LRBA_HUMAN
ID LRBA_HUMAN Reviewed; 2863 AA.
AC P50851; Q4W5J4; Q4W5L6; Q8NFQ0; Q9H2U3; Q9H2U4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Lipopolysaccharide-responsive and beige-like anchor protein;
DE AltName: Full=Beige-like protein {ECO:0000303|PubMed:11254716};
DE AltName: Full=CDC4-like protein {ECO:0000303|PubMed:1505956};
GN Name=LRBA {ECO:0000303|PubMed:15554694, ECO:0000312|HGNC:HGNC:1742};
GN Synonyms=BGL {ECO:0000303|PubMed:1505956},
GN CDC4L {ECO:0000303|PubMed:1505956}, LBA {ECO:0000303|PubMed:11254716};
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 [MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP GLY-1090.
RX PubMed=12160729; DOI=10.1006/geno.2002.6822;
RA Dyomin V.G., Chaganti S.R., Dyomina K., Palanisamy N., Murty V.V.V.S.,
RA Dalla-Favera R., Chaganti R.S.K.;
RT "BCL8 is a novel, evolutionarily conserved human gene family encoding
RT proteins with presumptive protein kinase A anchoring function.";
RL Genomics 80:158-165(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 775-2863 (ISOFORM 1).
RA Mager D.L.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2179-2863 (ISOFORM 1).
RX PubMed=1505956; DOI=10.1016/0888-7543(92)90041-p;
RA Feuchter A.E., Freeman J.D., Mager D.L.;
RT "Strategy for detecting cellular transcripts promoted by human endogenous
RT long terminal repeats: identification of a novel gene (CDC4L) with homology
RT to yeast CDC4.";
RL Genomics 13:1237-1246(1992).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10; SER-1100 AND SER-1139, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-1135; SER-1247;
RP SER-1261; SER-1488; SER-1498; SER-2064 AND SER-2496, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261 AND SER-1605, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION.
RX PubMed=33773106; DOI=10.1016/j.molcel.2021.03.001;
RA Nguyen T.N., Padman B.S., Zellner S., Khuu G., Uoselis L., Lam W.K.,
RA Skulsuppaisarn M., Lindblom R.S.J., Watts E.M., Behrends C., Lazarou M.;
RT "ATG4 family proteins drive phagophore growth independently of the
RT LC3/GABARAP lipidation system.";
RL Mol. Cell 81:2013-2030(2021).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2076-2489.
RX PubMed=15554694; DOI=10.1021/bi049498y;
RA Gebauer D., Li J., Jogl G., Shen Y., Myszka D.G., Tong L.;
RT "Crystal structure of the PH-BEACH domains of human LRBA/BGL.";
RL Biochemistry 43:14873-14880(2004).
RN [19]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-2038; ARG-2274 AND LYS-2701.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [20]
RP VARIANT CVID8 SER-2657.
RX PubMed=22608502; DOI=10.1016/j.ajhg.2012.04.015;
RA Lopez-Herrera G., Tampella G., Pan-Hammarstrom Q., Herholz P.,
RA Trujillo-Vargas C.M., Phadwal K., Simon A.K., Moutschen M., Etzioni A.,
RA Mory A., Srugo I., Melamed D., Hultenby K., Liu C., Baronio M., Vitali M.,
RA Philippet P., Dideberg V., Aghamohammadi A., Rezaei N., Enright V., Du L.,
RA Salzer U., Eibel H., Pfeifer D., Veelken H., Stauss H., Lougaris V.,
RA Plebani A., Gertz E.M., Schaffer A.A., Hammarstrom L., Grimbacher B.;
RT "Deleterious mutations in LRBA are associated with a syndrome of immune
RT deficiency and autoimmunity.";
RL Am. J. Hum. Genet. 90:986-1001(2012).
