MY18A_HUMAN
ID MY18A_HUMAN Reviewed; 2054 AA.
AC Q92614; Q5H9U3; Q5QD01; Q5W9F9; Q5W9G1; Q8IXP8;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Unconventional myosin-XVIIIa {ECO:0000305};
DE AltName: Full=Molecule associated with JAK3 N-terminus;
DE Short=MAJN;
DE AltName: Full=Myosin containing a PDZ domain;
DE AltName: Full=Surfactant protein receptor SP-R210 {ECO:0000303|PubMed:16087679};
DE Short=SP-R210 {ECO:0000303|PubMed:16087679};
GN Name=MYO18A {ECO:0000312|HGNC:HGNC:31104};
GN Synonyms=CD245 {ECO:0000303|PubMed:27467939}, KIAA0216, MYSPDZ, TIAF1;
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 5), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 9-2054 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist in the
RT human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND VARIANT VAL-958.
RX PubMed=16087679; DOI=10.1074/jbc.m505229200;
RA Yang C.H., Szeliga J., Jordan J., Faske S., Sever-Chroneos Z., Dorsett B.,
RA Christian R.E., Settlage R.E., Shabanowitz J., Hunt D.F., Whitsett J.A.,
RA Chroneos Z.C.;
RT "Identification of the surfactant protein A receptor 210 as the
RT unconventional myosin 18A.";
RL J. Biol. Chem. 280:34447-34457(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-958.
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT VAL-958.
RC TISSUE=Testis;
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 [6]
RP INTERACTION WITH JAK3.
RX PubMed=10733938; DOI=10.1006/bbrc.2000.2413;
RA Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.;
RT "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2
RT deprival.";
RL Biochem. Biophys. Res. Commun. 270:267-271(2000).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RX PubMed=12761286; DOI=10.1093/jb/mvg053;
RA Mori K., Furusawa T., Okubo T., Inoue T., Ikawa S., Yanai N., Mori K.J.,
RA Obinata M.;
RT "Genome structure and differential expression of two isoforms of a novel
RT PDZ-containing myosin (MysPDZ) (Myo18A).";
RL J. Biochem. 133:405-413(2003).
RN [8]
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, INTERACTION WITH ACTIN, AND
RP MUTAGENESIS OF 114-ARG-GLY-115 AND 117-VAL-LEU-118.
RX PubMed=15835906; DOI=10.1021/bi0475931;
RA Isogawa Y., Kon T., Inoue T., Ohkura R., Yamakawa H., Ohara O., Sutoh K.;
RT "The N-terminal domain of MYO18A has an ATP-insensitive actin-binding
RT site.";
RL Biochemistry 44:6190-6196(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1970 AND SER-1974, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH LURAP1
RP AND CDC42BPA/CDC42BPB.
RX PubMed=18854160; DOI=10.1016/j.cell.2008.09.018;
RA Tan I., Yong J., Dong J.M., Lim L., Leung T.;
RT "A tripartite complex containing MRCK modulates lamellar actomyosin
RT retrograde flow.";
RL Cell 135:123-136(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2020, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1070; SER-1998; SER-2002;
RP SER-2020; SER-2041; SER-2043 AND THR-2045, AND IDENTIFICATION BY MASS
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1970 AND SER-1974, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [15]
RP FUNCTION IN GOLGI MEMBRANE BUDDING, INTERACTION WITH GOLPH3, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19837035; DOI=10.1016/j.cell.2009.07.052;
RA Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.K., Kerr M.L.,
RA Peterman M.C., Sim R., Wiharto P.A., Galbraith K.A., Madhavarapu S.,
RA Fuchs G.J., Meerloo T., Farquhar M.G., Zhou H., Field S.J.;
RT "GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch
RT and shape the Golgi to promote budding.";
RL Cell 139:337-351(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2041 AND SER-2043, AND
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-140; SER-2041 AND
RP SER-2043, AND IDENTIFICATION BY 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 [18]
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 [19]
RP FUNCTION.
