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Database: UniProt
Entry: T1G474_HELRO
LinkDB: T1G474_HELRO
Original site: T1G474_HELRO 
ID   T1G474_HELRO            Unreviewed;       327 AA.
AC   T1G474;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Latrophilin Cirl {ECO:0000256|ARBA:ARBA00015543};
GN   Name=20215872 {ECO:0000313|EnsemblMetazoa:HelroP80944};
GN   ORFNames=HELRODRAFT_80944 {ECO:0000313|EMBL:ESO03089.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP80944, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESO03089.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP80944}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region non-covalently linked to a seven-transmembrane moiety.
CC       {ECO:0000256|ARBA:ARBA00011834}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AMQM01004767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB096676; ESO03089.1; -; Genomic_DNA.
DR   RefSeq; XP_009018782.1; XM_009020534.1.
DR   AlphaFoldDB; T1G474; -.
DR   STRING; 6412.T1G474; -.
DR   EnsemblMetazoa; HelroT80944; HelroP80944; HelroG80944.
DR   GeneID; 20215872; -.
DR   KEGG; hro:HELRODRAFT_80944; -.
DR   CTD; 20215872; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_002753_3_1_1; -.
DR   InParanoid; T1G474; -.
DR   OMA; WKFIAGK; -.
DR   OrthoDB; 1114672at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   CDD; cd15440; 7tmB2_latrophilin-like_invertebrate; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR048072; 7tmB2_latrophilin-like.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF347; LATROPHILIN CIRL; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..291
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
SQ   SEQUENCE   327 AA;  37078 MW;  FE921279F6814C05 CRC64;
     MIVFSEWSNE GCHVMSHNKT HVTCSCEHLT SFAVLMSYSA HETKELDFIT YFGCCLSLVS
     MLLAFVTFTC FKNLRCDRNS IHKNLVANLF VAELIFCLGI NQQLTNKPTT HQTLCSVISI
     LLHYFFLTSF CWMCMEGVHL YILLVVVFNG ATSHLKYYCA LSYAVPAIIV IISMSVNIEG
     YGTEDHCWLS TEHGFSWAFL APVIFILTIN SVVLSVTIGT MCRLKLNTPQ ASTDNNVLTN
     FSALVLMVIL GSTWLLGVFN INQSSITMVY IFTILNTLQG FLIFLFHCLL NKKVGWLCCR
     WQVVSSHHTF EGSFKQIFFF ISFLQLI
//
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