MY18A_MOUSE
ID MY18A_MOUSE Reviewed; 2050 AA.
AC Q9JMH9; Q3TBB2; Q3UH48; Q3UV60; Q5QD54; Q5QD55; Q5QD56; Q5SYN8; Q5SYN9;
AC Q5SYP0; Q5SYP1; Q811D7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Unconventional myosin-XVIIIa;
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:25965346};
DE Short=SP-R210 {ECO:0000303|PubMed:25965346};
GN Name=Myo18a; Synonyms=Myspdz {ECO:0000303|PubMed:15582604};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=10733906; DOI=10.1006/bbrc.2000.2377;
RA Furusawa T., Ikawa S., Yanai N., Obinata M.;
RT "Isolation of a novel PDZ-containing myosin from hematopoietic supportive
RT bone marrow stromal cell lines.";
RL Biochem. Biophys. Res. Commun. 270:67-75(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-873 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1032-2050 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1933-2050 (ISOFORMS 1/4/5/7), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Alveolus;
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 [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), SUBCELLULAR LOCATION (ISOFORMS 1
RP AND 2), AND DIFFERENTIAL EXPRESSION.
RC TISSUE=Spleen;
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 PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14969583; DOI=10.1042/bj20031978;
RA Cross M., Csar X.F., Wilson N.J., Manes G., Addona T.A., Marks D.C.,
RA Whitty G.A., Ashman K., Hamilton J.A.;
RT "A novel 110 kDa form of myosin XVIIIA (MysPDZ) is tyrosine-phosphorylated
RT after colony-stimulating factor-1 receptor signalling.";
RL Biochem. J. 380:243-253(2004).
RN [9]
RP HOMODIMER, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN.
RX PubMed=15582604; DOI=10.1016/j.bbrc.2004.11.058;
RA Mori K., Matsuda K., Furusawa T., Kawata M., Inoue T., Obinata M.;
RT "Subcellular localization and dynamics of MysPDZ (Myo18A) in live mammalian
RT cells.";
RL Biochem. Biophys. Res. Commun. 326:491-498(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-164;
RP SER-1966; SER-2037 AND SER-2039, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2037 AND SER-2039, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [13]
RP FUNCTION IN GOLGI ORGANIZATION, AND MUTAGENESIS OF 503-GLY-LYS-504.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-102; SER-103;
RP SER-157; SER-160; SER-164; SER-983; SER-1966; SER-1994; SER-2016; SER-2032;
RP SER-2037; SER-2039 AND THR-2041, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
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 [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
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). Alternatively, in concert with LURAP1 and
CC CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin
CC retrograde flow that is crucial to cell protrusion and migration (By
CC similarity). May be involved in the maintenance of the stromal cell
CC architectures required for cell to cell contact (PubMed:10733906).
CC Regulates trafficking, expression, and activation of innate immune
CC receptors on macrophages. Plays a role to suppress inflammatory
CC responsiveness of macrophages via a mechanism that modulates CD14
CC trafficking (PubMed:25965346). Acts as a receptor of surfactant-
CC associated protein A (SFTPA1/SP-A) and plays an important role in
CC internalization and clearance of SFTPA1-opsonized S.aureus by alveolar
CC macrophages (PubMed:21123169). Strongly enhances natural killer cell
CC cytotoxicity (By similarity). {ECO:0000250|UniProtKB:Q92614,
CC ECO:0000269|PubMed:10733906, ECO:0000269|PubMed:19837035,
CC ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:25965346}.
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 (By similarity). Binds F-actin; regulated
CC by ADP and GOLPH3 (PubMed:15582604). Interacts with GOLPH3; the
CC interaction is direct and may link Golgi membranes to the actin
CC cytoskeleton (By similarity). Interacts with JAK3 (PubMed:10733938).
CC Interacts with MSR1 and CD14 (By similarity).
CC {ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:10733938,
CC ECO:0000269|PubMed:15582604}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92614}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92614}.
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 (By similarity).