RX PubMed=21123169; DOI=10.1074/jbc.m110.125567;
RA Sever-Chroneos Z., Krupa A., Davis J., Hasan M., Yang C.H., Szeliga J.,
RA Herrmann M., Hussain M., Geisbrecht B.V., Kobzik L., Chroneos Z.C.;
RT "Surfactant protein A (SP-A)-mediated clearance of Staphylococcus aureus
RT involves binding of SP-A to the staphylococcal adhesin eap and the
RT macrophage receptors SP-A receptor 210 and scavenger receptor class A.";
RL J. Biol. Chem. 286:4854-4870(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-1970; SER-2007;
RP SER-2041 AND SER-2043, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP INTERACTION WITH GOLPH3, F-ACTIN-BINDING, NUCLEOTIDE-BINDING, AND DOMAIN.
RX PubMed=23990465; DOI=10.1074/jbc.m113.497180;
RA Taft M.H., Behrmann E., Munske-Weidemann L.C., Thiel C., Raunser S.,
RA Manstein D.J.;
RT "Functional Characterization of Human Myosin-18A and its Interaction with
RT F-actin and GOLPH3.";
RL J. Biol. Chem. 288:30029-30041(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-52; SER-72; SER-74;
RP SER-83; SER-145; SER-164; SER-234; SER-1640; SER-1843; SER-1970; SER-2007;
RP SER-2020; SER-2041 AND SER-2043, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [23]
RP FUNCTION, AND INTERACTION WITH GOLPH3.
RX PubMed=23345592; DOI=10.1091/mbc.e12-07-0525;
RA Ng M.M., Dippold H.C., Buschman M.D., Noakes C.J., Field S.J.;
RT "GOLPH3L antagonizes GOLPH3 to determine Golgi morphology.";
RL Mol. Biol. Cell 24:796-808(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79; SER-98; THR-99; SER-103;
RP SER-140; SER-234; SER-1067; SER-1068; SER-1640; SER-1942; SER-1970;
RP SER-1974; SER-1998; SER-2002; SER-2006; SER-2014; SER-2020; TYR-2035;
RP SER-2041 AND SER-2043, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1922
RP (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1959 (ISOFORM
RP 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1501 (ISOFORM 5), 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 [25]
RP FUNCTION, AND INTERACTION WITH MSR1; CD14 AND CD11B.
RX PubMed=25965346; DOI=10.1371/journal.pone.0126576;
RA Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
RA Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
RA Christensen N.D., Chroneos Z.C.;
RT "SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
RT and activation.";
RL PLoS ONE 10:E0126576-E0126576(2015).
RN [26]
RP FUNCTION.
RX PubMed=27467939; DOI=10.1080/2162402x.2015.1127493;
RA De Masson A., Giustiniani J., Marie-Cardine A., Bouaziz J.D., Dulphy N.,
RA Gossot D., Validire P., Tazi A., Garbar C., Bagot M., Merrouche Y.,
RA Bensussan A.;
RT "Identification of CD245 as myosin 18A, a receptor for surfactant A: A
RT novel pathway for activating human NK lymphocytes.";
RL OncoImmunology 5:E1127493-E1127493(2016).
CC -!- FUNCTION: May link Golgi membranes to the cytoskeleton and participate
CC in the tensile force required for vesicle budding from the Golgi.
CC Thereby, may play a role in Golgi membrane trafficking and could
CC indirectly give its flattened shape to the Golgi apparatus
CC (PubMed:19837035, PubMed:23345592). Alternatively, in concert with
CC LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar
CC actomyosin retrograde flow that is crucial to cell protrusion and
CC migration (PubMed:18854160). May be involved in the maintenance of the
CC stromal cell architectures required for cell to cell contact (By
CC similarity). Regulates trafficking, expression, and activation of
CC innate immune receptors on macrophages. Plays a role to suppress
CC inflammatory responsiveness of macrophages via a mechanism that
CC modulates CD14 trafficking (PubMed:25965346). Acts as a receptor of
CC surfactant-associated protein A (SFTPA1/SP-A) and plays an important
CC role in internalization and clearance of SFTPA1-opsonized S.aureus by
CC alveolar macrophages (PubMed:16087679, PubMed:21123169). Strongly
CC enhances natural killer cell cytotoxicity (PubMed:27467939).
CC {ECO:0000250|UniProtKB:Q9JMH9, ECO:0000269|PubMed:16087679,
CC ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:19837035,
CC ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:23345592,
CC ECO:0000269|PubMed:25965346, ECO:0000269|PubMed:27467939}.
CC -!- SUBUNIT: Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB
CC and LURAP1 with the latter acting as an adapter connecting
CC CDC42BPA/CDC42BPB and MYO18A. Binds F-actin; regulated by ADP and
CC GOLPH3. Interacts with GOLPH3; the interaction is direct and may link
CC Golgi membranes to the actin cytoskeleton. Interacts with JAK3.
