ID   LMBD2_CAEEL             Reviewed;         644 AA.
AC   Q18695;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=G-protein coupled receptor-associated protein LMBRD2 {ECO:0000250|UniProtKB:Q68DH5};
GN   ORFNames=C47G2.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: May associate with G-protein coupled receptors and regulate
CC       downstream signaling pathways. {ECO:0000250|UniProtKB:Q68DH5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q68DH5};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the LIMR family. {ECO:0000305}.
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DR   EMBL; Z49125; CAA88936.1; -; Genomic_DNA.
DR   PIR; T20034; T20034.
DR   RefSeq; NP_496413.1; NM_064012.6.
DR   AlphaFoldDB; Q18695; -.
DR   SMR; Q18695; -.
DR   STRING; 6239.C47G2.4; -.
DR   EPD; Q18695; -.
DR   PaxDb; Q18695; -.
DR   PeptideAtlas; Q18695; -.
DR   PRIDE; Q18695; -.
DR   EnsemblMetazoa; C47G2.4.1; C47G2.4.1; WBGene00008165.
DR   GeneID; 174724; -.
DR   KEGG; cel:CELE_C47G2.4; -.
DR   UCSC; C47G2.4; c. elegans.
DR   CTD; 174724; -.
DR   WormBase; C47G2.4; CE02167; WBGene00008165; -.
DR   eggNOG; KOG2296; Eukaryota.
DR   GeneTree; ENSGT00390000018651; -.
DR   HOGENOM; CLU_018886_0_0_1; -.
DR   InParanoid; Q18695; -.
DR   OMA; ERICYSA; -.
DR   OrthoDB; 778022at2759; -.
DR   PhylomeDB; Q18695; -.
DR   PRO; PR:Q18695; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00008165; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006876; LMBR1-like_membr_prot.
DR   Pfam; PF04791; LMBR1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..644
FT                   /note="G-protein coupled receptor-associated protein
FT                   LMBRD2"
FT                   /id="PRO_0000299167"
FT   TOPO_DOM        1..3
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..412
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        475..502
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        524..644
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          567..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          219..242
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        573..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   644 AA;  73646 MW;  056776A638B2667E CRC64;
     MGTISLAVQL FIVFLLTSYL LNKYSTIRKQ NPIVTISTFI GWYFSLIIVF VLPLDVAITF
     FHKCENDRQR ILNTTTSTPA PVVPECELPG GYVPDDVLFN LWRVVYWSAQ LLTWLILPLL
     QSYVTAGNFT ILGKIRAAVI NNALYYAIYS LCFLAILIYA MFKGVSINIE NLKVIVVSAS
     NTWGLFLLVV LLGHGLVELP RSLWHHGNRH YRLRKTYFDI EKLASEKSEA EENVKDIYKK
     VRVLFNSMKN DSNGQRRKVR TILSKFSDDV IDNLFPSRQV IDNAHLDESG PCSEAKLISL
     HKKTIYAVQT LNNATAQWKV LVDRALFLEN LAFSESNGYN LELSRNTCVP IGVRRFWYTR
     LQTPFCRILG IVTVFMTFFV LFSECTFFVV SYTLSPAAFV TEYASTRFHY KYTQFVAFGI
     IVYLITSAYF TIFRLQIYKY YHLDPNGHTD ENSILFSAIL LCRLTPPICL NFLGMIHMDS
     HISMAKSFGI ETQFTKLMGH LDVIPILAKG INIYLPICII LLCAIHYYRV GAYVLHNIGF
     DQFVEADEMT NDMINSGRSL VQIERNSIKR SNDRSQRTQN WTNSFGSSNA GNGSTTSKFK
     RSNKNDEERP MLEDDDEEVE ESSTRISMMS PTEHPSSSGF FDDM