ID   LMD2B_DANRE             Reviewed;         704 AA.
AC   Q6P4P2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=G-protein coupled receptor-associated protein LMBRD2B {ECO:0000250|UniProtKB:Q68DH5};
DE   AltName: Full=LMBR1 domain-containing protein 2-B;
GN   Name=lmbrd2b; Synonyms=lmbrd2; ORFNames=zgc:73387;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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; BC063324; AAH63324.1; -; mRNA.
DR   RefSeq; NP_956238.1; NM_199944.1.
DR   AlphaFoldDB; Q6P4P2; -.
DR   SMR; Q6P4P2; -.
DR   STRING; 7955.ENSDARP00000122007; -.
DR   PaxDb; Q6P4P2; -.
DR   GeneID; 335257; -.
DR   KEGG; dre:335257; -.
DR   CTD; 335257; -.
DR   ZFIN; ZDB-GENE-030131-7197; lmbrd2b.
DR   eggNOG; KOG2296; Eukaryota.
DR   InParanoid; Q6P4P2; -.
DR   OrthoDB; 778022at2759; -.
DR   PhylomeDB; Q6P4P2; -.
DR   PRO; PR:Q6P4P2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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   GO; GO:0071875; P:adrenergic receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR006876; LMBR1-like_membr_prot.
DR   Pfam; PF04791; LMBR1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..704
FT                   /note="G-protein coupled receptor-associated protein
FT                   LMBRD2B"
FT                   /id="PRO_0000299164"
FT   TOPO_DOM        1..3
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..481
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        503..527
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        549..704
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          613..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          235..266
FT                   /evidence="ECO:0000255"
FT   COILED          576..612
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        622..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   704 AA;  82046 MW;  B2E7C97FCF85FE4C CRC64;
     MSGAALGIEI VVVFFLALFL LHRYGDFKKQ QRMVLFGTLL AWYLCFLIVF ILPLDVSTTI
     YNQCLIDQEA QTQTPSVSPV LSEQTTANAS ISPAKSTQRV CYKPWSYIPD GIMPVFWRVV
     YWTSQCLTWL LLPFMQSYAR SGGFTITGKI KTALIENAIY YGTYLFIFGS LLIYVAVHPQ
     WHLSWYELQT IGITAANTWG LFLLVLLLGY GLVDIPRSYW EASRQGHLLI KTYFKAAKLM
     TEKADSEENL EDVMEEVRKI NESIKYNHPL RKNVDTILRK CPLEYQEKMG RNMDDFEDFD
     DKQNSYPTER SLSKLHKQVI YAVQRHNRTR VQWQILLEQA FHLEDVAKNE TSTSRQFVHS
     FAPPEPVGWF RRYIYTPTAE WYWECLLKQW FYRVLAVVLA LFSVAVVWSE CTFFSTHPVL
     SLFAVFIQLA ERDYNYLYIE MACFITIFFL CTCVYSTVFR IRVFNYYYLA SHHQTDAYSL
     QFSGMLFCRL TPPLCLNFLG LIHMDSAISH QAKKQTAYTS IMGSMRVLSF IANGFYIYYP
     MLIVVLCIAT YFSLGTRCLN LLGFQQFMGE NEMTSDLIDE GRELLRRERR KRQRIEDGEN
     RRREWRERYA QRDENAARNR TSMSEMKETN YGETLNANTN RQAKYTRSGS QSGRDSIELL
     QDAEPLDFNA ETLTDDPLQS DTGRHAGGRY LSMSSSRNRI FDDV