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Unconventional myosin-XVIIIa (Molecule associated with JAK3 N-terminus) (MAJN) (Myosin containing a PDZ domain) (Surfactant protein receptor SP-R210) (SP-R210)

 MY18A_MOUSE             Reviewed;        2050 AA.
Q9JMH9; Q3TBB2; Q3UH48; Q3UV60; Q5QD54; Q5QD55; Q5QD56; Q5SYN8; Q5SYN9;
Q5SYP0; Q5SYP1; Q811D7;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
17-JUN-2020, entry version 167.
RecName: Full=Unconventional myosin-XVIIIa;
AltName: Full=Molecule associated with JAK3 N-terminus;
Short=MAJN;
AltName: Full=Myosin containing a PDZ domain;
AltName: Full=Surfactant protein receptor SP-R210 {ECO:0000303|PubMed:25965346};
Short=SP-R210 {ECO:0000303|PubMed:25965346};
Name=Myo18a; Synonyms=Myspdz {ECO:0000303|PubMed:15582604};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=10733906; DOI=10.1006/bbrc.2000.2377;
Furusawa T., Ikawa S., Yanai N., Obinata M.;
"Isolation of a novel PDZ-containing myosin from hematopoietic supportive
bone marrow stromal cell lines.";
Biochem. Biophys. Res. Commun. 270:67-75(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 1-873 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Bone, and Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1032-2050 (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1933-2050 (ISOFORMS 1/4/5/7), AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Alveolus;
PubMed=16087679; DOI=10.1074/jbc.m505229200;
Yang C.H., Szeliga J., Jordan J., Faske S., Sever-Chroneos Z., Dorsett B.,
Christian R.E., Settlage R.E., Shabanowitz J., Hunt D.F., Whitsett J.A.,
Chroneos Z.C.;
"Identification of the surfactant protein A receptor 210 as the
unconventional myosin 18A.";
J. Biol. Chem. 280:34447-34457(2005).
[6]
INTERACTION WITH JAK3.
PubMed=10733938; DOI=10.1006/bbrc.2000.2413;
Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.;
"A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2
deprival.";
Biochem. Biophys. Res. Commun. 270:267-271(2000).
[7]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1
AND 2), AND DIFFERENTIAL EXPRESSION.
TISSUE=Spleen;
PubMed=12761286; DOI=10.1093/jb/mvg053;
Mori K., Furusawa T., Okubo T., Inoue T., Ikawa S., Yanai N., Mori K.J.,
Obinata M.;
"Genome structure and differential expression of two isoforms of a novel
PDZ-containing myosin (MysPDZ) (Myo18A).";
J. Biochem. 133:405-413(2003).
[8]
PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14969583; DOI=10.1042/bj20031978;
Cross M., Csar X.F., Wilson N.J., Manes G., Addona T.A., Marks D.C.,
Whitty G.A., Ashman K., Hamilton J.A.;
"A novel 110 kDa form of myosin XVIIIA (MysPDZ) is tyrosine-phosphorylated
after colony-stimulating factor-1 receptor signalling.";
Biochem. J. 380:243-253(2004).
[9]
HOMODIMER, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN.
PubMed=15582604; DOI=10.1016/j.bbrc.2004.11.058;
Mori K., Matsuda K., Furusawa T., Kawata M., Inoue T., Obinata M.;
"Subcellular localization and dynamics of MysPDZ (Myo18A) in live mammalian
cells.";
Biochem. Biophys. Res. Commun. 326:491-498(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-164;
SER-1966; SER-2037 AND SER-2039, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2037 AND SER-2039, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion affinity
chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[13]
FUNCTION IN GOLGI ORGANIZATION, AND MUTAGENESIS OF 503-GLY-LYS-504.
PubMed=19837035; DOI=10.1016/j.cell.2009.07.052;
Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.K., Kerr M.L.,
Peterman M.C., Sim R., Wiharto P.A., Galbraith K.A., Madhavarapu S.,
Fuchs G.J., Meerloo T., Farquhar M.G., Zhou H., Field S.J.;
"GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch
and shape the Golgi to promote budding.";
Cell 139:337-351(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-83; SER-102; SER-103;
SER-157; SER-160; SER-164; SER-983; SER-1966; SER-1994; SER-2016; SER-2032;
SER-2037; SER-2039 AND THR-2041, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION.
