MYO9A_HUMAN
ID MYO9A_HUMAN Reviewed; 2548 AA.
AC B2RTY4; B0I1T5; C9IYB3; C9JA86; Q14787; Q3YLD7; Q3YLD8; Q6P986; Q9H8T5;
AC Q9NTG2; Q9NUY2; Q9UEP3; Q9UNJ2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Unconventional myosin-IXa;
DE AltName: Full=Unconventional myosin-9a;
GN Name=MYO9A; Synonyms=MYR7;
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] (ISOFORMS 1 AND 5), TISSUE SPECIFICITY, AND
RP VARIANTS GLN-85; ASP-168; PRO-211; GLN-946; GLU-1193; PRO-1362 AND
RP CYS-1834.
RX PubMed=10409426; DOI=10.1006/geno.1999.5867;
RA Gorman S.W., Haider N.B., Grieshammer U., Swiderski R.E., Kim E.,
RA Welch J.W., Searby C., Leng S., Carmi R., Sheffield V.C., Duhl D.M.;
RT "The cloning and developmental expression of unconventional myosin IXA
RT (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at chromosome
RT 15q22-q23.";
RL Genomics 59:150-160(1999).
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 [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-1193.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP LYS-37 AND GLU-1193.
RC TISSUE=Placenta;
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 1-774 (ISOFORMS 1/4).
RX PubMed=9819351; DOI=10.1242/jcs.111.24.3597;
RA Chieregatti E., Gaertner A., Stoeffler H.-E., Baehler M.;
RT "Myr 7 is a novel myosin IX-RhoGAP expressed in rat brain.";
RL J. Cell Sci. 111:3597-3608(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-2548 (ISOFORM 1), AND VARIANT
RP GLU-1193.
RC TISSUE=Brain;
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: preparation of full-length cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 234-322 (ISOFORMS 1/2/3/4).
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-445 (ISOFORMS 1/2/3/4/5).
RX PubMed=16204458; DOI=10.1093/nar/gki870;
RA Hiller M., Huse K., Platzer M., Backofen R.;
RT "Non-EST based prediction of exon skipping and intron retention events
RT using Pfam information.";
RL Nucleic Acids Res. 33:5611-5621(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1223-2548 (ISOFORM 4).
RC TISSUE=Testis;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1981 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1984-2548 (ISOFORMS 1/2/4/5).
RC TISSUE=Ovary, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1299; SER-1317; SER-1364;
RP SER-2294 AND SER-2464, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
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 [15]
RP PHOSPHORYLATION.
RX PubMed=27169898; DOI=10.1038/srep25740;
RA Lee C.P., Chiang S.L., Ko A.M., Liu Y.F., Ma C., Lu C.Y., Huang C.M.,
RA Chang J.G., Kuo T.M., Chen C.L., Tsai E.M., Ko Y.C.;
RT "ALPK1 phosphorylates myosin IIA modulating TNF-alpha trafficking in gout
RT flares.";
RL Sci. Rep. 6:25740-25740(2016).
RN [16]
RP INVOLVEMENT IN CMS24, AND VARIANTS CMS24 HIS-1517; GLY-1698 AND HIS-2283.
RX PubMed=27259756; DOI=10.1093/brain/aww130;
RA O'Connor E., Toepf A., Mueller J.S., Cox D., Evangelista T., Colomer J.,
RA Abicht A., Senderek J., Hasselmann O., Yaramis A., Laval S.H.,
RA Lochmueller H.;
RT "Identification of mutations in the MYO9A gene in patients with congenital
RT myasthenic syndrome.";
RL Brain 139:2143-2153(2016).
RN [17]
RP INVOLVEMENT IN CMS24, AND VARIANTS CMS24 CYS-203 AND GLU-2282.
