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 27-MAR-2024, entry version 204. 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 VARIANTS FSGS6 47-TYR--ILE-1108 DEL AND ILE-119. RX PubMed=23595123; DOI=10.1038/jhg.2013.27; RA Al-Hamed M.H., Al-Sabban E., Al-Mojalli H., Al-Harbi N., Faqeih E., RA Al Shaya H., Alhasan K., Al-Hissi S., Rajab M., Edwards N., Al-Abbad A., RA Al-Hassoun I., Sayer J.A., Meyer B.F.; RT "A molecular genetic analysis of childhood nephrotic syndrome in a cohort RT of Saudi Arabian families."; RL J. Hum. Genet. 58:480-489(2013). RN [17] RP VARIANTS GLY-185; TRP-523 AND 660-GLN--ILE-1108 DEL, AND VARIANT FSGS6 RP HIS-388. RX PubMed=25349199; DOI=10.1681/asn.2014050489; RG SRNS Study Group; RA Sadowski C.E., Lovric S., Ashraf S., Pabst W.L., Gee H.Y., Kohl S., RA Engelmann S., Vega-Warner V., Fang H., Halbritter J., Somers M.J., Tan W., RA Shril S., Fessi I., Lifton R.P., Bockenhauer D., El-Desoky S., Kari J.A., RA Zenker M., Kemper M.J., Mueller D., Fathy H.M., Soliman N.A., RA Hildebrandt F.; RT "A single-gene cause in 29.5% of cases of steroid-resistant nephrotic RT syndrome."; RL J. Am. Soc. Nephrol. 26:1279-1289(2015). RN [18] 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). RN [19] RP CHARACTERIZATION OF VARIANTS FSGS6 ILE-119 AND HIS-388, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=36316095; DOI=10.1681/asn.2021111505; RA Liu P.J., Gunther L.K., Garone M.E., Zhang C., Perez D., Bi-Karchin J., RA Pellenz C.D., Chase S.E., Presti M.F., Plante E.L., Martin C.E., Lovric S., RA Yengo C.M., Hildebrandt F., Krendel M.; RT "Steroid-Resistant Nephrotic Syndrome-Associated MYO1E Mutations Have RT Differential Effects on Myosin 1e Localization, Dynamics, and Activity."; RL J. Am. Soc. Nephrol. 33:1989-2007(2022). CC -!- FUNCTION: Actin-based motor molecule with ATPase activity CC (PubMed:11940582, PubMed:36316095). Unconventional myosins serve in CC intracellular movements. Their highly divergent tails bind to CC membranous compartments, which are then moved relative to actin CC filaments. Binds to membranes containing anionic phospholipids via its CC tail domain. Involved in clathrin-mediated endocytosis and CC intracellular movement of clathrin-coated vesicles (PubMed:36316095). CC Required for normal morphology of the glomerular basement membrane, CC normal development of foot processes by kidney podocytes and normal CC kidney function. In dendritic cells, may control the movement of class CC II-containing cytoplasmic vesicles along the actin cytoskeleton by CC connecting them with the actin network via ARL14EP and ARL14. CC {ECO:0000269|PubMed:11940582, ECO:0000269|PubMed:17257598, CC ECO:0000269|PubMed:20860408, ECO:0000269|PubMed:36316095}. 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 {ECO:0000250|UniProtKB:E9Q634}. CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:E9Q634}. Cytoplasmic CC vesicle {ECO:0000250|UniProtKB:E9Q634}. Cytoplasmic vesicle, clathrin- CC coated vesicle {ECO:0000269|PubMed:36316095}. Cell junction CC {ECO:0000269|PubMed:36316095}. Note=Colocalizes with F-actin (By CC similarity). In cultured podocytes, it localizes close to and is CC associated with the cytoplasmic membrane, with enrichment at the CC lamellipodia tips. Colocalizes with cytoplasmic vesicles, including CC endocytic clathrin-coated vesicles. Colocalizes with dynamin at CC cytoplasmic vesicles. {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 ECO:0000269|PubMed:23595123, ECO:0000269|PubMed:25349199, CC ECO:0000269|PubMed:36316095}. Note=The disease is caused by variants CC affecting the gene represented 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}. 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; 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; 202. DR CORUM; Q12965; -. DR DIP; DIP-884N; -. DR IntAct; Q12965; 51. DR MINT; Q12965; -. DR STRING; 9606.ENSP00000288235; -. DR DrugBank; DB03366; Imidazole. DR GlyCosmos; Q12965; 1 site, 1 glycan. DR GlyGen; Q12965; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q12965; -. DR PhosphoSitePlus; Q12965; -. DR SwissPalm; Q12965; -. DR BioMuta; MYO1E; -. DR DMDM; 215274106; -. DR EPD; Q12965; -. DR jPOST; Q12965; -. DR MassIVE; Q12965; -. DR PaxDb; 9606-ENSP00000288235; -. DR PeptideAtlas; Q12965; -. DR PRIDE; Q12965; -. DR ProteomicsDB; 59057; -. DR Pumba; Q12965; -. DR Antibodypedia; 12911; 174 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 AGR; HGNC:7599; -. 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; RFEEKTH; -. DR OrthoDB; 1094820at2759; -. DR PhylomeDB; Q12965; -. DR TreeFam; TF312960; -. DR PathwayCommons; Q12965; -. DR SignaLink; Q12965; -. DR SIGNOR; Q12965; -. DR BioGRID-ORCS; 4643; 39 hits in 1150 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 148 other cell types or tissues. DR ExpressionAtlas; Q12965; baseline and differential. 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:0031982; C:vesicle; 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; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.4820; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR13140; MYOSIN; 1. DR PANTHER; PTHR13140:SF341; UNCONVENTIONAL MYOSIN-IE; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS51757; TH1; 1. DR Genevisible; Q12965; HS. 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 47..1108 FT /note="Missing (in FSGS6)" FT /evidence="ECO:0000269|PubMed:23595123" FT /id="VAR_087568" FT VARIANT 119 FT /note="T -> I (in FSGS6; results in altered clathrin-coated FT vesicle dynamics when expressed in a heterolgous system; FT severely decreased localization to cell-cell junctions and FT clathrin-coated vesicles)" FT /evidence="ECO:0000269|PubMed:23595123, FT ECO:0000269|PubMed:36316095" FT /id="VAR_087569" 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 ECO:0000269|PubMed:25349199" FT /id="VAR_065959" FT VARIANT 221 FT /note="A -> V" FT /evidence="ECO:0000269|PubMed:21756023" FT /id="VAR_065960" FT VARIANT 388 FT /note="D -> H (in FSGS6; loss of microfilament motor FT activity; results in altered clathrin-coated vesicle FT dynamics when expressed in a heterolgous system; no effect FT on localization to cell-cell junctions and clathrin-coated FT vesicles)" FT /evidence="ECO:0000269|PubMed:25349199, FT ECO:0000269|PubMed:36316095" FT /id="VAR_087570" FT VARIANT 469 FT /note="T -> M (in dbSNP:rs1173043275)" FT /evidence="ECO:0000269|PubMed:28837161" FT /id="VAR_081166" FT VARIANT 523 FT /note="R -> W (found in a patient with steroid-resistant FT nephrotic syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:25349199" FT /id="VAR_087571" FT VARIANT 660..1108 FT /note="Missing (found in a patient with steroid-resistant, FT minimal change nephrotic syndrome; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:25349199" FT /id="VAR_087572" 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 //