PubMed=21123169; DOI=10.1074/jbc.m110.125567;
Sever-Chroneos Z., Krupa A., Davis J., Hasan M., Yang C.H., Szeliga J.,
Herrmann M., Hussain M., Geisbrecht B.V., Kobzik L., Chroneos Z.C.;
"Surfactant protein A (SP-A)-mediated clearance of Staphylococcus aureus
involves binding of SP-A to the staphylococcal adhesin eap and the
macrophage receptors SP-A receptor 210 and scavenger receptor class A.";
J. Biol. Chem. 286:4854-4870(2011).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25965346; DOI=10.1371/journal.pone.0126576;
Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
Christensen N.D., Chroneos Z.C.;
"SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
and activation.";
PLoS ONE 10:E0126576-E0126576(2015).
-!- FUNCTION: May link Golgi membranes to the cytoskeleton and participate
in the tensile force required for vesicle budding from the Golgi.
Thereby, may play a role in Golgi membrane trafficking and could
indirectly give its flattened shape to the Golgi apparatus
(PubMed:19837035). Alternatively, in concert with LURAP1 and
CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin
retrograde flow that is crucial to cell protrusion and migration (By
similarity). May be involved in the maintenance of the stromal cell
architectures required for cell to cell contact (PubMed:10733906).
Regulates trafficking, expression, and activation of innate immune
receptors on macrophages. Plays a role to suppress inflammatory
responsiveness of macrophages via a mechanism that modulates CD14
trafficking (PubMed:25965346). Acts as a receptor of surfactant-
associated protein A (SFTPA1/SP-A) and plays an important role in
internalization and clearance of SFTPA1-opsonized S.aureus by alveolar
macrophages (PubMed:21123169). Strongly enhances natural killer cell
cytotoxicity (By similarity). {ECO:0000250|UniProtKB:Q92614,
ECO:0000269|PubMed:10733906, ECO:0000269|PubMed:19837035,
ECO:0000269|PubMed:21123169, ECO:0000269|PubMed:25965346}.
-!- SUBUNIT: Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB
and LURAP1 with the latter acting as an adapter connecting
CDC42BPA/CDC42BPB and MYO18A (By similarity). Binds F-actin; regulated
by ADP and GOLPH3 (PubMed:15582604). Interacts with GOLPH3; the
interaction is direct and may link Golgi membranes to the actin
cytoskeleton (By similarity). Interacts with JAK3 (PubMed:10733938).
Interacts with MSR1 and CD14 (By similarity).
{ECO:0000250|UniProtKB:Q92614, ECO:0000269|PubMed:10733938,
ECO:0000269|PubMed:15582604}.
-!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92614}.
Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92614}.
Postsynaptic Golgi apparatus {ECO:0000250|UniProtKB:D3ZFD0}. Cytoplasm,
cytoskeleton, microtubule organizing center
{ECO:0000250|UniProtKB:D3ZFD0}. Note=Recruited to the Golgi apparatus
by GOLPH3 (By similarity). Localizes to the postsynaptic Golgi
apparatus region, also named Golgi outpost, which shapes dendrite
morphology by functioning as sites of acentrosomal microtubule
nucleation (By similarity). {ECO:0000250|UniProtKB:D3ZFD0,
ECO:0000250|UniProtKB:Q92614}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000269|PubMed:12761286}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:12761286}. Note=Colocalizes with
actin. {ECO:0000269|PubMed:12761286}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
{ECO:0000269|PubMed:12761286}. Note=Lacks the PDZ domain. Diffusely
localized in the cytoplasm. {ECO:0000269|PubMed:12761286}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=3; Synonyms=SP-R210L {ECO:0000303|PubMed:25965346};
IsoId=Q9JMH9-3; Sequence=Displayed;
Name=1; Synonyms=Alpha;
IsoId=Q9JMH9-1; Sequence=VSP_023062;
Name=2; Synonyms=Beta;
IsoId=Q9JMH9-2; Sequence=VSP_007873, VSP_007874;
Name=4;
IsoId=Q9JMH9-4; Sequence=VSP_023061, VSP_023062;
Name=5;
IsoId=Q9JMH9-5; Sequence=VSP_007873, VSP_007874, VSP_023062;
Name=6;
IsoId=Q9JMH9-6; Sequence=VSP_023060;
Name=7;
IsoId=Q9JMH9-7; Sequence=VSP_007873, VSP_023059, VSP_023062;
-!- TISSUE SPECIFICITY: Isoform 1; Expressed ubiquitously. Isoform 2:
Specifically expressed in most hematopoietic cells. Isoform 3:
Predominantly expressed in alveolar macrophages (PubMed:25965346).