CC Interacts with MSR1 and CD14 (PubMed:25965346). Isoform 5 interacts
CC with CD11B (PubMed:25965346). {ECO:0000269|PubMed:10733938,
CC ECO:0000269|PubMed:15835906, ECO:0000269|PubMed:18854160,
CC ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:23345592,
CC ECO:0000269|PubMed:23990465, ECO:0000269|PubMed:25965346}.
CC -!- INTERACTION:
CC Q92614; Q9H4A6: GOLPH3; NbExp=6; IntAct=EBI-949059, EBI-2465479;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19837035}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19837035}.
CC Golgi outpost {ECO:0000250|UniProtKB:D3ZFD0}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:D3ZFD0}.
CC Note=Recruited to the Golgi apparatus by GOLPH3 (PubMed:19837035).
CC Localizes to the postsynaptic Golgi apparatus region, also named Golgi
CC outpost, which shapes dendrite morphology by functioning as sites of
CC acentrosomal microtubule nucleation (By similarity).
CC {ECO:0000250|UniProtKB:D3ZFD0, ECO:0000269|PubMed:19837035}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:Q9JMH9}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q9JMH9}. Note=Colocalizes with
CC actin. {ECO:0000250|UniProtKB:Q9JMH9}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:12761286}. Note=Lacks the PDZ domain
CC (PubMed:12761286). Diffusely localized in the cytoplasm
CC (PubMed:12761286). {ECO:0000269|PubMed:12761286}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell surface
CC {ECO:0000269|PubMed:16087679}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Alpha, SP-R210L {ECO:0000303|PubMed:16087679};
CC IsoId=Q92614-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q92614-2; Sequence=VSP_007869, VSP_007870;
CC Name=3;
CC IsoId=Q92614-3; Sequence=VSP_007871, VSP_007872;
CC Name=4;
CC IsoId=Q92614-4; Sequence=VSP_007872;
CC Name=5; Synonyms=SP-R210S {ECO:0000303|PubMed:16087679};
CC IsoId=Q92614-5; Sequence=VSP_023058, VSP_007872;
CC Name=TIAF1;
CC IsoId=O95411-1; Sequence=External;
CC -!- DOMAIN: The myosin motor domain binds ADP and ATP but has no intrinsic
CC ATPase activity. Mediates ADP-dependent binding to actin
CC (PubMed:23990465). {ECO:0000269|PubMed:23990465}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: The TIAF1 protein is coded in the 3'-UTR region of MYO18A.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13206.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD66838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB177858; BAD66836.1; -; mRNA.
DR EMBL; AB177860; BAD66838.1; ALT_INIT; mRNA.
DR EMBL; AY703984; AAV80770.1; -; mRNA.
DR EMBL; D86970; BAA13206.2; ALT_INIT; mRNA.
DR EMBL; CR933614; CAI45931.1; -; mRNA.
DR EMBL; BC039612; AAH39612.1; -; mRNA.
DR CCDS; CCDS45641.1; -. [Q92614-4]
DR CCDS; CCDS45642.1; -. [Q92614-1]
DR CCDS; CCDS86587.1; -. [Q92614-3]
DR RefSeq; NP_001333696.1; NM_001346767.1. [Q92614-3]
DR RefSeq; NP_001333697.1; NM_001346768.1. [Q92614-5]
DR RefSeq; NP_510880.2; NM_078471.3. [Q92614-1]
DR RefSeq; NP_976063.1; NM_203318.1. [Q92614-4]
DR AlphaFoldDB; Q92614; -.
DR SMR; Q92614; -.
DR BioGRID; 134384; 315.
DR DIP; DIP-46631N; -.
DR IntAct; Q92614; 191.
DR MINT; Q92614; -.
DR STRING; 9606.ENSP00000437073; -.
DR CarbonylDB; Q92614; -.
DR iPTMnet; Q92614; -.
DR MetOSite; Q92614; -.
DR PhosphoSitePlus; Q92614; -.
DR SwissPalm; Q92614; -.
DR BioMuta; MYO18A; -.
DR DMDM; 33301318; -.
DR EPD; Q92614; -.
DR jPOST; Q92614; -.
DR MassIVE; Q92614; -.
DR MaxQB; Q92614; -.
