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Database: UniProt
Entry: A0A3B4A5M1_9GOBI
LinkDB: A0A3B4A5M1_9GOBI
Original site: A0A3B4A5M1_9GOBI 
ID   A0A3B4A5M1_9GOBI        Unreviewed;      1464 AA.
AC   A0A3B4A5M1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000012358.1};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000012358.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000012358.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; 409849.ENSPMGP00000012358; -.
DR   Ensembl; ENSPMGT00000013186.1; ENSPMGP00000012358.1; ENSPMGG00000010201.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; cd16007; 7tmB2_Latrophilin-1; 1.
DR   CDD; cd22844; Gal_Rha_Lectin_LPHN1; 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; IPR031234; Latrophilin-1_TM.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 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; 1.
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   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        835..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        874..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        903..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        942..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        981..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1025..1048
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1054..1077
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..121
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          129..388
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          463..519
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          837..1078
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          406..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1280..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        130..312
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1464 AA;  163944 MW;  AFBE28412175AFAB CRC64;
     MINNRVSPSP PPSTPALSRS MMPFGLMRRE LACEGYPIEL RCPGSDVIMI ETANYGRTDD
     KICDADPFQM ENTQCYLPDA FKIMSQRCNN RTQCVVVAGS DVFPDPCPGT YKYLEIQYEC
     VPYSEYLFVC PGTLLRVQAA SSQQEAEHQA GAWCKDPLQS GDRLYVMPWT PYRTDVLYEY
     ASWEDFKQTR ATTTYKLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT RIKSGEAIIT
     NANYHDTSPY RWGGKSDIDL AVDENGLWVI YATESNNGRL VVSQVNPYTL RFEGTWETSF
     DKRMASNAFM ACGVLYAVRS VYQDDDSEAG GDLILYAYNT NRNREEPVSI PFPNPYQYIS
     SVDYNPRDNQ LYVWNNYNVL RYPLEFGPPD PTTGPLTTTQ VTTTLPARPF SSSASPSTAR
     PIAPTSRPIG SINKHPDLRP ITATVPVTRR PSHPPQGPEL YLCEPKMVRG VQWPATLRGE
     TVDRPCPKGS LGIASYQCLA DQVIWNPRGP DLSNCTSPWV NQVAQKIKSG ENAANIAGEL
     VNHTRSRIQA GDVSSSVRLI EQLLDILDAQ LQALRPGNKD LATRNYNKVR QATEILKLTY
     YAVIQIVDNL LRPEALESWQ DMNSTEQAHT ATMLLDVLEK GAFLLANNMY ANYFTDHAPN
     LEVHVLNTEM ELQDLSFPQN YASDSAIQLS ASTIKQYSRN GQVKVVFLLY KNLGSFLSTE
     NATVKMEMES NHDRRRLAVN SHVIAASINK ESSRVFLTEP VVFTLRHLQM DNYHTPNCSF
     WNYSERSMTG QWSSQGCRLL SSNSTHTTCS CSHLTNFAVL MASHEPDYQG RMHELILFVI
     TWVGIVISLV CLAICISTFC FLRGLQTDRN TIHKNLCINL FIAELLFLIG IDKTDYQIAC
     PIFAGLLHFF FLAAFCWMCL EGVQLYLMLV EVFESEYSRK KYYYLCGYCF PALVVGISAA
     IDYRSYGTKK ACWLRVDNYF IWSFIGPVSF VIMLNLMFLM VTLHKMIRNS SALKPDSSRL
     DNIKSWALGA ITLLFLLGLT WAFGLLFINE NTVIMAYLFT TFNAFQGMFI FIFHCALQKK
     VHKEYSKCLR HSYCCSRTST SSSHGSLKNS GLRTNNRYYS GSQSRIRRMW NDTVRKQSES
     SFMAGDINST PTLNRATMGN HLLTNPVLQT RSGTSPYNTL LAESFTPPSP GVFNSTGYTL
     SKGRDPCGME TLPLNGNFNN SYSLRTGPGA GGSCDFLSAD RNSPPLLNPR GAETLGGGAR
     RNLTDAAALE KMIISELVHN NLRGGGGGEQ GDRICANMNR PHAGLGRGPV EQSLSLDEDE
     DFLREGHQRT PQDVELLYKA LEEPLLLQQA QSVLYQSDAE ESESYTADLT ENSPARDSLY
     TSITNLRDSP YPDSSPEPLE VVPRSAQPPE ELYYSSGRPA LGSRGAPMQT FYQAAPRRPS
     GEGPPALEPP HSEGDGQMQL VTSL
//
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