{ECO:0000269|PubMed:25965346}.
-!- DOMAIN: The myosin motor domain binds ADP and ATP but has no intrinsic
ATPase activity. Mediates ADP-dependent binding to actin (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine upon CSF1R activation. Isoform 6 is
phosphorylated on Ser-340. {ECO:0000269|PubMed:14969583}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
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EMBL; AB026497; BAA93660.1; -; mRNA.
EMBL; AK137574; BAE23413.1; -; mRNA.
EMBL; AK147584; BAE28009.1; -; mRNA.
EMBL; AK171342; BAE42402.1; -; mRNA.
EMBL; AL591065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC046638; AAH46638.1; -; mRNA.
EMBL; AY692137; AAV80765.1; -; mRNA.
EMBL; AY692138; AAV80766.1; -; mRNA.
EMBL; AY692139; AAV80767.1; -; mRNA.
CCDS; CCDS25085.1; -. [Q9JMH9-1]
RefSeq; NP_001278141.1; NM_001291212.1.
RefSeq; NP_001278142.1; NM_001291213.1.
RefSeq; NP_001278143.1; NM_001291214.1.
RefSeq; NP_001278144.1; NM_001291215.1.
RefSeq; NP_035716.1; NM_011586.3. [Q9JMH9-1]
RefSeq; XP_006533667.1; XM_006533604.3. [Q9JMH9-3]
RefSeq; XP_006533669.1; XM_006533606.2. [Q9JMH9-1]
RefSeq; XP_006533677.2; XM_006533614.3. [Q9JMH9-2]
RefSeq; XP_017170115.1; XM_017314626.1.
SMR; Q9JMH9; -.
BioGRID; 237427; 6.
IntAct; Q9JMH9; 8.
MINT; Q9JMH9; -.
STRING; 10090.ENSMUSP00000130696; -.
iPTMnet; Q9JMH9; -.
PhosphoSitePlus; Q9JMH9; -.
jPOST; Q9JMH9; -.
MaxQB; Q9JMH9; -.
PaxDb; Q9JMH9; -.
PeptideAtlas; Q9JMH9; -.
PRIDE; Q9JMH9; -.
Antibodypedia; 7183; 68 antibodies.
Ensembl; ENSMUST00000092884; ENSMUSP00000090560; ENSMUSG00000000631. [Q9JMH9-5]
Ensembl; ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631. [Q9JMH9-1]
Ensembl; ENSMUST00000102488; ENSMUSP00000099546; ENSMUSG00000000631. [Q9JMH9-1]
Ensembl; ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631. [Q9JMH9-3]
Ensembl; ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631. [Q9JMH9-4]
Ensembl; ENSMUST00000130305; ENSMUSP00000119574; ENSMUSG00000000631. [Q9JMH9-7]
Ensembl; ENSMUST00000130627; ENSMUSP00000119839; ENSMUSG00000000631. [Q9JMH9-6]
Ensembl; ENSMUST00000164334; ENSMUSP00000131771; ENSMUSG00000000631. [Q9JMH9-2]
GeneID; 360013; -.
KEGG; mmu:360013; -.
UCSC; uc007khg.2; mouse. [Q9JMH9-1]
UCSC; uc007khh.2; mouse. [Q9JMH9-5]
UCSC; uc007khi.2; mouse. [Q9JMH9-7]
CTD; 399687; -.
MGI; MGI:2667185; Myo18a.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00940000155768; -.
InParanoid; Q9JMH9; -.
KO; K10362; -.
PhylomeDB; Q9JMH9; -.
BioGRID-ORCS; 360013; 0 hits in 12 CRISPR screens.
