MYO1E_HUMAN
ID MYO1E_HUMAN Reviewed; 1108 AA.
AC Q12965; Q14778;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Unconventional myosin-Ie;
DE AltName: Full=Myosin-Ic;
DE AltName: Full=Unconventional myosin 1E;
GN Name=MYO1E; Synonyms=MYO1C;
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].
RX PubMed=7932763; DOI=10.1006/jmbi.1994.1662;
RA Bement W.M., Wirth J.A., Mooseker M.S.;
RT "Cloning and mRNA expression of human unconventional myosin-IC. A homologue
RT of amoeboid myosins-I with a single IQ motif and an SH3 domain.";
RL J. Mol. Biol. 243:356-363(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-196.
RX PubMed=8022818; DOI=10.1073/pnas.91.14.6549;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RT "Identification and overlapping expression of multiple unconventional
RT myosin genes in vertebrate cell types.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994).
RN [4]
RP ERRATUM OF PUBMED:8022818.
RX PubMed=7972138; DOI=10.1073/pnas.91.24.11767-c;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994).
RN [5]
RP FUNCTION IN ATP HYDROLYSIS, AND INTERACTION WITH F-ACTIN AND CALM.
RX PubMed=11940582; DOI=10.1074/jbc.m200713200;
RA El Mezgueldi M., Tang N., Rosenfeld S.S., Ostap E.M.;
RT "The kinetic mechanism of Myo1e (human myosin-IC).";
RL J. Biol. Chem. 277:21514-21521(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SYNJ1; DNM1 AND DNM2.
RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
RA Krendel M., Osterweil E.K., Mooseker M.S.;
RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in
RT endocytosis.";
RL FEBS Lett. 581:644-650(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980 AND SER-1002, 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 [8]
RP INTERACTION WITH CARMIL1.
RX PubMed=19846667; DOI=10.1091/mbc.e08-10-1071;
RA Liang Y., Niederstrasser H., Edwards M., Jackson C.E., Cooper J.A.;
RT "Distinct roles for CARMIL isoforms in cell migration.";
RL Mol. Biol. Cell 20:5290-5305(2009).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20860408; DOI=10.1021/bi1012657;
RA Feeser E.A., Ignacio C.M., Krendel M., Ostap E.M.;
RT "Myo1e binds anionic phospholipids with high affinity.";
RL Biochemistry 49:9353-9360(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, 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 [11]
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 [12]
RP INTERACTION WITH ARL14EP, AND TISSUE SPECIFICITY.
RX PubMed=21458045; DOI=10.1016/j.cell.2011.03.023;
RA Paul P., van den Hoorn T., Jongsma M.L., Bakker M.J., Hengeveld R.,
RA Janssen L., Cresswell P., Egan D.A., van Ham M., Ten Brinke A., Ovaa H.,
RA Beijersbergen R.L., Kuijl C., Neefjes J.;
RT "A Genome-wide multidimensional RNAi screen reveals pathways controlling
RT MHC class II antigen presentation.";
RL Cell 145:268-283(2011).
RN [13]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT FSGS6 PRO-159, VARIANTS
RP GLY-185; VAL-221; ARG-795 AND HIS-1049, AND CHARACTERIZATION OF VARIANT
RP FSGS6 PRO-159.
RX PubMed=21756023; DOI=10.1056/nejmoa1101273;
RA Mele C., Iatropoulos P., Donadelli R., Calabria A., Maranta R., Cassis P.,
RA Buelli S., Tomasoni S., Piras R., Krendel M., Bettoni S., Morigi M.,
RA Delledonne M., Pecoraro C., Abbate I., Capobianchi M.R., Hildebrandt F.,
RA Otto E., Schaefer F., Macciardi F., Ozaltin F., Emre S., Ibsirlioglu T.,
RA Benigni A., Remuzzi G., Noris M.;
RT "MYO1E mutations and childhood familial focal segmental
RT glomerulosclerosis.";
RL N. Engl. J. Med. 365:295-306(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [15]
RP VARIANT FSGS6 PRO-159.
RX PubMed=21697813; DOI=10.1038/ki.2011.148;
RA Sanna-Cherchi S., Burgess K.E., Nees S.N., Caridi G., Weng P.L.,
RA Dagnino M., Bodria M., Carrea A., Allegretta M.A., Kim H.R., Perry B.J.,
RA Gigante M., Clark L.N., Kisselev S., Cusi D., Gesualdo L., Allegri L.,
RA Scolari F., D'Agati V., Shapiro L.S., Pecoraro C., Palomero T.,
RA Ghiggeri G.M., Gharavi A.G.;
RT "Exome sequencing identified MYO1E and NEIL1 as candidate genes for human
RT autosomal recessive steroid-resistant nephrotic syndrome.";
RL Kidney Int. 80:389-396(2011).
RN [16]
RP VARIANT MET-469.