CC -!- FUNCTION: Involved in coupling signal transduction and vesicle
CC trafficking to enable polarized secretion and/or membrane deposition of
CC immune effector molecules (By similarity). Involved in phagophore
CC growth during mitophagy by regulating ATG9A trafficking to mitochondria
CC (PubMed:33773106). {ECO:0000250|UniProtKB:Q9ESE1,
CC ECO:0000269|PubMed:33773106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ESE1};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q9ESE1}; Single-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9ESE1}; Single-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9ESE1};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50851-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50851-2; Sequence=VSP_038225, VSP_038226;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12160729}.
CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS).
CC -!- DISEASE: Immunodeficiency, common variable, 8, with autoimmunity
CC (CVID8) [MIM:614700]: An autosomal recessive immunologic disorder
CC associated with defective B-cell differentiation and decreased or
CC absent antibody production. Affected individuals have early-childhood
CC onset of recurrent infections, particularly respiratory infections, and
CC also develop variable autoimmune disorders, including idiopathic
CC thrombocytopenic purpura, autoimmune hemolytic anemia, and inflammatory
CC bowel disease. {ECO:0000269|PubMed:22608502}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- CAUTION: Was originally said to be similar to yeast CDC4, but that
CC similarity is very limited. {ECO:0000305|PubMed:1505956}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09603.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF216648; AAG48558.2; -; mRNA.
DR EMBL; AF217149; AAG48559.1; -; mRNA.
DR EMBL; AF467287; AAM53530.1; -; mRNA.
DR EMBL; AC092544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093748; AAY40984.1; -; Genomic_DNA.
DR EMBL; AC097373; AAY40973.1; -; Genomic_DNA.
DR EMBL; AC104796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M83822; AAB09603.1; ALT_FRAME; mRNA.
DR CCDS; CCDS3773.1; -. [P50851-1]
DR CCDS; CCDS58928.1; -. [P50851-2]
DR RefSeq; NP_001186211.2; NM_001199282.2. [P50851-2]
DR RefSeq; NP_006717.2; NM_006726.4. [P50851-1]
DR RefSeq; XP_011530736.1; XM_011532434.2. [P50851-1]
DR PDB; 1T77; X-ray; 2.40 A; A/B/C/D=2076-2489.
DR PDBsum; 1T77; -.
DR SMR; P50851; -.
DR BioGRID; 107423; 122.
DR DIP; DIP-50531N; -.
DR IntAct; P50851; 31.
DR MINT; P50851; -.
DR STRING; 9606.ENSP00000349629; -.
DR GlyGen; P50851; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P50851; -.
DR MetOSite; P50851; -.
DR PhosphoSitePlus; P50851; -.
DR SwissPalm; P50851; -.
DR BioMuta; LRBA; -.
DR DMDM; 259016388; -.
DR EPD; P50851; -.
DR jPOST; P50851; -.
DR MassIVE; P50851; -.
DR MaxQB; P50851; -.
DR PaxDb; P50851; -.
DR PeptideAtlas; P50851; -.
DR PRIDE; P50851; -.
DR ProteomicsDB; 56265; -. [P50851-1]
DR ProteomicsDB; 56266; -. [P50851-2]
DR Antibodypedia; 16513; 72 antibodies from 17 providers.
DR DNASU; 987; -.
DR Ensembl; ENST00000357115.9; ENSP00000349629.3; ENSG00000198589.14. [P50851-1]
DR Ensembl; ENST00000510413.5; ENSP00000421552.1; ENSG00000198589.14. [P50851-2]
DR GeneID; 987; -.
DR KEGG; hsa:987; -.
DR UCSC; uc003ilu.5; human. [P50851-1]
DR CTD; 987; -.
DR DisGeNET; 987; -.
DR GeneCards; LRBA; -.
DR HGNC; HGNC:1742; LRBA.
DR HPA; ENSG00000198589; Low tissue specificity.
DR MalaCards; LRBA; -.
DR MIM; 606453; gene.
DR MIM; 614700; phenotype.
DR neXtProt; NX_P50851; -.
DR OpenTargets; ENSG00000198589; -.
DR Orphanet; 445018; Combined immunodeficiency due to LRBA deficiency.
