ID   UN93B_HUMAN             Reviewed;         597 AA.
AC   Q9H1C4; O95764; Q569H6; Q710D4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Protein unc-93 homolog B1 {ECO:0000305};
DE            Short=Unc-93B1;
DE            Short=hUNC93B1;
GN   Name=UNC93B1 {ECO:0000312|HGNC:HGNC:13481}; Synonyms=UNC93, UNC93B;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=11867227; DOI=10.1016/s0378-1119(01)00856-3;
RA   Kashuba V.I., Protopopov A.I., Kvasha S.M., Gizatullin R.Z., Wahlestedt C.,
RA   Kisselev L.L., Klein G., Zabarovsky E.R.;
RT   "hUNC93B1: a novel human gene representing a new gene family and encoding
RT   an unc-93-like protein.";
RL   Gene 283:209-217(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-497.
RC   TISSUE=Uterus;
RA   Kollewe A.;
RT   "Cloning and characterization of mammalian homologs of unc-93 from
RT   Caenorhabditis elegans, a protein relevant for muscle contraction.";
RL   Thesis (2001), University of Hannover, Germany.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP   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   [6]
RP   INVOLVEMENT IN IIAE1.
RX   PubMed=16973841; DOI=10.1126/science.1128346;
RA   Casrouge A., Zhang S.-Y., Eidenschenk C., Jouanguy E., Puel A., Yang K.,
RA   Alcais A., Picard C., Mahfoufi N., Nicolas N., Lorenzo L., Plancoulaine S.,
RA   Senechal B., Geissmann F., Tabeta K., Hoebe K., Du X., Miller R.L.,
RA   Heron B., Mignot C., de Villemeur T.B., Lebon P., Dulac O., Rozenberg F.,
RA   Beutler B., Tardieu M., Abel L., Casanova J.-L.;
RT   "Herpes simplex virus encephalitis in human UNC-93B deficiency.";
RL   Science 314:308-312(2006).
RN   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18082565; DOI=10.1016/j.humimm.2007.07.007;
RA   Koehn J., Huesken D., Jaritz M., Rot A., Zurini M., Dwertmann A.,
RA   Beutler B., Korthaeuer U.;
RT   "Assessing the function of human UNC-93B in Toll-like receptor signaling
RT   and major histocompatibility complex II response.";
RL   Hum. Immunol. 68:871-878(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=19006693; DOI=10.1016/j.immuni.2008.09.015;
RA   Isnardi I., Ng Y.S., Srdanovic I., Motaghedi R., Rudchenko S.,
RA   von Bernuth H., Zhang S.Y., Puel A., Jouanguy E., Picard C., Garty B.Z.,
RA   Camcioglu Y., Doffinger R., Kumararatne D., Davies G., Gallin J.I.,
RA   Haraguchi S., Day N.K., Casanova J.L., Meffre E.;
RT   "IRAK-4- and MyD88-dependent pathways are essential for the removal of
RT   developing autoreactive B cells in humans.";
RL   Immunity 29:746-757(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-550, AND
RP   IDENTIFICATION BY 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [11]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21642595; DOI=10.1182/blood-2010-11-319699;
RA   Defays A., David A., de Gassart A., De Angelis Rigotti F., Wenger T.,
RA   Camossetto V., Brousset P., Petrella T., Dalod M., Gatti E., Pierre P.;
RT   "BAD-LAMP is a novel biomarker of nonactivated human plasmacytoid dendritic
RT   cells.";
RL   Blood 118:609-617(2011).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-550, AND
RP   IDENTIFICATION BY 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   [14]
RP   INTERACTION WITH TLR5.
RX   PubMed=24778236; DOI=10.1073/pnas.1322838111;
RA   Huh J.W., Shibata T., Hwang M., Kwon E.H., Jang M.S., Fukui R., Kanno A.,
RA   Jung D.J., Jang M.H., Miyake K., Kim Y.M.;
RT   "UNC93B1 is essential for the plasma membrane localization and signaling of
RT   Toll-like receptor 5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7072-7077(2014).
RN   [15] {ECO:0007744|PDB:7C76, ECO:0007744|PDB:7CYN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) IN COMPLEX WITH TLR3 AND
RP   TLR7, AND INTERACTION WITH TLR3 AND TLR7.