RX PubMed=28837161; DOI=10.1038/gim.2017.113;
RA Ansar M., Riazuddin S., Sarwar M.T., Makrythanasis P., Paracha S.A.,
RA Iqbal Z., Khan J., Assir M.Z., Hussain M., Razzaq A., Polla D.L., Taj A.S.,
RA Holmgren A., Batool N., Misceo D., Iwaszkiewicz J., de Brouwer A.P.M.,
RA Guipponi M., Hanquinet S., Zoete V., Santoni F.A., Frengen E., Ahmed J.,
RA Riazuddin S., van Bokhoven H., Antonarakis S.E.;
RT "Biallelic variants in LINGO1 are associated with autosomal recessive
RT intellectual disability, microcephaly, speech and motor delay.";
RL Genet. Med. 20:778-784(2018).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails bind to membranous compartments, which are then moved
CC relative to actin filaments. Binds to membranes containing anionic
CC phospholipids via its tail domain. Required for normal morphology of
CC the glomerular basement membrane, normal development of foot processes
CC by kidney podocytes and normal kidney function. In dendritic cells, may
CC control the movement of class II-containing cytoplasmic vesicles along
CC the actin cytoskeleton by connecting them with the actin network via
CC ARL14EP and ARL14. {ECO:0000269|PubMed:11940582,
CC ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:20860408}.
CC -!- SUBUNIT: Interacts with CALM and F-actin (PubMed:11940582). Interacts
CC (via SH3 domain) with SYNJ1, DNM1 and DNM2 (PubMed:17257598). Interacts
CC with ARL14EP (PubMed:21458045). Interacts with CARMIL1
CC (PubMed:19846667). {ECO:0000269|PubMed:11940582,
CC ECO:0000269|PubMed:17257598, ECO:0000269|PubMed:19846667,
CC ECO:0000269|PubMed:21458045}.
CC -!- INTERACTION:
CC Q12965; Q8N8R7: ARL14EP; NbExp=2; IntAct=EBI-4279548, EBI-2807994;
CC Q12965; P50570: DNM2; NbExp=2; IntAct=EBI-4279548, EBI-346547;
CC Q12965; P21575: Dnm1; Xeno; NbExp=2; IntAct=EBI-4279548, EBI-80070;
CC Q12965; Q62910: Synj1; Xeno; NbExp=2; IntAct=EBI-4279548, EBI-1149123;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic
CC vesicle. Cytoplasmic vesicle, clathrin-coated vesicle. Cell junction
CC {ECO:0000250}. Note=Colocalizes with F-actin (By similarity). In
CC cultured podocytes, it localizes close to and is associated with the
CC cytoplasmic membrane, with enrichment at the lamellipodia tips.
CC Colocalizes with cytoplasmic vesicles, including endocytic clathrin-
CC coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the immune system. In the kidney,
CC predominantly expressed in the glomerulus, including podocytes.
CC {ECO:0000269|PubMed:21458045, ECO:0000269|PubMed:21756023}.
CC -!- DISEASE: Focal segmental glomerulosclerosis 6 (FSGS6) [MIM:614131]: A
CC renal pathology defined by the presence of segmental sclerosis in
CC glomeruli and resulting in proteinuria, reduced glomerular filtration
CC rate and progressive decline in renal function. Renal insufficiency
CC often progresses to end-stage renal disease, a highly morbid state
CC requiring either dialysis therapy or kidney transplantation. FSGS6 is a
CC childhood-onset disorder resulting in nephrotic syndrome, which
CC includes massive proteinuria, hypoalbuminemia, hyperlipidemia, and
CC edema. {ECO:0000269|PubMed:21697813, ECO:0000269|PubMed:21756023}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; U14391; AAA62667.1; -; mRNA.
DR EMBL; AC092756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L29139; AAA20902.1; -; mRNA.
DR CCDS; CCDS32254.1; -.
DR PIR; S53601; S53601.
DR RefSeq; NP_004989.2; NM_004998.3.
DR AlphaFoldDB; Q12965; -.
DR SMR; Q12965; -.
DR BioGRID; 110727; 133.
DR CORUM; Q12965; -.
DR DIP; DIP-884N; -.
DR IntAct; Q12965; 47.
DR MINT; Q12965; -.
DR STRING; 9606.ENSP00000288235; -.
DR DrugBank; DB03366; Imidazole.
DR GlyGen; Q12965; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q12965; -.
DR PhosphoSitePlus; Q12965; -.
DR BioMuta; MYO1E; -.
DR DMDM; 215274106; -.
DR EPD; Q12965; -.
DR jPOST; Q12965; -.
DR MassIVE; Q12965; -.
DR PaxDb; Q12965; -.
DR PeptideAtlas; Q12965; -.
DR PRIDE; Q12965; -.
DR ProteomicsDB; 59057; -.