ChiTaRS; Myo18a; mouse.
PRO; PR:Q9JMH9; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; Q9JMH9; protein.
Bgee; ENSMUSG00000000631; Expressed in skeletal muscle tissue and 284 other tissues.
ExpressionAtlas; Q9JMH9; baseline and differential.
Genevisible; Q9JMH9; MM.
GO; GO:0042641; C:actomyosin; ISO:MGI.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:MGI.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
GO; GO:0150051; C:postsynaptic Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISO:MGI.
GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
GO; GO:0090164; P:asymmetric Golgi ribbon formation; ISO:MGI.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
GO; GO:0090161; P:Golgi ribbon formation; ISO:MGI.
GO; GO:0048194; P:Golgi vesicle budding; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1903028; P:positive regulation of opsonization; IMP:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
CDD; cd01386; MYSc_Myo18; 1.
Gene3D; 2.30.42.10; -; 1.
Gene3D; 3.40.850.10; -; 1.
Gene3D; 4.10.270.10; -; 1.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR031244; MYO18A.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR027401; Myosin_IQ_contain_sf.
InterPro; IPR004009; Myosin_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR036064; MYSc_Myo18.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR45615:SF13; PTHR45615:SF13; 1.
Pfam; PF00063; Myosin_head; 2.
Pfam; PF01576; Myosin_tail_1; 1.
Pfam; PF00595; PDZ; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00015; IQ; 1.
SMART; SM00242; MYSc; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS51844; SH3_LIKE; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell junction; Coiled coil; Cytoplasm;
Cytoskeleton; Golgi apparatus; Motor protein; Myosin; Nucleotide-binding;
Phosphoprotein; Reference proteome; Synapse.
CHAIN 1..2050
/note="Unconventional myosin-XVIIIa"
/id="PRO_0000123477"
DOMAIN 220..311
/note="PDZ"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
DOMAIN 349..401
/note="Myosin N-terminal SH3-like"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
DOMAIN 405..1181
/note="Myosin motor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
DOMAIN 1184..1213
/note="IQ"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
NP_BIND 498..505
/note="ATP"
/evidence="ECO:0000255"
REGION 1..398
/note="Mediates nucleotide-independent binding to F-actin
and interaction with GOLPH3"
/evidence="ECO:0000250|UniProtKB:Q92614"
COILED 1242..1967
/evidence="ECO:0000255"
MOTIF 114..118
/note="Interaction with actin"
/evidence="ECO:0000250"
COMPBIAS 6..25
/note="Lys-rich"
MOD_RES 35
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 52
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 72
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079"
MOD_RES 74
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 79
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 83
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079"
MOD_RES 98
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 99
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 102
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 103
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 140
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 145
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 157
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 160
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 164
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079"
MOD_RES 234
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 983
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 1063
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1064
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1066
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1636
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1938
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1966
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079"
MOD_RES 1970
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 1994
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 1998
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 2002
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 2003
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92614"
MOD_RES 2016
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 2032
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 2037
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941, ECO:0000244|PubMed:21183079"
MOD_RES 2039
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941, ECO:0000244|PubMed:21183079"
MOD_RES 2041
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:21183079"
VAR_SEQ 1..331
/note="Missing (in isoform 2, isoform 5 and isoform 7)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_007873"
VAR_SEQ 332..333
/note="AD -> ML (in isoform 2 and isoform 5)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_007874"
VAR_SEQ 332..333
/note="AD -> MLLDPEAASPAYSQ (in isoform 7)"
/evidence="ECO:0000305"
/id="VSP_023059"
VAR_SEQ 333
/note="D -> DLDPEAASPAYSQ (in isoform 6)"
/evidence="ECO:0000305"
/id="VSP_023060"
VAR_SEQ 1567..1603
/note="Missing (in isoform 4)"
/evidence="ECO:0000305"
/id="VSP_023061"
VAR_SEQ 1948..1962
/note="Missing (in isoform 1, isoform 4, isoform 5 and
isoform 7)"
/evidence="ECO:0000303|PubMed:10733906,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16087679,
ECO:0000303|PubMed:16141072"
/id="VSP_023062"
MUTAGEN 503..504
/note="GK->SA: Loss of function."