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:0000250|UniProtKB:Q92614}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000269|PubMed:12761286}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:12761286}. Note=Colocalizes with
CC actin. {ECO:0000269|PubMed:12761286}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:12761286}. Note=Lacks the PDZ domain. Diffusely
CC localized in the cytoplasm. {ECO:0000269|PubMed:12761286}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=3; Synonyms=SP-R210L {ECO:0000303|PubMed:25965346};
CC IsoId=Q9JMH9-3; Sequence=Displayed;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9JMH9-1; Sequence=VSP_023062;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9JMH9-2; Sequence=VSP_007873, VSP_007874;
CC Name=4;
CC IsoId=Q9JMH9-4; Sequence=VSP_023061, VSP_023062;
CC Name=5;
CC IsoId=Q9JMH9-5; Sequence=VSP_007873, VSP_007874, VSP_023062;
CC Name=6;
CC IsoId=Q9JMH9-6; Sequence=VSP_023060;
CC Name=7;
CC IsoId=Q9JMH9-7; Sequence=VSP_007873, VSP_023059, VSP_023062;
CC -!- TISSUE SPECIFICITY: Isoform 1; Expressed ubiquitously. Isoform 2:
CC Specifically expressed in most hematopoietic cells. Isoform 3:
CC Predominantly expressed in alveolar macrophages (PubMed:25965346).
CC {ECO:0000269|PubMed:25965346}.
CC -!- DOMAIN: The myosin motor domain binds ADP and ATP but has no intrinsic
CC ATPase activity. Mediates ADP-dependent binding to actin (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine upon CSF1R activation. Isoform 6 is
CC phosphorylated on Ser-340. {ECO:0000269|PubMed:14969583}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AB026497; BAA93660.1; -; mRNA.
DR EMBL; AK137574; BAE23413.1; -; mRNA.
DR EMBL; AK147584; BAE28009.1; -; mRNA.
DR EMBL; AK171342; BAE42402.1; -; mRNA.
DR EMBL; AL591065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046638; AAH46638.1; -; mRNA.
DR EMBL; AY692137; AAV80765.1; -; mRNA.
DR EMBL; AY692138; AAV80766.1; -; mRNA.
DR EMBL; AY692139; AAV80767.1; -; mRNA.
DR CCDS; CCDS25085.1; -. [Q9JMH9-1]
DR RefSeq; NP_001278141.1; NM_001291212.1.
DR RefSeq; NP_001278142.1; NM_001291213.1.
DR RefSeq; NP_001278143.1; NM_001291214.1.
DR RefSeq; NP_001278144.1; NM_001291215.1.
DR RefSeq; NP_035716.1; NM_011586.3. [Q9JMH9-1]
DR RefSeq; XP_006533667.1; XM_006533604.3. [Q9JMH9-3]
DR RefSeq; XP_006533669.1; XM_006533606.2. [Q9JMH9-1]
DR RefSeq; XP_006533677.2; XM_006533614.3. [Q9JMH9-2]
DR RefSeq; XP_017170115.1; XM_017314626.1.
DR AlphaFoldDB; Q9JMH9; -.
DR SMR; Q9JMH9; -.
DR BioGRID; 237427; 16.
DR IntAct; Q9JMH9; 5.
DR MINT; Q9JMH9; -.
DR STRING; 10090.ENSMUSP00000130696; -.
DR iPTMnet; Q9JMH9; -.
DR PhosphoSitePlus; Q9JMH9; -.
DR jPOST; Q9JMH9; -.
DR MaxQB; Q9JMH9; -.
DR PaxDb; Q9JMH9; -.
DR PeptideAtlas; Q9JMH9; -.
DR PRIDE; Q9JMH9; -.
DR ProteomicsDB; 252618; -. [Q9JMH9-3]
DR ProteomicsDB; 252619; -. [Q9JMH9-1]
DR ProteomicsDB; 252620; -. [Q9JMH9-2]
DR ProteomicsDB; 252621; -. [Q9JMH9-4]
DR ProteomicsDB; 252622; -. [Q9JMH9-5]
DR ProteomicsDB; 252623; -. [Q9JMH9-6]
DR ProteomicsDB; 252624; -. [Q9JMH9-7]
DR Antibodypedia; 7183; 83 antibodies from 23 providers.
DR DNASU; 360013; -.