RX   PubMed=33432245; DOI=10.1038/s41594-020-00542-w;
RA   Ishida H., Asami J., Zhang Z., Nishizawa T., Shigematsu H., Ohto U.,
RA   Shimizu T.;
RT   "Cryo-EM structures of Toll-like receptors in complex with UNC93B1.";
RL   Nat. Struct. Mol. Biol. 28:173-180(2021).
CC   -!- FUNCTION: Plays an important role in innate and adaptive immunity by
CC       regulating nucleotide-sensing Toll-like receptor (TLR) signaling.
CC       Required for the transport of a subset of TLRs (including TLR3, TLR7
CC       and TLR9) from the endoplasmic reticulum to endolysosomes where they
CC       can engage pathogen nucleotides and activate signaling cascades. May
CC       play a role in autoreactive B-cells removal.
CC       {ECO:0000269|PubMed:19006693}.
CC   -!- SUBUNIT: Interacts with TLR3, TLR5, TLR7, and TLR9 (probably via
CC       transmembrane domain). {ECO:0000250|UniProtKB:Q8VCW4,
CC       ECO:0000269|PubMed:24778236, ECO:0000269|PubMed:33432245}.
CC   -!- INTERACTION:
CC       Q9H1C4; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-4401271, EBI-19947314;
CC       Q9H1C4; Q8WV48: CCDC107; NbExp=3; IntAct=EBI-4401271, EBI-947033;
CC       Q9H1C4; P11912: CD79A; NbExp=3; IntAct=EBI-4401271, EBI-7797864;
CC       Q9H1C4; O95471: CLDN7; NbExp=3; IntAct=EBI-4401271, EBI-740744;
CC       Q9H1C4; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-4401271, EBI-6942903;
CC       Q9H1C4; P55060: CSE1L; NbExp=2; IntAct=EBI-4401271, EBI-286709;
CC       Q9H1C4; Q15125: EBP; NbExp=3; IntAct=EBI-4401271, EBI-3915253;
CC       Q9H1C4; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-4401271, EBI-781551;
CC       Q9H1C4; Q969F0: FATE1; NbExp=3; IntAct=EBI-4401271, EBI-743099;
CC       Q9H1C4; O14843: FFAR3; NbExp=3; IntAct=EBI-4401271, EBI-17762181;
CC       Q9H1C4; Q96P66: GPR101; NbExp=3; IntAct=EBI-4401271, EBI-17935713;
CC       Q9H1C4; O60883: GPR37L1; NbExp=3; IntAct=EBI-4401271, EBI-2927498;
CC       Q9H1C4; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-4401271, EBI-13067820;
CC       Q9H1C4; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-4401271, EBI-2867874;
CC       Q9H1C4; P26715: KLRC1; NbExp=3; IntAct=EBI-4401271, EBI-9018187;
CC       Q9H1C4; Q14974: KPNB1; NbExp=2; IntAct=EBI-4401271, EBI-286758;
CC       Q9H1C4; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-4401271, EBI-10173166;
CC       Q9H1C4; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-4401271, EBI-17490413;
CC       Q9H1C4; Q9H400: LIME1; NbExp=3; IntAct=EBI-4401271, EBI-2830566;
CC       Q9H1C4; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-4401271, EBI-11956541;
CC       Q9H1C4; Q9H902: REEP1; NbExp=3; IntAct=EBI-4401271, EBI-1644241;
CC       Q9H1C4; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-4401271, EBI-17295964;
CC       Q9H1C4; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-4401271, EBI-17280858;
CC       Q9H1C4; Q9H7V2: SYNDIG1; NbExp=3; IntAct=EBI-4401271, EBI-726331;
CC       Q9H1C4; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-4401271, EBI-13351685;
CC       Q9H1C4; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-4401271, EBI-10982110;
CC       Q9H1C4; P0DTD8: 7b; Xeno; NbExp=2; IntAct=EBI-4401271, EBI-25475914;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Endosome {ECO:0000250}.
CC       Lysosome {ECO:0000250}. Cytoplasmic vesicle, phagosome {ECO:0000250}.
CC       Note=Relocalizes from endoplasmic reticulum to endosome and lysosome
CC       upon cell-stimulation with CpG dinucleotides (By similarity).
CC       Colocalizes with LAMP5 in large endosomal intracellular vesicles.
CC       {ECO:0000250, ECO:0000269|PubMed:18082565,
CC       ECO:0000269|PubMed:21642595}.
