LRBA_MOUSE
ID LRBA_MOUSE Reviewed; 2856 AA.
AC Q9ESE1; Q9ESD3; Q9ESD4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Lipopolysaccharide-responsive and beige-like anchor protein;
DE AltName: Full=Beige-like protein {ECO:0000303|PubMed:11254716};
GN Name=Lrba;
GN Synonyms=Bgl {ECO:0000303|PubMed:11254716},
GN Lba {ECO:0000303|PubMed:11254716};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11254716; DOI=10.4049/jimmunol.166.7.4586;
RA Wang J.-W., Howson J., Haller E., Kerr W.G.;
RT "Identification of a novel lipopolysaccharide-inducible gene with key
RT features of both A kinase anchor proteins and chs1/beige proteins.";
RL J. Immunol. 166:4586-4595(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-1003; SER-1219;
RP SER-1221; SER-1228; SER-1770 AND SER-1773, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in coupling signal transduction and vesicle
CC trafficking to enable polarized secretion and/or membrane deposition of
CC immune effector molecules (PubMed:11254716). Involved in phagophore
CC growth during mitophagy by regulating ATG9A trafficking to mitochondria
CC (By similarity). {ECO:0000250|UniProtKB:P50851,
CC ECO:0000269|PubMed:11254716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11254716};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:11254716}; Single-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11254716}; Single-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:11254716}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=lba-alpha {ECO:0000303|PubMed:11254716};
CC IsoId=Q9ESE1-1; Sequence=Displayed;
CC Name=2; Synonyms=lba-beta {ECO:0000303|PubMed:11254716};
CC IsoId=Q9ESE1-2; Sequence=VSP_038229, VSP_038230;
CC Name=3; Synonyms=lba-gamma {ECO:0000303|PubMed:11254716};
CC IsoId=Q9ESE1-3; Sequence=VSP_038227, VSP_038228;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the brain, is absent from
CC the lung and the bone marrow and is less abundant in the spleen.
CC Isoform 2 is expressed in the spleen, lung, brain and bone marrow.
CC Isoform 3 is expressed in the brain, is absent from the bone marrow and
CC is less abundant in the spleen and lung. {ECO:0000269|PubMed:11254716}.
CC -!- INDUCTION: By lipopolysaccharide (LPS). {ECO:0000269|PubMed:11254716}.
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DR EMBL; AF187731; AAG14003.1; -; mRNA.
DR EMBL; AF188506; AAG15400.1; -; mRNA.
DR EMBL; AF188507; AAG15401.1; -; mRNA.
DR RefSeq; NP_001071155.1; NM_001077687.1.
DR RefSeq; NP_001071156.1; NM_001077688.1.
DR RefSeq; NP_109620.2; NM_030695.2.
DR SMR; Q9ESE1; -.
DR BioGRID; 219824; 1.
DR IntAct; Q9ESE1; 2.
DR STRING; 10090.ENSMUSP00000103261; -.
DR iPTMnet; Q9ESE1; -.
DR PhosphoSitePlus; Q9ESE1; -.
DR EPD; Q9ESE1; -.
DR jPOST; Q9ESE1; -.
DR MaxQB; Q9ESE1; -.
DR PaxDb; Q9ESE1; -.
DR PeptideAtlas; Q9ESE1; -.
DR PRIDE; Q9ESE1; -.
DR ProteomicsDB; 290145; -. [Q9ESE1-1]
DR ProteomicsDB; 290146; -. [Q9ESE1-2]
DR ProteomicsDB; 290147; -. [Q9ESE1-3]
DR DNASU; 80877; -.
DR GeneID; 80877; -.
DR KEGG; mmu:80877; -.
DR CTD; 987; -.
DR MGI; MGI:1933162; Lrba.
DR eggNOG; KOG1787; Eukaryota.
DR InParanoid; Q9ESE1; -.
DR OrthoDB; 153369at2759; -.
DR PhylomeDB; Q9ESE1; -.
DR BioGRID-ORCS; 80877; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Lrba; mouse.
DR PRO; PR:Q9ESE1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ESE1; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; ISA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0016197; P:endosomal transport; TAS:MGI.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISA:MGI.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR CDD; cd06071; Beach; 1.
DR CDD; cd01201; PH_BEACH; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR010508; NBEA-like_DUF1088.
