LMBD2_CAEBR
ID LMBD2_CAEBR Reviewed; 644 AA.
AC Q61ZW5; A8WT65;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=G-protein coupled receptor-associated protein LMBRD2 {ECO:0000250|UniProtKB:Q68DH5};
GN ORFNames=CBG02934;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601438; CAP23676.1; -; Genomic_DNA.
DR RefSeq; XP_002631150.1; XM_002631104.1.
DR AlphaFoldDB; Q61ZW5; -.
DR SMR; Q61ZW5; -.
DR STRING; 6238.CBG02934; -.
DR GeneID; 8572664; -.
DR KEGG; cbr:CBG_02934; -.
DR CTD; 8572664; -.
DR WormBase; CBG02934; CBP41562; WBGene00025893; -.
DR eggNOG; KOG2296; Eukaryota.
DR HOGENOM; CLU_018886_0_0_1; -.
DR InParanoid; Q61ZW5; -.
DR OMA; ERICYSA; -.
DR OrthoDB; 778022at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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_0000299166"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..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 216..245
FT /evidence="ECO:0000255"
FT COMPBIAS 573..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
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; 74057 MW; 905AF4BFDB72EFFC CRC64;
MGTVSLAVQL FIVFLLTSYL LNKYSTIRKQ NPIVTISTFI GWYFSLIIVF VLPLDVAITF
FHKCENDRQR VLNTTSTPAP IVPECELPGG YVPDDVLFDL WRVVYWSAQI LTWLILPLLQ
SYVTAGNFTI FGKIRAAVIN NTVYYAIYSL CFLAILIYAM FKGVSINIEN LKVILVSASN
TWGLFLLVVL LGHGLVELPR SLWHHGNRHY RLRKTYFDIE KLASEKSEAE ENVKEIYKKV
RVLFNSMKND QNGQRRKVRT ILSKFSDDVI DQLFPSRQVI DNASMEEIGD YCSEAKLINL
HKKTIYAVQT LNNATAQWKV LVDRALFLEN LAFSESNGYN LDLARNICVP VGVRRFWYTR
LQTPFCRVLG VVTVFMTFFV LFSECTFFVV SYTVSPAAFV TEYASNRFHY KYTQFVAFGI
IVYLITCAYF TIFRLQIYKY YHLDPNGHTD ENSILFSAIL LCRLTPPICL NFLGMIHMDS
HVSMAKSFGV ETQFTKLMGH LDVIPILAKG INIYLPICII LLCAIHYYRV GAYVLHNIGF
DQFVESDEMT NDMINSGRSL VQIERNSIKR SNERNQRNQS WTNTITSNTS TTSNAVNKYK
RSRKNEEERP MLEEEEEMEE VSSTTRISLS PTEHPSSSGF FDDM