UN93B_HUMAN
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 03-AUG-2022, entry version 144.
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/";
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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 SMR; Q9H1C4; -.
DR BioGRID; 123557; 460.
DR IntAct; Q9H1C4; 360.
DR MINT; Q9H1C4; -.
DR STRING; 9606.ENSP00000227471; -.
DR TCDB; 2.A.1.58.7; the major facilitator superfamily (mfs).
DR GlyGen; Q9H1C4; 4 sites.
DR iPTMnet; Q9H1C4; -.
DR PhosphoSitePlus; Q9H1C4; -.
DR BioMuta; UNC93B1; -.
DR DMDM; 67462081; -.
DR EPD; Q9H1C4; -.
DR jPOST; Q9H1C4; -.
DR MassIVE; Q9H1C4; -.
DR MaxQB; Q9H1C4; -.
DR PaxDb; Q9H1C4; -.
DR PeptideAtlas; Q9H1C4; -.
DR PRIDE; Q9H1C4; -.
DR ProteomicsDB; 80398; -.
DR ABCD; Q9H1C4; 12 sequenced antibodies.
DR Antibodypedia; 30503; 123 antibodies from 24 providers.
DR DNASU; 81622; -.
DR Ensembl; ENST00000227471.7; ENSP00000227471.3; ENSG00000110057.8.
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 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; YCYWVME; -.
DR OrthoDB; 394901at2759; -.
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 267 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 103 other tissues.
DR ExpressionAtlas; Q9H1C4; baseline and differential.
DR Genevisible; Q9H1C4; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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: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 InterPro; IPR010291; Ion_channel_UNC-93.
DR InterPro; IPR043268; UNC93B1.
DR PANTHER; PTHR46744; PTHR46744; 1.
DR Pfam; PF05978; UNC-93; 1.
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