DR Ensembl; ENSMUST00000092884; ENSMUSP00000090560; ENSMUSG00000000631. [Q9JMH9-5]
DR Ensembl; ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631. [Q9JMH9-1]
DR Ensembl; ENSMUST00000102488; ENSMUSP00000099546; ENSMUSG00000000631. [Q9JMH9-1]
DR Ensembl; ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631. [Q9JMH9-3]
DR Ensembl; ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631. [Q9JMH9-4]
DR Ensembl; ENSMUST00000130305; ENSMUSP00000119574; ENSMUSG00000000631. [Q9JMH9-7]
DR Ensembl; ENSMUST00000130627; ENSMUSP00000119839; ENSMUSG00000000631. [Q9JMH9-6]
DR Ensembl; ENSMUST00000164334; ENSMUSP00000131771; ENSMUSG00000000631. [Q9JMH9-2]
DR GeneID; 360013; -.
DR KEGG; mmu:360013; -.
DR UCSC; uc007khg.2; mouse. [Q9JMH9-1]
DR UCSC; uc007khh.2; mouse. [Q9JMH9-5]
DR UCSC; uc007khi.2; mouse. [Q9JMH9-7]
DR CTD; 399687; -.
DR MGI; MGI:2667185; Myo18a.
DR VEuPathDB; HostDB:ENSMUSG00000000631; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155768; -.
DR InParanoid; Q9JMH9; -.
DR OMA; WLGHAKN; -.
DR PhylomeDB; Q9JMH9; -.
DR BioGRID-ORCS; 360013; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myo18a; mouse.
DR PRO; PR:Q9JMH9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JMH9; protein.
DR Bgee; ENSMUSG00000000631; Expressed in hindlimb stylopod muscle and 262 other tissues.
DR ExpressionAtlas; Q9JMH9; baseline and differential.
DR Genevisible; Q9JMH9; MM.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
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:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO:MGI.
DR GO; GO:0048194; P:Golgi vesicle budding; ISS:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903028; P:positive regulation of opsonization; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS: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; IPR036034; PDZ_sf.
DR PANTHER; PTHR45615:SF13; PTHR45615:SF13; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR Pfam; PF00595; PDZ; 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..2050
FT /note="Unconventional myosin-XVIIIa"
FT /id="PRO_0000123477"
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..1181
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1184..1213
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:0000250|UniProtKB:Q92614"
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 1051..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1955..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1242..1967
FT /evidence="ECO:0000255"
FT MOTIF 114..118
FT /note="Interaction with actin"
FT /evidence="ECO:0000250"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1955..1981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2050
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:0000250|UniProtKB:Q92614"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 1994
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 2002
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 2003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92614"
FT MOD_RES 2016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 2039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 2041
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..331
FT /note="Missing (in isoform 2, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007873"
FT VAR_SEQ 332..333
FT /note="AD -> ML (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007874"
FT VAR_SEQ 332..333
FT /note="AD -> MLLDPEAASPAYSQ (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_023059"
FT VAR_SEQ 333
FT /note="D -> DLDPEAASPAYSQ (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_023060"
FT VAR_SEQ 1567..1603
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_023061"
FT VAR_SEQ 1948..1962
FT /note="Missing (in isoform 1, isoform 4, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:10733906,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16087679,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023062"
FT MUTAGEN 503..504
FT /note="GK->SA: Loss of function."