DR InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR InterPro; IPR023362; PH-BEACH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF06469; DUF1088; 1.
DR Pfam; PF15787; DUF4704; 1.
DR Pfam; PF14844; PH_BEACH; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS51783; PH_BEACH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Golgi apparatus; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT CHAIN 2..2856
FT /note="Lipopolysaccharide-responsive and beige-like anchor
FT protein"
FT /id="PRO_0000386545"
FT TRANSMEM 1529..1545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 1298..1340
FT /note="WD 1"
FT DOMAIN 2066..2174
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 2193..2482
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 2584..2626
FT /note="WD 2"
FT REPEAT 2629..2672
FT /note="WD 3"
FT REPEAT 2688..2728
FT /note="WD 4"
FT REPEAT 2770..2809
FT /note="WD 5"
FT REPEAT 2812..2851
FT /note="WD 6"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT MOD_RES 2489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50851"
FT VAR_SEQ 2569..2579
FT /note="ACGTGTHRRQV -> GLPLLSLFAIH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11254716"
FT /id="VSP_038227"
FT VAR_SEQ 2580..2856
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11254716"
FT /id="VSP_038228"
FT VAR_SEQ 2777..2792
FT /note="AIQLSRDGQYLLTGGD -> VSAVGSTLFLLLGSSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11254716"
FT /id="VSP_038229"
FT VAR_SEQ 2793..2856
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11254716"
FT /id="VSP_038230"
SQ SEQUENCE 2856 AA; 317064 MW; 6E7C5DD865384BEA CRC64;
MASEDNRAPS RPPTGDDGGG GGKEETPTEG GALSLKPGLP IRGIRMKFAV LTGLVEVGEV
SNRDIVETVF NLLVGGQFDL EMNFIIQEGE SIMCMVELLE KCDVTCQAEV WSMFTAILKK
SIRNLQVCTE VGLVEKVLGK IEKVDSMIAD LLVDMLGVLA SYNLTVRELK LFFSKLQGDK
GQWPPHAGKL LSVLKHMPQK YGPDAFFNFP GKSAAAIALP PIARWPYQNG FTFHTWLRMD
PVNNINVDKD KPYLYCFRTS KGLGYSAHFV GGCLIITSIK SKGKGFQHCV KFDFKPQKWY
MVTIVHIYNR WKNSELRCYV NGELASYGEI TWFVNTSDTF DKCFLGSSET ADANRVFCGQ
MTAVYLFSDA LNAAQIFAIY QLGLGYKGTF KFKAESDLFL AEHHKLLLYD GKLSSAIAFM
YNPRATDAQL CLESSPKDNP SIFVHSPHAL MLQDVKAVLT HSIQSAMHSI GGVQVLFPLF
AQLDYKQYLS DEVDLTICTT LLAFIMELLK NSIAMQEQML ACKGFLVIGY SLEKSSKSHV
SRAVLELCLA FSKYLSNLQN GMPLLKQLCD HILLNPAVWI HTPAKVQLML YTYLSTEFIG
TVNIYNTIRR VGTVLLIMHT LKYYYWAVNP QDRSGITPKG LDGPRPNQKE ILSLRAFLLM