RX PubMed=26752647; DOI=10.1172/jci84457;
RA Bayram Y., Karaca E., Coban Akdemir Z., Yilmaz E.O., Tayfun G.A., Aydin H.,
RA Torun D., Bozdogan S.T., Gezdirici A., Isikay S., Atik M.M., Gambin T.,
RA Harel T., El-Hattab A.W., Charng W.L., Pehlivan D., Jhangiani S.N.,
RA Muzny D.M., Karaman A., Celik T., Yuregir O.O., Yildirim T., Bayhan I.A.,
RA Boerwinkle E., Gibbs R.A., Elcioglu N., Tuysuz B., Lupski J.R.;
RT "Molecular etiology of arthrogryposis in multiple families of mostly
RT Turkish origin.";
RL J. Clin. Invest. 126:762-778(2016).
RN [18]
RP VARIANT CMS24 513-ARG--VAL-2548 DEL.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Regulates Rho
CC by stimulating it's GTPase activity in neurons. Required for the
CC regulation of neurite branching and motor neuron axon guidance (By
CC similarity). {ECO:0000250|UniProtKB:Q8C170,
CC ECO:0000250|UniProtKB:Q9Z1N3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}.
CC Synapse {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell
CC bodies, dendrites and axons with occasional hints of an enrichment near
CC the plasma membrane. Localized at the neuromuscular junction (By
CC similarity). {ECO:0000250|UniProtKB:Q8C170,
CC ECO:0000250|UniProtKB:Q9Z1N3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=B2RTY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2RTY4-2; Sequence=VSP_035157;
CC Name=3;
CC IsoId=B2RTY4-3; Sequence=VSP_035158, VSP_035159;
CC Name=4;
CC IsoId=B2RTY4-4; Sequence=VSP_035160;
CC Name=5;
CC IsoId=B2RTY4-5; Sequence=VSP_035156;
CC -!- TISSUE SPECIFICITY: Found to be expressed in testis and placenta and at
CC lower levels in all the examined tissues with the exception of liver
CC (PubMed:10409426). Isoform 5: Found in leukocytes but not in brain,
CC retina or testis (PubMed:10409426). {ECO:0000269|PubMed:10409426}.
CC -!- PTM: Phosphorylated by ALPK1 following monosodium urate monohydrate
CC (MSU)-induced inflammation. {ECO:0000269|PubMed:27169898}.
CC -!- DISEASE: Myasthenic syndrome, congenital, 24, presynaptic (CMS24)
CC [MIM:618198]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features include easy fatigability
CC and muscle weakness. CMS24 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:26752647, ECO:0000269|PubMed:27259756,
CC ECO:0000269|PubMed:30237576}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 5]: Lacks the ATP-binding domain which suggests
CC that it cannot interact with actin. {ECO:0000305}.
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-9 (MYH9). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91979.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14517.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF117888; AAD49195.1; -; mRNA.
DR EMBL; AC020779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77880.1; -; Genomic_DNA.
DR EMBL; BC060886; AAH60886.1; -; mRNA.
DR EMBL; BC140869; AAI40870.1; -; mRNA.
DR EMBL; AJ001714; CAA04947.1; -; mRNA.
DR EMBL; AB290183; BAG06737.1; -; mRNA.
DR EMBL; L29148; AAA20911.1; -; mRNA.
DR EMBL; DQ088983; AAZ85978.1; -; mRNA.
DR EMBL; DQ088984; AAZ85979.1; -; mRNA.
DR EMBL; AL137287; CAB70679.1; -; mRNA.
DR EMBL; AK001923; BAA91979.1; ALT_INIT; mRNA.
DR EMBL; AK023306; BAB14517.1; ALT_INIT; mRNA.
DR CCDS; CCDS10239.1; -. [B2RTY4-1]
DR PIR; E59435; E59435.
DR PIR; I61699; I61699.
DR PIR; T46354; T46354.
DR RefSeq; NP_008832.2; NM_006901.3. [B2RTY4-1]
DR RefSeq; XP_006720602.1; XM_006720539.2. [B2RTY4-4]
DR AlphaFoldDB; B2RTY4; -.
DR SMR; B2RTY4; -.
DR BioGRID; 110733; 91.
DR IntAct; B2RTY4; 32.
DR STRING; 9606.ENSP00000348349; -.
DR GlyGen; B2RTY4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; B2RTY4; -.