CC   -!- TISSUE SPECIFICITY: Expressed in plasmocytoid dendritic cells (at
CC       protein level). Highly expressed in antigen-presenting cells. Expressed
CC       in heart, and at lower level in kidney. Expressed at low level in other
CC       tissues. {ECO:0000269|PubMed:11867227, ECO:0000269|PubMed:18082565,
CC       ECO:0000269|PubMed:21642595}.
CC   -!- INDUCTION: Up-regulated by TLRs agonists.
CC       {ECO:0000269|PubMed:18082565}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- DISEASE: Encephalopathy, acute, infection-induced, 1, herpes-specific
CC       (IIAE1) [MIM:610551]: A rare complication of human herpesvirus 1 (HHV-
CC       1) infection, occurring in only a small minority of HHV-1 infected
CC       individuals. It is characterized by hemorrhagic necrosis of parts of
CC       the temporal and frontal lobes. Onset is over several days and involves
CC       fever, headache, seizures, stupor, and often coma, frequently with a
CC       fatal outcome. {ECO:0000269|PubMed:16973841}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry. Mutations in UNC93B1 resulting in autosomal
CC       recessive UNC93B1 deficiency predispose otherwise healthy individuals
CC       to isolated herpes simplex encephalitis due to impaired IFNs
CC       production. UNC93B1 deficiency, however, does not compromise immunity
CC       to most pathogens, unlike most known primary immunodeficiencies.
CC   -!- SIMILARITY: Belongs to the unc-93 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=UNC93B1base; Note=UNC93B1 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/UNC93B1base/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ271326; CAC19791.1; -; mRNA.
DR   EMBL; AC004923; AAD15416.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC092472; AAH92472.1; -; mRNA.
DR   EMBL; BC101568; AAI01569.1; -; mRNA.
DR   EMBL; BC105104; AAI05105.1; -; mRNA.
DR   EMBL; AJ422142; CAD19522.1; -; mRNA.
DR   CCDS; CCDS73334.1; -.
DR   RefSeq; NP_112192.2; NM_030930.3.
DR   PDB; 7C76; EM; 3.40 A; B=1-597.
DR   PDB; 7CYN; EM; 4.20 A; C/D=1-597.
DR   PDBsum; 7C76; -.
DR   PDBsum; 7CYN; -.
DR   AlphaFoldDB; Q9H1C4; -.
DR   EMDB; EMD-30293; -.
DR   EMDB; EMD-30501; -.
DR   SMR; Q9H1C4; -.
DR   BioGRID; 123557; 463.
DR   IntAct; Q9H1C4; 360.
DR   MINT; Q9H1C4; -.
DR   STRING; 9606.ENSP00000227471; -.
DR   TCDB; 2.A.1.58.7; the major facilitator superfamily (mfs).
DR   GlyCosmos; Q9H1C4; 3 sites, No reported glycans.
DR   GlyGen; Q9H1C4; 4 sites.
DR   iPTMnet; Q9H1C4; -.
DR   PhosphoSitePlus; Q9H1C4; -.
DR   SwissPalm; Q9H1C4; -.
DR   BioMuta; UNC93B1; -.
DR   DMDM; 67462081; -.
DR   EPD; Q9H1C4; -.
DR   jPOST; Q9H1C4; -.
DR   MassIVE; Q9H1C4; -.
DR   MaxQB; Q9H1C4; -.
DR   PaxDb; 9606-ENSP00000227471; -.
DR   PeptideAtlas; Q9H1C4; -.
DR   ProteomicsDB; 80398; -.
DR   Pumba; Q9H1C4; -.
DR   ABCD; Q9H1C4; 12 sequenced antibodies.
DR   Antibodypedia; 30503; 136 antibodies from 24 providers.
DR   DNASU; 81622; -.
DR   Ensembl; ENST00000227471.7; ENSP00000227471.3; ENSG00000110057.9.
DR   GeneID; 81622; -.
DR   KEGG; hsa:81622; -.
DR   MANE-Select; ENST00000227471.7; ENSP00000227471.3; NM_030930.4; NP_112192.2.
DR   UCSC; uc031xth.1; human.
DR   AGR; HGNC:13481; -.
DR   CTD; 81622; -.
DR   DisGeNET; 81622; -.
DR   GeneCards; UNC93B1; -.
DR   HGNC; HGNC:13481; UNC93B1.
DR   HPA; ENSG00000110057; Tissue enhanced (lymphoid).
DR   MalaCards; UNC93B1; -.
DR   MIM; 608204; gene.
DR   MIM; 610551; phenotype.