/evidence="ECO:0000269|PubMed:19837035"
CONFLICT 399
/note="A -> T (in Ref. 2; BAE28009)"
/evidence="ECO:0000305"
CONFLICT 466
/note="R -> Q (in Ref. 2; BAE42402)"
/evidence="ECO:0000305"
CONFLICT 680..683
/note="Missing (in Ref. 2; BAE42402)"
/evidence="ECO:0000305"
CONFLICT 680
/note="E -> EPLEEQD (in Ref. 2; BAE28009)"
/evidence="ECO:0000305"
CONFLICT 798
/note="G -> D (in Ref. 2; BAE42402)"
/evidence="ECO:0000305"
CONFLICT 1362
/note="D -> N (in Ref. 2; BAE42402)"
/evidence="ECO:0000305"
CONFLICT 1655
/note="K -> R (in Ref. 2; BAE28009)"
/evidence="ECO:0000305"
CONFLICT 1978
/note="G -> R (in Ref. 5; AAV80766)"
/evidence="ECO:0000305"
CONFLICT 1990
/note="S -> P (in Ref. 5; AAV80765)"
/evidence="ECO:0000305"
CONFLICT 2027
/note="S -> F (in Ref. 5; AAV80767)"
/evidence="ECO:0000305"
MOD_RES Q9JMH9-6:340
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:16452087"
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


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WP1011: T Cell Receptor Signaling Pathway
WP1689: Porphyrin and chlorophyll metabolism
WP352: T Cell Receptor Signaling Pathway
WP480: T Cell Receptor Signaling Pathway
WP780: T Cell Receptor Signaling Pathway
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WP794: B Cell Receptor Signaling Pathway
WP10: IL-9 Signaling Pathway
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Related Genes :
[Jak3] Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3)
[JAK3] Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) (L-JAK)
[Jak3] Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3)
[Myo1c] Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb)
[MYO6 KIAA0389] Unconventional myosin-VI (Unconventional myosin-6)
[MYO9B MYR5] Unconventional myosin-IXb (Unconventional myosin-9b)
[MYO10 KIAA0799] Unconventional myosin-X (Unconventional myosin-10)
[MYO1C] Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb)
[Myo1c Myr2] Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb) (Myosin heavy chain myr 2)
[Myo19 Myohd1] Unconventional myosin-XIX (Myosin head domain-containing protein 1)
[Myo10] Unconventional myosin-X (Unconventional myosin-10)
[Myo9a Myr7] Unconventional myosin-IXa (Unconventional myosin-9a)
[MYO9A MYR7] Unconventional myosin-IXa (Unconventional myosin-9a)
[MYO15A MYO15] Unconventional myosin-XV (Unconventional myosin-15)
[MYO1E MYO1C] Unconventional myosin-Ie (Myosin-Ic) (Unconventional myosin 1E)
[MYO16 KIAA0865 MYO16B NYAP3] Unconventional myosin-XVI (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16)
[Myo15a Myo15] Unconventional myosin-XV (Unconventional myosin-15)
[MYO5A MYH12] Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle) (Myosin heavy chain 12) (Myosin-12) (Myoxin)
[Myo9b Myr5] Unconventional myosin-IXb (Unconventional myosin-9b)
[Myo9b Myr5] Unconventional myosin-IXb (Unconventional myosin-9b)
[MYO7A USH1B] Unconventional myosin-VIIa
[nnrE nnrD TR210_2552] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[Myo16 Myr8 Nyap3] Unconventional myosin-XVI (Myosin heavy chain myr 8) (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16)
[MYO5B KIAA1119] Unconventional myosin-Vb
[Myo5a Dilute] Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle)
[MYO10] Unconventional myosin-X (Unconventional myosin-10)
[Myo31DF Myo1D CG7438] Unconventional myosin ID (MyoID) (Brush border myosin IA) (BBMIA) (Myosin 1D) (Myo1D) (Myosin-IA) (MIA) (MyoIA)
[MYO19 MYOHD1] Unconventional myosin-XIX (Myosin head domain-containing protein 1)
[Myo10] Unconventional myosin-X (Unconventional myosin-10)
[Myo16 Kiaa0865 Nyap3] Unconventional myosin-XVI (Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3) (Unconventional myosin-16)

Bibliography :