FIKQLVMKDS GVKEDELQAI LNYLLTMHED DNLMDVLQLL VALMAEHPNS MIPAFDQRNG
LRVIYKLLAS KSEGIRVQAL KALGYFLKHL APKRKAEVML GHGLFSLLAE RLMLQTNLIT
MTMYNVLFEI LIEQICTQVI HKQHPDPDST VKIQNPQILK VIATLLRNSP QCPESMEVRR
AFLSDMIKLF NNSRENRRSL LQCSVWQEWM LSLCYFNPKN SDEQKITEMV YAIFRILLYH
AVKYEWGGWR VWVDTLSITH SKVTFEIHKE NLANIFREEQ RKGDEETGPC SSSLVPEGTG
ATRGVDVSVG SQHEDRKDSP ISPHFTRNSD ENSSIGRASS IDSASNTELQ THDMSSDEKK
VERENQELLD QATVEETATN GAKDDLETSS DAAEPVTINS NSLEPGKDTV TISEVSASIS
SPSEEDAAEM PELLEKSGVE EKEDDDYVEL KVEGSPTEEA GLPTELQGEG LSVAASGGRE
EPDMCGHGCE VQVEAPITKI HNDPETTDSE DSRFPTVATA GSLATSSEVP VPQATVQSDS
HEMLDGGMKA TNLAGETESV SDCADNVSEA PATSEQKITK LDVSSVASDT ERFELKASTS
TEAPQPQRHG LEISRQQEQT AQGTAPDAVD QQRRDSRSTM FRIPEFKWSQ MHQRLLTDLL
FSIETDIQMW RSHSTKTVMD FVNSSDNVIF VHNTIHLISQ VMDNMVMACG GILPLLSAAT
SATHELENIE PTQGLSIEAS VTFLQRLISL VDVLIFASSL GFTEIEAEKN MSSGGILRQC
LRLVCAVAVR NCLECQQHSQ LKARGDTAKS SKTIHSLIPM GKSAAKSPVD IVTGGISSVR
DLDRLPARTW TLIGLRAVVF RDIEDSKQAQ FLALAVVYFI SVLMVSKYRD ILEPQDERHS
QSLKETSSDN GNASLPDAEN TPAEFSSLTL SSVEESLEGT SCTRRRDSGL GEETASGLGS
GLSVASPAAP LGVSAGPDAI SEVLCTLSLE VNKSQETRID GGNELDRKVT PSVPVSKNVN
VKDILRSLVN MPADGVTVDP ALLPPACLGA LGDLSVDPPM QFRSFDRSVI IATKKSSVLP
SALTTSAPSS AVSVVSSVDP THASDTGGES PGSRSPKCKT ALSCKQLAPS HKTPAAHMSI
TERLEHALEK AAPLLREIFV DFAPFLSRTL LGSHGQELLI EGTSLVCMKS SSSVVELVML
LCSQEWQNSI QKNAGLAFIE LVNEGRLLSQ TMKDHLVRVA NEAEFILSRQ RAEDIHRHAE
FESLCAQYSA DKREEEKMCD HLIRAAKYRD HVTATQLIQK IINLLTDKHG AWGSSAVSRP
REFWRLDYWE DDLRRRRRFV RNPLGSTHPE ATLKTAVEHA ADEDILAKGK QSIKSQALGN
QNSENEALLE GDDDTLSSVD EKDLENLAGP VSLSTPAQLV APSVVVKGTL SVTSSELYFE
VDEEDPNFKK IDPKILAYTE GLHGKWLFTE IRSIFSRRYL LQNTALEIFM ANRVAVMFNF
PDPATVKKVV NYLPRVGVGT SFGLPQTRRI SLATPRQLFK ASNMTQRWQH REISNFEYLM
FLNTIAGRSY NDLNQYPVFP WVITNYESEE LDLTLPSNFR DLSKPIGALN PKRAAFFAER
FESWEDDQVP KFHYGTHYST ASFVLAWLLR IEPFTTYFLN LQGGKFDHAD RTFSSVSRAW
RNSQRDTSDI KELIPEFYYL PEMFVNFNNY NLGVMDDGTV VSDVELPPWA KTSEEFVRIN
RLALESEFVS CQLHQWIDLI FGYKQQGPEA VRALNVFYYL TYEGAVNLNS ITDPVLREAV
EAQIRSFGQT PSQLLIEPHP PRGSAMQASP LMFTDQAQQD VIMVLKFPSN SPVTHVAANT
QPGLAMPAVI TVTANRLFAV NKWHNLPAHQ GAVQDQPYQL PVEIDPLIAC GTGTHRRQVT
DLLDQSIQVH SQCFVITSDN RYILVCGFWD KSFRVYSTDT GKLIQVVFGH WDVVTCLARS
ESYIGGNCYI LSGSRDATLL LWYWNGKSSG IGDNPGGETA TPRAILTGHD YEITCAAVCA
ELGLVLSGSQ EGPCLIHSMN GDLLRTLEGP ENCLKPKLIQ ASREGHCVIF YENGCFCTFS
VNGKLQATVE TDDHIRAIQL SRDGQYLLTG GDNGVVIVRQ VSDLKQLFAY PGCDAGIRAM
ALSFDQRCII SGMASGSIVL FYNDFNRWHH EYQTRY