DR Antibodypedia; 12911; 165 antibodies from 26 providers.
DR DNASU; 4643; -.
DR Ensembl; ENST00000288235.9; ENSP00000288235.4; ENSG00000157483.9.
DR GeneID; 4643; -.
DR KEGG; hsa:4643; -.
DR MANE-Select; ENST00000288235.9; ENSP00000288235.4; NM_004998.4; NP_004989.2.
DR CTD; 4643; -.
DR DisGeNET; 4643; -.
DR GeneCards; MYO1E; -.
DR HGNC; HGNC:7599; MYO1E.
DR HPA; ENSG00000157483; Low tissue specificity.
DR MalaCards; MYO1E; -.
DR MIM; 601479; gene.
DR MIM; 614131; phenotype.
DR neXtProt; NX_Q12965; -.
DR OpenTargets; ENSG00000157483; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA31401; -.
DR VEuPathDB; HostDB:ENSG00000157483; -.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000157461; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q12965; -.
DR OMA; IKGAFRY; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q12965; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; Q12965; -.
DR SignaLink; Q12965; -.
DR SIGNOR; Q12965; -.
DR BioGRID-ORCS; 4643; 39 hits in 1072 CRISPR screens.
DR ChiTaRS; MYO1E; human.
DR GeneWiki; MYO1E; -.
DR GenomeRNAi; 4643; -.
DR Pharos; Q12965; Tbio.
DR PRO; PR:Q12965; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q12965; protein.
DR Bgee; ENSG00000157483; Expressed in calcaneal tendon and 146 other tissues.
DR ExpressionAtlas; Q12965; baseline and differential.
DR Genevisible; Q12965; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035507; Ie/If_SH3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Cell junction; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Disease variant; Lipid-binding;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..1108
FT /note="Unconventional myosin-Ie"
FT /id="PRO_0000123450"
FT DOMAIN 19..692
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 695..724
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 730..922
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1051..1108
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 581..591
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 919..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 159
FT /note="A -> P (in FSGS6; the mutant shows diffuse cytosolic
FT localization with a punctate pattern; dbSNP:rs387906807)"
FT /evidence="ECO:0000269|PubMed:21697813,
FT ECO:0000269|PubMed:21756023"
FT /id="VAR_065958"
FT VARIANT 185
FT /note="D -> G (in dbSNP:rs141565214)"
FT /evidence="ECO:0000269|PubMed:21756023"
FT /id="VAR_065959"
FT VARIANT 221
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:21756023"
FT /id="VAR_065960"
FT VARIANT 469
FT /note="T -> M (in dbSNP:rs1173043275)"
FT /evidence="ECO:0000269|PubMed:28837161"
FT /id="VAR_081166"
FT VARIANT 795
FT /note="G -> R (in dbSNP:rs180951130)"
FT /evidence="ECO:0000269|PubMed:21756023"
FT /id="VAR_065961"
FT VARIANT 1049
FT /note="P -> H (in dbSNP:rs147579391)"
FT /evidence="ECO:0000269|PubMed:21756023"
FT /id="VAR_065962"
FT CONFLICT 889..892
FT /note="WSAG -> GVQGA (in Ref. 1; AAA62667)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="N -> I (in Ref. 1; AAA62667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="Q -> P (in Ref. 1; AAA62667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1108 AA; 127062 MW; 3073050B9BB4DDC6 CRC64;
MGSKGVYQYH WQSHNVKHSG VDDMVLLSKI TENSIVENLK KRYMDDYIFT YIGSVLISVN
PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADNMYRNMI IDRENQCVII SGESGAGKTV
AAKYIMSYIS RVSGGGTKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS AEQKHSLGIT SMDYYYYLSL
SGSYKVDDID DRREFQETLH AMNVIGIFAE EQTLVLQIVA GILHLGNISF KEVGNYAAVE
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ENKVNPPGIM SILDDVCATM HAVGEGADQT
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPRDWEE
SRVKHQVEYL GLKENIRVRR AGYAYRRIFQ KFLQRYAILT KATWPSWQGE EKQGVLHLLQ
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKSWRKFV ARKKYVQMRE
EASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADTV TKYDRRFKGV
KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEIER ILSVSLSTMQ DDIFILHEQE
YDSLLESVFK TEFLSLLAKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFH
QGFGDLAVLK PSNKVLQVSI GPGLPKNSRP TRRNTTQNTG YSSGTQNANY PVRAAPPPPG
YHQNGVIRNQ YVPYPHAPGS QRSNQKSLYT SMARPPLPRQ QSTSSDRVSQ TPESLDFLKV
PDQGAAGVRR QTTSRPPPAG GRPKPQPKPK PQVPQCKALY AYDAQDTDEL SFNANDIIDI
IKEDPSGWWT GRLRGKQGLF PNNYVTKI