DR PaxDb; Q92614; -.
DR PeptideAtlas; Q92614; -.
DR PRIDE; Q92614; -.
DR ProteomicsDB; 75358; -. [Q92614-1]
DR ProteomicsDB; 75359; -. [Q92614-2]
DR ProteomicsDB; 75360; -. [Q92614-3]
DR ProteomicsDB; 75361; -. [Q92614-4]
DR ProteomicsDB; 75362; -. [Q92614-5]
DR ABCD; Q92614; 1 sequenced antibody.
DR Antibodypedia; 7183; 83 antibodies from 23 providers.
DR DNASU; 399687; -.
DR Ensembl; ENST00000527372.7; ENSP00000437073.1; ENSG00000196535.18. [Q92614-1]
DR Ensembl; ENST00000531253.5; ENSP00000434228.1; ENSG00000196535.18. [Q92614-4]
DR Ensembl; ENST00000533112.5; ENSP00000435932.1; ENSG00000196535.18. [Q92614-3]
DR GeneID; 399687; -.
DR KEGG; hsa:399687; -.
DR MANE-Select; ENST00000527372.7; ENSP00000437073.1; NM_078471.4; NP_510880.2.
DR UCSC; uc002hdt.2; human. [Q92614-1]
DR CTD; 399687; -.
DR DisGeNET; 399687; -.
DR GeneCards; MYO18A; -.
DR HGNC; HGNC:31104; MYO18A.
DR HPA; ENSG00000196535; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 609517; gene.
DR MIM; 610067; gene.
DR neXtProt; NX_Q92614; -.
DR OpenTargets; ENSG00000196535; -.
DR PharmGKB; PA134978348; -.
DR VEuPathDB; HostDB:ENSG00000196535; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155768; -.
DR HOGENOM; CLU_000192_1_0_1; -.
DR InParanoid; Q92614; -.
DR OMA; WLGHAKN; -.
DR PhylomeDB; Q92614; -.
DR TreeFam; TF339614; -.
DR PathwayCommons; Q92614; -.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR SignaLink; Q92614; -.
DR BioGRID-ORCS; 399687; 31 hits in 1077 CRISPR screens.
DR ChiTaRS; MYO18A; human.
DR GeneWiki; MYO18A; -.
DR GenomeRNAi; 399687; -.
DR Pharos; Q92614; Tbio.
DR PRO; PR:Q92614; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92614; protein.
DR Bgee; ENSG00000196535; Expressed in gastrocnemius and 93 other tissues.
DR ExpressionAtlas; Q92614; baseline and differential.
DR Genevisible; Q92614; HS.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; IMP:CACAO.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:CACAO.
DR GO; GO:0048194; P:Golgi vesicle budding; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:1903028; P:positive regulation of opsonization; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
DR CDD; cd01386; MYSc_Myo18; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR031244; MYO18A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45615:SF13; PTHR45615:SF13; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2054
FT /note="Unconventional myosin-XVIIIa"
FT /id="PRO_0000123476"
FT DOMAIN 220..311
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 349..401
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 405..1185
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1188..1217
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..398
FT /note="Mediates nucleotide-independent binding to F-actin
FT and interaction with GOLPH3"
FT /evidence="ECO:0000269|PubMed:23990465"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1246..1971
FT /evidence="ECO:0000255"
FT MOTIF 114..118
FT /note="Interaction with actin"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1962..1985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2016..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1942
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569"
FT MOD_RES 1998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2006
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2035
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH9"
FT MOD_RES 2041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2045
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..458
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15491607"
FT /id="VSP_023058"
FT VAR_SEQ 1..331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007869"
FT VAR_SEQ 332..333
FT /note="SD -> MR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007870"
FT VAR_SEQ 1571..1607
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007871"
FT VAR_SEQ 1952..1966
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607, ECO:0000303|PubMed:17974005"
FT /id="VSP_007872"
FT VARIANT 958
FT /note="A -> V (in dbSNP:rs8076604)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16087679, ECO:0000269|PubMed:9039502"
FT /id="VAR_030585"
FT MUTAGEN 114..115
FT /note="RG->AA: No effect on interaction with actin."
FT /evidence="ECO:0000269|PubMed:15835906"
FT MUTAGEN 117..118
FT /note="VL->AA: Abolishes interaction with actin."