DR   neXtProt; NX_Q9H1C4; -.
DR   OpenTargets; ENSG00000110057; -.
DR   Orphanet; 1930; Herpes simplex virus encephalitis.
DR   PharmGKB; PA37781; -.
DR   VEuPathDB; HostDB:ENSG00000110057; -.
DR   eggNOG; KOG3097; Eukaryota.
DR   GeneTree; ENSGT00530000063359; -.
DR   HOGENOM; CLU_037591_1_0_1; -.
DR   InParanoid; Q9H1C4; -.
DR   OMA; FWAPKPR; -.
DR   OrthoDB; 5315849at2759; -.
DR   PhylomeDB; Q9H1C4; -.
DR   TreeFam; TF314905; -.
DR   PathwayCommons; Q9H1C4; -.
DR   Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
DR   Reactome; R-HSA-5602415; UNC93B1 deficiency - HSE.
DR   SignaLink; Q9H1C4; -.
DR   BioGRID-ORCS; 81622; 13 hits in 324 CRISPR screens.
DR   ChiTaRS; UNC93B1; human.
DR   GeneWiki; UNC93B1; -.
DR   GenomeRNAi; 81622; -.
DR   Pharos; Q9H1C4; Tbio.
DR   PRO; PR:Q9H1C4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9H1C4; Protein.
DR   Bgee; ENSG00000110057; Expressed in granulocyte and 105 other cell types or tissues.
DR   ExpressionAtlas; Q9H1C4; baseline and differential.
DR   GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
DR   GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR   GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR   GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd17408; MFS_unc93B1; 1.
DR   InterPro; IPR043268; UNC93B1.
DR   PANTHER; PTHR46744; PROTEIN UNC-93 HOMOLOG B1; 1.
DR   PANTHER; PTHR46744:SF1; PROTEIN UNC-93 HOMOLOG B1; 1.
DR   Genevisible; Q9H1C4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Antiviral defense; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; Endosome; Glycoprotein; Immunity; Innate immunity;
KW   Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..597
FT                   /note="Protein unc-93 homolog B1"
FT                   /id="PRO_0000190040"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         436
FT                   /note="Y -> C (in dbSNP:rs3175471)"
FT                   /id="VAR_059850"
FT   CONFLICT        514
FT                   /note="M -> I (in Ref. 1; CAC19791)"
FT                   /evidence="ECO:0000305"
FT   HELIX           47..88
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           92..97
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           104..116
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           137..151
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           158..198
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           214..234
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           237..241
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   TURN            242..245
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           250..253
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   STRAND          276..278
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           282..305
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           313..320
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           324..327
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           330..333
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           334..336
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           340..358
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   TURN            359..365
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           375..395
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           404..421
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           433..460
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           464..487
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:7C76"
FT   HELIX           495..517
FT                   /evidence="ECO:0007829|PDB:7C76"
SQ   SEQUENCE   597 AA;  66631 MW;  8CAAB41678095157 CRC64;
     MEAEPPLYPM AGAAGPQGDE DLLGVPDGPE APLDELVGAY PNYNEEEEER RYYRRKRLGV
     LKNVLAASAG GMLTYGVYLG LLQMQLILHY DETYREVKYG NMGLPDIDSK MLMGINVTPI
     AALLYTPVLI RFFGTKWMMF LAVGIYALFV STNYWERYYT LVPSAVALGM AIVPLWASMG
     NYITRMAQKY HEYSHYKEQD GQGMKQRPPR GSHAPYLLVF QAIFYSFFHL SFACAQLPMI
     YFLNHYLYDL NHTLYNVQSC GTNSHGILSG FNKTVLRTLP RSGNLIVVES VLMAVAFLAM
     LLVLGLCGAA YRPTEEIDLR SVGWGNIFQL PFKHVRDYRL RHLVPFFIYS GFEVLFACTG
     IALGYGVCSV GLERLAYLLV AYSLGASAAS LLGLLGLWLP RPVPLVAGAG VHLLLTFILF
     FWAPVPRVLQ HSWILYVAAA LWGVGSALNK TGLSTLLGIL YEDKERQDFI FTIYHWWQAV
     AIFTVYLGSS LHMKAKLAVL LVTLVAAAVS YLRMEQKLRR GVAPRQPRIP RPQHKVRGYR
     YLEEDNSDES DAEGEHGDGA EEEAPPAGPR PGPEPAGLGR RPCPYEQAQG GDGPEEQ
//