ID LMBD2_CHICK Reviewed; 688 AA.
AC Q5F3F5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=G-protein coupled receptor-associated protein LMBRD2 {ECO:0000250|UniProtKB:Q68DH5};
GN Name=LMBRD2 {ECO:0000250|UniProtKB:Q68DH5};
GN ORFNames=RCJMB04_18o10 {ECO:0000312|EMBL:CAH65329.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ851695; CAH65329.1; -; mRNA.
DR RefSeq; NP_001026750.1; NM_001031579.1.
DR AlphaFoldDB; Q5F3F5; -.
DR SMR; Q5F3F5; -.
DR STRING; 9031.ENSGALP00000021784; -.
DR GlyCosmos; Q5F3F5; 1 site, No reported glycans.
DR PaxDb; 9031-ENSGALP00000021784; -.
DR GeneID; 429640; -.
DR KEGG; gga:429640; -.
DR CTD; 92255; -.
DR VEuPathDB; HostDB:geneid_429640; -.
DR eggNOG; KOG2296; Eukaryota.
DR InParanoid; Q5F3F5; -.
DR OMA; QLERICY; -.
DR OrthoDB; 1068841at2759; -.
DR PhylomeDB; Q5F3F5; -.
DR PRO; PR:Q5F3F5; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
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 PANTHER; PTHR21355:SF0; G-PROTEIN COUPLED RECEPTOR-ASSOCIATED PROTEIN LMBRD2; 1.
DR PANTHER; PTHR21355; UNCHARACTERIZED; 1.
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..688
FT /note="G-protein coupled receptor-associated protein
FT LMBRD2"
FT /id="PRO_0000299163"
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..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 600..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..254
FT /evidence="ECO:0000255"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 688 AA; 80291 MW; 6B6F6BA11BE09522 CRC64;
MSGAALGLEI VFVFFLALFL LHRYGDFKKQ HRLVIIATLL AWYLCFLIVF ILPLDVSTTI
YNRCKLAVNS SPAESNSSFV TLAPSKQQCF KPWSYIPNGI MPIFWRVVYW TSQFLTWILL
PFMQSYARSG GFSITGKIKT ALIENAIYYG TYLLIFGAFL IYVAVNPKFN LQWNQLQTIG
IAAANTWGLF LLVLLLGYGL VEIPRSHWNG AKRGYLLMKT YFKAAKLMTE KADAEENLED
IMEEVRKVSE SIKYNHPLRK CVDTILKKCP TEYQERMGRN MDDYEDFDER QNSYPSEKSL
VKLHKQVIYS VQRHRRTQVQ WQILLEQAFY LEDVAKNETS ATRQFVHTFQ SQEPENKIIQ
YFYTPTVEWY WECLLRPWFY RVLAVVLAAF SVIVVWSECT FFSTRPVLSL VAVFIQLAEK
TYNYIYIEMA CFLTIFFLSI CVYSTVFRIR VFNYYYLASH HQTDAYSLLF SGMLFCRLTP
PLCLNFLGLT HMDATISHTD AQPTAYTSIM GSMKVLSFIA DGFYIYYPML VVILCIATYF
SLGTRCLNLL GFQQFMGDSE MTSDLIDEGK ELIRREKGRR QRQEEGENRR REWKERYGNR
EDSTRNRVVH TEQKESSFSE TNTNRPLSKY TRTNGRTERD RIELLQDAEP LDFNADSIND
DPLESDSGRY QPGGRYLSMS RSRIFEDV
//