DR PhosphoSitePlus; B2RTY4; -.
DR BioMuta; MYO9A; -.
DR EPD; B2RTY4; -.
DR jPOST; B2RTY4; -.
DR MassIVE; B2RTY4; -.
DR MaxQB; B2RTY4; -.
DR PaxDb; B2RTY4; -.
DR PeptideAtlas; B2RTY4; -.
DR PRIDE; B2RTY4; -.
DR ProteomicsDB; 3450; -. [B2RTY4-1]
DR ProteomicsDB; 3451; -. [B2RTY4-2]
DR ProteomicsDB; 3452; -. [B2RTY4-3]
DR ProteomicsDB; 3453; -. [B2RTY4-4]
DR ProteomicsDB; 3454; -. [B2RTY4-5]
DR Antibodypedia; 26536; 32 antibodies from 14 providers.
DR DNASU; 4649; -.
DR Ensembl; ENST00000356056.10; ENSP00000348349.5; ENSG00000066933.16. [B2RTY4-1]
DR Ensembl; ENST00000424560.2; ENSP00000399162.2; ENSG00000066933.16. [B2RTY4-3]
DR Ensembl; ENST00000444904.5; ENSP00000398250.2; ENSG00000066933.16. [B2RTY4-1]
DR GeneID; 4649; -.
DR KEGG; hsa:4649; -.
DR MANE-Select; ENST00000356056.10; ENSP00000348349.5; NM_006901.4; NP_008832.2.
DR UCSC; uc002atl.6; human. [B2RTY4-1]
DR CTD; 4649; -.
DR DisGeNET; 4649; -.
DR GeneCards; MYO9A; -.
DR GeneReviews; MYO9A; -.
DR HGNC; HGNC:7608; MYO9A.
DR HPA; ENSG00000066933; Tissue enhanced (retina).
DR MalaCards; MYO9A; -.
DR MIM; 604875; gene.
DR MIM; 618198; phenotype.
DR neXtProt; NX_B2RTY4; -.
DR OpenTargets; ENSG00000066933; -.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA31413; -.
DR VEuPathDB; HostDB:ENSG00000066933; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_7_5_1; -.
DR InParanoid; B2RTY4; -.
DR OMA; KYQAANM; -.
DR OrthoDB; 14881at2759; -.
DR PhylomeDB; B2RTY4; -.
DR TreeFam; TF316834; -.
DR PathwayCommons; B2RTY4; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; B2RTY4; -.
DR SIGNOR; B2RTY4; -.
DR BioGRID-ORCS; 4649; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; MYO9A; human.
DR GenomeRNAi; 4649; -.
DR Pharos; B2RTY4; Tbio.
DR PRO; PR:B2RTY4; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; B2RTY4; protein.
DR Bgee; ENSG00000066933; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; B2RTY4; baseline and differential.
DR Genevisible; B2RTY4; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0016461; C:unconventional myosin complex; NAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028558; MYO9A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; PTHR46184:SF3; 2.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Congenital myasthenic syndrome; Cytoplasm; Disease variant;
KW GTPase activation; Membrane; Metal-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..2548
FT /note="Unconventional myosin-IXa"
FT /id="PRO_0000348440"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..112
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..1016
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1021..1041
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1042..1071
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1074..1103
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1115..1144
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1138..1167
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2063..2251
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1999..2048
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 2068..2119
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 898..920
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1021..1162
FT /note="Neck or regulatory domain"
FT REGION 1163..2511
FT /note="Tail"
FT REGION 1223..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2359..2383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2401..2424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2490..2531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1264..1291
FT /evidence="ECO:0000255"
FT COILED 1486..1532
FT /evidence="ECO:0000255"
FT COILED 2315..2358
FT /evidence="ECO:0000255"
FT COMPBIAS 1319..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2368..2383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2410..2424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2496..2510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N3"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C170"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N3"
FT MOD_RES 1299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C170"