DR PharmGKB; PA30444; -.
DR VEuPathDB; HostDB:ENSG00000198589; -.
DR eggNOG; KOG1787; Eukaryota.
DR GeneTree; ENSGT00940000154778; -.
DR HOGENOM; CLU_000218_2_0_1; -.
DR InParanoid; P50851; -.
DR OrthoDB; 153369at2759; -.
DR PhylomeDB; P50851; -.
DR TreeFam; TF313490; -.
DR PathwayCommons; P50851; -.
DR SignaLink; P50851; -.
DR SIGNOR; P50851; -.
DR BioGRID-ORCS; 987; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; LRBA; human.
DR EvolutionaryTrace; P50851; -.
DR GeneWiki; LRBA; -.
DR GenomeRNAi; 987; -.
DR Pharos; P50851; Tbio.
DR PRO; PR:P50851; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P50851; protein.
DR Bgee; ENSG00000198589; Expressed in upper leg skin and 188 other tissues.
DR ExpressionAtlas; P50851; baseline and differential.
DR Genevisible; P50851; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Disease variant; Endoplasmic reticulum; Golgi apparatus;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..2863
FT /note="Lipopolysaccharide-responsive and beige-like anchor
FT protein"
FT /id="PRO_0000051068"
FT TRANSMEM 1531..1548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 1301..1343
FT /note="WD 1"
FT DOMAIN 2073..2181
FT /note="BEACH-type PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT DOMAIN 2200..2489
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT REPEAT 2591..2633
FT /note="WD 2"
FT REPEAT 2636..2679
FT /note="WD 3"
FT REPEAT 2695..2735
FT /note="WD 4"
FT REPEAT 2777..2816
FT /note="WD 5"
FT REPEAT 2819..2858
FT /note="WD 6"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1006..1053
FT /evidence="ECO:0000255"
FT COMPBIAS 1173..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESE1"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESE1"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESE1"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESE1"
FT MOD_RES 2064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 2016..2026
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12160729"
FT /id="VSP_038225"
FT VAR_SEQ 2684
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12160729"
FT /id="VSP_038226"
FT VARIANT 1090
FT /note="A -> G (in dbSNP:rs1782360)"
FT /evidence="ECO:0000269|PubMed:12160729"
FT /id="VAR_057605"
FT VARIANT 1230
FT /note="G -> D (in dbSNP:rs34708681)"
FT /id="VAR_057606"
FT VARIANT 1677
FT /note="N -> S (in dbSNP:rs17027133)"
FT /id="VAR_057607"
FT VARIANT 1997
FT /note="R -> C (in dbSNP:rs35879351)"
FT /id="VAR_057608"
FT VARIANT 2038
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035883"
FT VARIANT 2274
FT /note="G -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035884"
FT VARIANT 2657
FT /note="I -> S (in CVID8; dbSNP:rs199469663)"
FT /evidence="ECO:0000269|PubMed:22608502"
FT /id="VAR_068690"
FT VARIANT 2701
FT /note="T -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035885"
FT VARIANT 2704
FT /note="A -> T (in dbSNP:rs3749574)"
FT /id="VAR_057609"
