGA FMLADNLLKT DTVQETTDNI QLEVARLSTD GNLADLTFPQ SELHGNSIQL
SASTLKQHGR NGEIRMAFVL YRNLGAYLST ENASVRLSSE AVYPNYSVIV NSPVITASIN
KESNKVYLSE PVVFTVKHLQ HSEENFNPNC SFWSYSKRTM TGFWSTQDCR LLATNRTHTS
CSCTHLTSFA VLMAHVEVKK AGSMHDLLLD VITWVGILLS LVCLLICIFT FCFFRGLQSD
RNTIHKNLCI SLFIAESLFL VGINRADQPI ACAVFAALLH FFFLAAFTWM FLEGVQLYIM
LVEVFESEHS RTKYFYLAGY GVPAVIVAVS AAVDYRSYGT DRVCWLRLDT YFIWSFIGPA
TLIIMLNVIF LGIALYKMFH HTAILKPDSG CLDNIKSWVI GAIALLCLLG LTWAFGLMYI
NESTVIMAYL FTIFNSLQGM FIFIFHCILQ KKVRKEYGKC LRTHCCSGKS VETSISSSSK
TTTSRTPGRY STGSQVSLPA CTPGRYSTAD SQSRIRRMWN DTVRKQESSF ITGDINSSAT
LNREGILNNA RDSSVMDTLP LNGNHANNYS MASSEYLSDC VQILDRSGGY GTHSNHKETT
LEKKILKELT SNYIPSYLNN HERATTERNH NLMNKLVNSS MANGGSMAGG SSSSSSGVSG
CVGSSKEDNG PMVMDNPAAF PHEENLGLEI IREESNAPLL PPRPPPPDSH PPPPPPPHSF
SRPRHIPQET SESFFPLLTN EHTNEHTHSP SHRDSLYTSM PVLTDLPDGQ MNGLTDGEED
SSGELQPCKS ATAPELDDVY YKSMPNLGSR NHLHELQSYY HMGRGGSDGY MVSGSKEESD
SSPEEPPVDP SHLVTSL
//