FT /evidence="ECO:0000269|PubMed:19837035"
FT CONFLICT 399
FT /note="A -> T (in Ref. 2; BAE28009)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="R -> Q (in Ref. 2; BAE42402)"
FT /evidence="ECO:0000305"
FT CONFLICT 680..683
FT /note="Missing (in Ref. 2; BAE42402)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="E -> EPLEEQD (in Ref. 2; BAE28009)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="G -> D (in Ref. 2; BAE42402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1362
FT /note="D -> N (in Ref. 2; BAE42402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1655
FT /note="K -> R (in Ref. 2; BAE28009)"
FT /evidence="ECO:0000305"
FT CONFLICT 1978
FT /note="G -> R (in Ref. 5; AAV80766)"
FT /evidence="ECO:0000305"
FT CONFLICT 1990
FT /note="S -> P (in Ref. 5; AAV80765)"
FT /evidence="ECO:0000305"
FT CONFLICT 2027
FT /note="S -> F (in Ref. 5; AAV80767)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9JMH9-6:340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
SQ SEQUENCE 2050 AA; 232755 MW; 3D82B901F03D73B4 CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHP
GLGIPRPGPR SRVPELVTKR FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM
LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADAKTEEQI AAEEAWYETE KVWLVHRDGF
SLASQLKSEE LSLPEGKARV KLDHDGAILD VDEDDIEKAN APSCDRLEDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLSTRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIVLLGSS GSGKTTSFQH LVQYLATIAG TSGTKVFSVE KWQALSTLLE
AFGNSPTIMN GSATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY
LLACGDATLR TELHLNHLAE NNVFGIVPLS KPEEKQKAAQ QFSKLQAAMK VLAISPEEQK
TCWLILASIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQLKG
GTLQRSTSFR QGPEESGLGE GTKLSALECL EGMASGLYSE LFTLLISLVN RALKSSQHSL
CSMMIVDTPG FQNPEWGGSA RGASFEELCH NYAQDRLQRL FHERTFLQEL ERYKEDNIEL
AFDDLEPVAD DSVAAVDQAS HLVRSLAHAD EARGLLWLLE EEALVPGATE DALLDRLFSY
YGPQEGDKKG QSPLLRSSKP RHFLLGHSHG TNWVEYNVAG WLNYTKQNPA TQNAPRLLQD
SQKKIISNLF LGRAGSATVL SGSIAGLEGG SQLALRRATS MRKTFTTGMA AVKKKSLCIQ
IKLQVDALID TIKRSKMHFV HCFLPVAEGW PGEPRSASSR RVSSSSELDL PPGDPCEAGL
LQLDVSLLRA QLRGSRLLDA MRMYRQGYPD HMVFSEFRRR FDVLAPHLTK KHGRNYIVVD
EKRAVEELLE SLDLEKSSCC LGLSRVFFRA GTLARLEEQR DEQTSRHLTL FQAACRGYLA
RQHFKKRKIQ DLAIRCVQKN IKKNKGVKDW PWWKLFTTVR PLIQVQLSEE QIRNKDEEIQ
QLRSKLEKVE KERNELRLSS DRLETRISEL TSELTDERNT GESASQLLDA ETAERLRTEK
EMKELQTQYD ALKKQMEVME MEVMEARLIR AAEINGEVDD DDAGGEWRLK YERAVREVDF
TKKRLQQELE DKMEVEQQSR RQLERRLGDL QADSDESQRA LQQLKKKCQR LTAELQDTKL
HLEGQQVRNH ELEKKQRRFD SELSQAHEET QREKLQREKL QREKDMLLAE AFSLKQQMEE
KDLDIAGFTQ KVVSLEAELQ DISSQESKDE ASLAKVKKQL RDLEAKVKDQ EEELDEQAGS
IQMLEQAKLR LEMEMERMRQ THSKEMESRD EEVEEARQSC QKKLKQMEVQ LEEEYEDKQK
ALREKRELES KLSTLSDQVN QRDFESEKRL RKDLKRTKAL LADAQIMLDH LKNNAPSKRE
IAQLKNQLEE SEFTCAAAVK ARKAMEVEME DLHLQIDDIA KAKTALEEQL SRLQREKNEI
QNRLEEDQED MNELMKKHKA AVAQASRDMA QMNDLQAQIE ESNKEKQELQ EKLQALQSQV
EFLEQSMVDK SLVSRQEAKI RELETRLEFE KTQVKRLENL ASRLKETMEK LTEERDQRAA
AENREKEQNK RLQRQLRDTK EEMSELARKE AEASRKKHEL EMDLESLEAA NQSLQADLKL
AFKRIGDLQA AIEDEMESDE NEDLINSLQD MVTKYQKKKN KLEGDSDVDS ELEDRVDGVK
SWLSKNKGPS KAPSDDGSLK SSSPTSHWKP LAPDPSDDEH DPVDSISRPR FSHSYLSDSD
TEAKLTETSA
