LMBD2_XENLA
ID LMBD2_XENLA Reviewed; 713 AA.
AC Q7ZYA0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=G-protein coupled receptor-associated protein LMBRD2 {ECO:0000250|UniProtKB:Q68DH5};
DE AltName: Full=LMBR1 domain-containing protein 2;
GN Name=lmbrd2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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; BC043881; AAH43881.1; -; mRNA.
DR RefSeq; NP_001080584.1; NM_001087115.1.
DR AlphaFoldDB; Q7ZYA0; -.
DR SMR; Q7ZYA0; -.
DR PRIDE; Q7ZYA0; -.
DR DNASU; 380276; -.
DR GeneID; 380276; -.
DR KEGG; xla:380276; -.
DR CTD; 380276; -.
DR Xenbase; XB-GENE-991218; lmbrd2.L.
DR OrthoDB; 778022at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 380276; Expressed in testis and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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..713
FT /note="G-protein coupled receptor-associated protein
FT LMBRD2"
FT /id="PRO_0000299165"
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..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 600..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..314
FT /evidence="ECO:0000255"
FT COILED 587..620
FT /evidence="ECO:0000255"
FT COMPBIAS 600..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 713 AA; 82694 MW; 7804C52BABBC1F4F CRC64;
MSGVALGIEI VSVFFLALFL LHRYGDFKKQ HKLVIVGTLL AWYLCFLIVF IIPLDVSTTI
YNRCVARHAV TPAPSNITVL SPTPGIVSNT TAQNHLPSAD KLRSSDNSLE ECSKPWSYIP
RGIMPIFWRV VYWTSQFLTW ILMPFMQSYA RSGGFSITGK IKTALIENAI YYGTYLLIFG
ALLIYVAVNP NLHLEWYQLQ TIGIAAANTW GLFLLVLLMG YGLVEIPRSQ WNGAKKGYLL
MKTYFKAAKL MTEKADAEET LEDVMEEVRK VNECIKYNHP LRKCVDTILK KCPAEYQEKM
GRNMDDYEDF EEKNISYPSE KTLVKLHKQV IYAVQRHRRT QVQWSILLEQ AFHLEDVAKN
ETSAAKQFVH TFPHQEPESW IMRRLYTPTI EWYWECLLRP WCSRILAVIL ALFSTVVVWS
ECTFFSAKPV LSLFAVFIQQ AEQTHNYIYV EVVCFLSIFF LSICVYSTVF RIRVFNYYYL
ASHHQTDAYS LLFSGMLFCR LTPPLCLNFL GLTHMDVSIS HQNIEPTAYT SIMGSLRVLP
LIADVFYIYY PMLVLILCIA TYFSLGTRCL NLLGFQQFMG DNDMTSDLTD EGKELIKREK
RKRQRLEDGE TRRREWKERY PTNREDTSRN RSVNSDQKEP TYTEMTTNRS SKYTRASNRT
ERDRIELLQD AEPLDFNADT FNDDPLDSES GRYQPGGRYL SMSQSNSRIF DDV