FT VARIANT 2713
FT /note="L -> F (in dbSNP:rs34662958)"
FT /id="VAR_057610"
FT VARIANT 2809
FT /note="S -> L (in dbSNP:rs2290846)"
FT /id="VAR_022028"
FT CONFLICT 377
FT /note="F -> L (in Ref. 2; AAM53530)"
FT /evidence="ECO:0000305"
FT CONFLICT 750..751
FT /note="LA -> RP (in Ref. 1; AAG48558)"
FT /evidence="ECO:0000305"
FT CONFLICT 2179
FT /note="Y -> F (in Ref. 1; AAG48558 and 3; AAB09603)"
FT /evidence="ECO:0000305"
FT STRAND 2079..2087
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2092..2099
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2101..2108
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2113..2117
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2120..2125
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2132..2134
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2135..2137
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2138..2146
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2149..2157
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2162..2166
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2170..2179
FT /evidence="ECO:0007829|PDB:1T77"
FT TURN 2195..2199
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2202..2208
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2211..2216
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2222..2233
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2240..2242
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2254..2257
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2263..2265
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2273..2276
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2278..2290
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2294..2296
FT /evidence="ECO:0007829|PDB:1T77"
FT STRAND 2300..2303
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2308..2315
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2321..2329
FT /evidence="ECO:0007829|PDB:1T77"
FT TURN 2336..2338
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2343..2352
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2362..2365
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2368..2371
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2400..2412
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2414..2417
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2420..2427
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2434..2440
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2446..2448
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2455..2457
FT /evidence="ECO:0007829|PDB:1T77"
FT HELIX 2461..2474
FT /evidence="ECO:0007829|PDB:1T77"
SQ SEQUENCE 2863 AA; 319108 MW; 58CD1F4314F685EE CRC64;
MASEDNRVPS PPPTGDDGGG GGREETPTEG GALSLKPGLP IRGIRMKFAV LTGLVEVGEV
SNRDIVETVF NLLVGGQFDL EMNFIIQEGE SINCMVDLLE KCDITCQAEV WSMFTAILKK
SIRNLQVCTE VGLVEKVLGK IEKVDNMIAD LLVDMLGVLA SYNLTVRELK LFFSKLQGDK
GRWPPHAGKL LSVLKHMPQK YGPDAFFNFP GKSAAAIALP PIAKWPYQNG FTFHTWLRMD
