LMBD2_HUMAN
ID LMBD2_HUMAN Reviewed; 695 AA.
AC Q68DH5; B3KRB6; Q9NTC7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=G-protein coupled receptor-associated protein LMBRD2 {ECO:0000305|PubMed:28388415};
DE AltName: Full=LMBR1 domain-containing protein 2 {ECO:0000312|HGNC:HGNC:25287};
GN Name=LMBRD2 {ECO:0000312|HGNC:HGNC:25287};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28388415; DOI=10.1016/j.cell.2017.03.028;
RA Paek J., Kalocsay M., Staus D.P., Wingler L., Pascolutti R., Paulo J.A.,
RA Gygi S.P., Kruse A.C.;
RT "Multidimensional Tracking of GPCR Signaling via Peroxidase-Catalyzed
RT Proximity Labeling.";
RL Cell 169:338-349(2017).
CC -!- FUNCTION: Recruited to ligand-activated beta-2 adrenergic
CC receptor/ADRB2, it negatively regulates the adrenergic receptor
CC signaling pathway (PubMed:28388415). May also regulate other G-protein
CC coupled receptors including type-1 angiotensin II receptor/AGTR1
CC (Probable). {ECO:0000269|PubMed:28388415, ECO:0000305|PubMed:28388415}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28388415};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the LIMR family. {ECO:0000305}.
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DR EMBL; AK091295; BAG52328.1; -; mRNA.
DR EMBL; CR749399; CAH18245.1; -; mRNA.
DR EMBL; AL137370; CAB70714.1; -; mRNA.
DR EMBL; BC110506; AAI10507.1; -; mRNA.
DR CCDS; CCDS34145.1; -.
DR PIR; T46434; T46434.
DR RefSeq; NP_001007528.1; NM_001007527.1.
DR RefSeq; XP_011512464.1; XM_011514162.2.
DR AlphaFoldDB; Q68DH5; -.
DR SMR; Q68DH5; -.
DR BioGRID; 124923; 60.
DR IntAct; Q68DH5; 22.
DR MINT; Q68DH5; -.
DR STRING; 9606.ENSP00000296603; -.
DR GlyGen; Q68DH5; 1 site.
DR iPTMnet; Q68DH5; -.
DR PhosphoSitePlus; Q68DH5; -.
DR SwissPalm; Q68DH5; -.
DR BioMuta; LMBRD2; -.
DR DMDM; 74708880; -.
DR EPD; Q68DH5; -.
DR jPOST; Q68DH5; -.
DR MassIVE; Q68DH5; -.
DR MaxQB; Q68DH5; -.
DR PaxDb; Q68DH5; -.
DR PeptideAtlas; Q68DH5; -.
DR PRIDE; Q68DH5; -.
DR ProteomicsDB; 66080; -.
DR Antibodypedia; 2569; 16 antibodies from 11 providers.
DR DNASU; 92255; -.
DR Ensembl; ENST00000296603.5; ENSP00000296603.4; ENSG00000164187.7.
DR GeneID; 92255; -.
DR KEGG; hsa:92255; -.
DR MANE-Select; ENST00000296603.5; ENSP00000296603.4; NM_001007527.2; NP_001007528.1.
DR UCSC; uc003jka.2; human.
DR CTD; 92255; -.
DR DisGeNET; 92255; -.
DR GeneCards; LMBRD2; -.
DR HGNC; HGNC:25287; LMBRD2.
DR HPA; ENSG00000164187; Low tissue specificity.
DR MIM; 619490; gene.
DR neXtProt; NX_Q68DH5; -.
DR OpenTargets; ENSG00000164187; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA142671541; -.
DR VEuPathDB; HostDB:ENSG00000164187; -.
DR eggNOG; KOG2296; Eukaryota.
DR GeneTree; ENSGT00390000018651; -.
DR HOGENOM; CLU_018886_0_0_1; -.
DR InParanoid; Q68DH5; -.
DR OMA; ERICYSA; -.
DR OrthoDB; 694650at2759; -.
DR PhylomeDB; Q68DH5; -.
DR TreeFam; TF314938; -.
DR PathwayCommons; Q68DH5; -.
DR SignaLink; Q68DH5; -.
DR BioGRID-ORCS; 92255; 13 hits in 1077 CRISPR screens.
DR GenomeRNAi; 92255; -.
DR Pharos; Q68DH5; Tdark.
DR PRO; PR:Q68DH5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q68DH5; protein.
DR Bgee; ENSG00000164187; Expressed in Brodmann (1909) area 23 and 187 other tissues.
DR Genevisible; Q68DH5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR Pfam; PF04791; LMBR1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..695
FT /note="G-protein coupled receptor-associated protein
FT LMBRD2"
FT /id="PRO_0000299161"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..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..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 581..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..262
FT /evidence="ECO:0000255"
FT COILED 571..603
FT /evidence="ECO:0000255"
FT COMPBIAS 581..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 695 AA; 81172 MW; 653291F14D535BC0 CRC64;
MSGAALGLEI VFVFFLALFL LHRYGDFKKQ HRLVIIGTLL AWYLCFLIVF ILPLDVSTTI
YNRCKHAAAN SSPPENSNIT GLYATANPVP SQHPCFKPWS YIPDGIMPIF WRVVYWTSQF
LTWILLPFMQ SYARSGGFSI TGKIKTALIE NAIYYGTYLL IFGAFLIYVA VNPHLHLEWN
QLQTIGIAAA NTWGLFLLVL LLGYGLVEIP RSYWNGAKRG YLLMKTYFKA AKLMTEKADA
EENLEDAMEE VRKVNESIKY NHPLRKCVDT ILKKCPTEYQ EKMGRNMDDY EDFDEKHSIY
PSEKSLVKLH KQVIYSVQRH RRTQVQWQIL LEQAFYLEDV AKNETSATHQ FVHTFQSPEP
ENRFIQYFYN PTFEWYWECL LRPWFYKILA VVLSIFSVIV VWSECTFFST TPVLSLFAVF
IQLAEKTYNY IYIEIACFLS IFFLSICVYS TVFRIRVFNY YYLASHHQTD AYSLLFSGML
FCRLTPPLCL NFLGLTHMDS SISHKNTQPT AYTSIMGSMK VLSFIADGFY IYYPMLVVIL
CIATYFSLGT RCLNLLGFQQ FMGDDDMTSD LVNEGKELIR KEKRKRQRQE EGENRRREWK
ERYGHNREDS TRNRNIHTDP KESNFSDVNT NRSAFKYTRA NNRTERDRIE LLQDAEPLDF
NAETFTDDPL ESESGRYQPG GRYLSMSRSD IFNDV