FT /evidence="ECO:0000269|PubMed:15835906"
FT CONFLICT 1014
FT /note="A -> V (in Ref. 1; BAD66838 and 2; AAV80770)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="S -> P (in Ref. 4; CAI45931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1757
FT /note="E -> K (in Ref. 4; CAI45931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1889
FT /note="E -> G (in Ref. 4; CAI45931)"
FT /evidence="ECO:0000305"
FT MOD_RES Q92614-3:1922
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q92614-4:1959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q92614-5:1501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 2054 AA; 233115 MW; 52BFA0AA273E18F7 CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSV ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHP
GPGIPRPGHR SRAPELVTKK FPVDLRLPPV VPLPPPTLRE LELQRRPTGD FGFSLRRTTM
LDRGPEGQAC RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVESKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDAKTEEQI AAEEAWNETE KVWLVHRDGF
SLASQLKSEE LNLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLEDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLGPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIILLGSS GSGKTTSCQH LVQYLATIAG ISGNKVFSVE KWQALYTLLE
AFGNSPTIIN GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY
LLACGDGTLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQAAMK VLGISPDEQK
ACWFILAAIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQHKG
GTLQRSTSFR QGPEESGLGD GTGPKLSALE CLEGMAAGLY SELFTLLVSL VNRALKSSQH
SLCSMMIVDT PGFQNPEQGG SARGASFEEL CHNYTQDRLQ RLFHERTFVQ ELERYKEENI
ELAFDDLEPP TDDSVAAVDQ ASHQSLVRSL ARTDEARGLL WLLEEEALVP GASEDTLLER
LFSYYGPQEG DKKGQSPLLH SSKPHHFLLG HSHGTNWVEY NVTGWLNYTK QNPATQNAPR
LLQDSQKKII SNLFLGRAGS ATVLSGSIAG LEGGSQLALR RATSMRKTFT TGMAAVKKKS
LCIQMKLQVD ALIDTIKKSK LHFVHCFLPV AEGWAGEPRS ASSRRVSSSS ELDLPSGDHC
EAGLLQLDVP LLRTQLRGSR LLDAMRMYRQ GYPDHMVFSE FRRRFDVLAP HLTKKHGRNY
IVVDERRAVE ELLECLDLEK SSCCMGLSRV FFRAGTLARL EEQRDEQTSR NLTLFQAACR
GYLARQHFKK RKIQDLAIRC VQKNIKKNKG VKDWPWWKLF TTVRPLIEVQ LSEEQIRNKD
EEIQQLRSKL EKAEKERNEL RLNSDRLESR ISELTSELTD ERNTGESASQ LLDAETAERL
RAEKEMKELQ TQYDALKKQM EVMEMEVMEA RLIRAAEING EVDDDDAGGE WRLKYERAVR
EVDFTKKRLQ QEFEDKLEVE QQNKRQLERR LGDLQADSEE SQRALQQLKK KCQRLTAELQ
DTKLHLEGQQ VRNHELEKKQ RRFDSELSQA HEEAQREKLQ REKLQREKDM LLAEAFSLKQ
QLEEKDMDIA GFTQKVVSLE AELQDISSQE SKDEASLAKV KKQLRDLEAK VKDQEEELDE
QAGTIQMLEQ AKLRLEMEME RMRQTHSKEM ESRDEEVEEA RQSCQKKLKQ MEVQLEEEYE
DKQKVLREKR ELEGKLATLS DQVNRRDFES EKRLRKDLKR TKALLADAQL MLDHLKNSAP
SKREIAQLKN QLEESEFTCA AAVKARKAME VEIEDLHLQI DDIAKAKTAL EEQLSRLQRE
KNEIQNRLEE DQEDMNELMK KHKAAVAQAS RDLAQINDLQ AQLEEANKEK QELQEKLQAL
QSQVEFLEQS MVDKSLVSRQ EAKIRELETR LEFERTQVKR LESLASRLKE NMEKLTEERD
QRIAAENREK EQNKRLQRQL RDTKEEMGEL ARKEAEASRK KHELEMDLES LEAANQSLQA
DLKLAFKRIG DLQAAIEDEM ESDENEDLIN SLQDMVTKYQ KRKNKLEGDS DVDSELEDRV
DGVKSWLSKN KGPSKAASDD GSLKSSSPTS YWKSLAPDRS DDEHDPLDNT SRPRYSHSYL
SDSDTEAKLT ETNA