PVNNINVDKD KPYLYCFRTS KGLGYSAHFV GGCLIVTSIK SKGKGFQHCV KFDFKPQKWY
MVTIVHIYNR WKNSELRCYV NGELASYGEI TWFVNTSDTF DKCFLGSSET ADANRVFCGQ
MTAVYLFSEA LNAAQIFAIY QLGLGYKGTF KFKAESDLFL AEHHKLLLYD GKLSSAIAFT
YNPRATDAQL CLESSPKDNP SIFVHSPHAL MLQDVKAVLT HSIQSAMHSI GGVQVLFPLF
AQLDYRQYLS DEIDLTICST LLAFIMELLK NSIAMQEQML ACKGFLVIGY SLEKSSKSHV
SRAVLELCLA FSKYLSNLQN GMPLLKQLCD HVLLNPAIWI HTPAKVQLML YTYLSTEFIG
TVNIYNTIRR VGTVLLIMHT LKYYYWAVNP QDRSGITPKG LDGPRPNQKE MLSLRAFLLM
FIKQLVMKDS GVKEDELQAI LNYLLTMHED DNLMDVLQLL VALMSEHPNS MIPAFDQRNG
LRVIYKLLAS KSEGIRVQAL KAMGYFLKHL APKRKAEVML GHGLFSLLAE RLMLQTNLIT
MTTYNVLFEI LIEQIGTQVI HKQHPDPDSS VKIQNPQILK VIATLLRNSP QCPESMEVRR
AFLSDMIKLF NNSRENRRSL LQCSVWQEWM LSLCYFNPKN SDEQKITEMV YAIFRILLYH
AVKYEWGGWR VWVDTLSITH SKVTFEIHKE NLANIFREQQ GKVDEEIGLC SSTSVQAASG
IRRDINVSVG SQQPDTKDSP VCPHFTTNGN ENSSIEKTSS LESASNIELQ TTNTSYEEMK
AEQENQELPD EGTLEETLTN ETRNADDLEV SSDIIEAVAI SSNSFITTGK DSMTVSEVTA
SISSPSEEDA SEMPEFLDKS IVEEEEDDDY VELKVEGSPT EEANLPTELQ DNSLSPAASE
AGEKLDMFGN DDKLIFQEGK PVTEKQTDTE TQDSKDSGIQ TMTASGSSAM SPETTVSQIA
VESDLGQMLE EGKKATNLTR ETKLINDCHG SVSEASSEQK IAKLDVSNVA TDTERLELKA
SPNVEAPQPH RHVLEISRQH EQPGQGIAPD AVNGQRRDSR STVFRIPEFN WSQMHQRLLT
DLLFSIETDI QMWRSHSTKT VMDFVNSSDN VIFVHNTIHL ISQVMDNMVM ACGGILPLLS
AATSATHELE NIEPTQGLSI EASVTFLQRL ISLVDVLIFA SSLGFTEIEA EKSMSSGGIL
RQCLRLVCAV AVRNCLECQQ HSQLKTRGDK ALKPMHSLIP LGKSAAKSPV DIVTGGISPV
RDLDRLLQDM DINRLRAVVF RDIEDSKQAQ FLALAVVYFI SVLMVSKYRD ILEPQNERHS
QSCTETGSEN ENVSLSEITP AAFSTLTTAS VEESESTSSA RRRDSGIGEE TATGLGSHVE
VTPHTAPPGV SAGPDAISEV LSTLSLEVNK SPETKNDRGN DLDTKATPSV SVSKNVNVKD
ILRSLVNIPA DGVTVDPALL PPACLGALGD LSVEQPVQFR SFDRSVIVAA KKSAVSPSTF
NTSIPTNAVS VVSSVDSAQA SDMGGESPGS RSSNAKLPSV PTVDSVSQDP VSNMSITERL
EHALEKAAPL LREIFVDFAP FLSRTLLGSH GQELLIEGTS LVCMKSSSSV VELVMLLCSQ
EWQNSIQKNA GLAFIELVNE GRLLSQTMKD HLVRVANEAE FILSRQRAED IHRHAEFESL
CAQYSADKRE DEKMCDHLIR AAKYRDHVTA TQLIQKIINI LTDKHGAWGN SAVSRPLEFW
RLDYWEDDLR RRRRFVRNPL GSTHPEATLK TAVEHVCIFK LRENSKATDE DILAKGKQSI
RSQALGNQNS ENEILLEGDD DTLSSVDEKD LENLAGPVSL STPAQLVAPS VVVKGTLSVT
SSELYFEVDE EDPNFKKIDP KILAYTEGLH GKWLFTEIRS IFSRRYLLQN TALEIFMANR
VAVMFNFPDP ATVKKVVNYL PRVGVGTSFG LPQTRRISLA SPRQLFKASN MTQRWQHREI
SNFEYLMFLN TIAGRSYNDL NQYPVFPWVI TNYESEELDL TLPTNFRDLS KPIGALNPKR
AAFFAERYES WEDDQVPKFH YGTHYSTASF VLAWLLRIEP FTTYFLNLQG GKFDHADRTF
SSISRAWRNS QRDTSDIKEL IPEFYYLPEM FVNFNNYNLG VMDDGTVVSD VELPPWAKTS
EEFVHINRLA LESEFVSCQL HQWIDLIFGY KQQGPEAVRA LNVFYYLTYE GAVNLNSITD
PVLREAVEAQ IRSFGQTPSQ LLIEPHPPRG SAMQVSPLMF TDKAQQDVIM VLKFPSNSPV
THVAANTQPG LATPAVITVT ANRLFAVNKW HNLPAHQGAV QDQPYQLPVE IDPLIASNTG
MHRRQITDLL DQSIQVHSQC FVITSDNRYI LVCGFWDKSF RVYSTDTGRL IQVVFGHWDV
VTCLARSESY IGGNCYILSG SRDATLLLWY WNGKCSGIGD NPGSETAAPR AILTGHDYEV
TCAAVCAELG LVLSGSQEGP CLIHSMNGDL LRTLEGPENC LKPKLIQASR EGHCVIFYEN
GLFCTFSVNG KLQATMETDD NIRAIQLSRD GQYLLTGGDR GVVVVRQVSD LKQLFAYPGC
DAGIRAMALS YDQRCIISGM ASGSIVLFYN DFNRWHHEYQ TRY