FT MOD_RES 2294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 45..280
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10409426"
FT /id="VSP_035156"
FT VAR_SEQ 367..385
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035157"
FT VAR_SEQ 729
FT /note="H -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035158"
FT VAR_SEQ 730..2548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035159"
FT VAR_SEQ 1714
FT /note="E -> EVARPAHKKKARMARTRSDFLTRGTFADGEGDTEEDDYDDIIEPLLS
FT LDQASHCELGPAPSLGQASHSDSEM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_035160"
FT VARIANT 37
FT /note="R -> K (in dbSNP:rs17855105)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046165"
FT VARIANT 85
FT /note="R -> Q"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046166"
FT VARIANT 161
FT /note="T -> I (in dbSNP:rs2929516)"
FT /id="VAR_046167"
FT VARIANT 168
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046168"
FT VARIANT 203
FT /note="Y -> C (in CMS24; unknown pathological significance;
FT dbSNP:rs374155761)"
FT /evidence="ECO:0000269|PubMed:26752647"
FT /id="VAR_081671"
FT VARIANT 211
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046169"
FT VARIANT 513..2548
FT /note="Missing (in CMS24; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30237576"
FT /id="VAR_082148"
FT VARIANT 825
FT /note="A -> V (in dbSNP:rs11637562)"
FT /id="VAR_056189"
FT VARIANT 946
FT /note="R -> Q (in dbSNP:rs754348944)"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046170"
FT VARIANT 1193
FT /note="G -> E (in dbSNP:rs2415129)"
FT /evidence="ECO:0000269|PubMed:10409426,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.6"
FT /id="VAR_046171"
FT VARIANT 1362
FT /note="S -> P (in dbSNP:rs55738821)"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046172"
FT VARIANT 1476
FT /note="P -> R (in dbSNP:rs16956375)"
FT /id="VAR_046173"
FT VARIANT 1517
FT /note="R -> H (in CMS24; unknown pathological significance;
FT dbSNP:rs149046541)"
FT /evidence="ECO:0000269|PubMed:27259756"
FT /id="VAR_081672"
FT VARIANT 1698
FT /note="D -> G (in CMS24; unknown pathological significance;
FT dbSNP:rs150726107)"
FT /evidence="ECO:0000269|PubMed:27259756"
FT /id="VAR_081673"
FT VARIANT 1795
FT /note="H -> Y (in dbSNP:rs16956367)"
FT /id="VAR_046174"
FT VARIANT 1805
FT /note="H -> Q (in dbSNP:rs2306575)"
FT /id="VAR_046175"
FT VARIANT 1834
FT /note="R -> C (in dbSNP:rs74475742)"
FT /evidence="ECO:0000269|PubMed:10409426"
FT /id="VAR_046176"
FT VARIANT 2282
FT /note="G -> E (in CMS24; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26752647"
FT /id="VAR_081674"
FT VARIANT 2283
FT /note="R -> H (in CMS24; unknown pathological significance;
FT dbSNP:rs142345927)"
FT /evidence="ECO:0000269|PubMed:27259756"
FT /id="VAR_081675"
FT VARIANT 2390
FT /note="I -> V (in dbSNP:rs2291280)"
FT /id="VAR_046177"
FT CONFLICT 88
FT /note="L -> R (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> Q (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="R -> H (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="H -> R (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="D -> N (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="S -> P (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="S -> C (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="E -> D (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="C -> Y (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="I -> M (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="L -> I (in Ref. 5; CAA04947)"
FT /evidence="ECO:0000305"
FT CONFLICT 1591
FT /note="S -> P (in Ref. 10; BAB14517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2548 AA; 292706 MW; 867835BD2B841C84 CRC64;
MNINDGGRRR FEDNEHTLRI YPGAISEGTI YCPIPARKNS TAAEVIESLI NKLHLDKTKC
YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
SILIVINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEDER SAFHLKQPEE
YHYLNQITKK PLRQSWDDYC YDSEPDCFTV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
SLLSAILHLG NICYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEHNTKT LSIGVLDIFG
FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEDNSYIEF PAVMEPAFII KHYAGKVKYG
VKDFREKNTD HMRPDIVALL RSSKNAFISG MIGIDPVAVF RWAILRAFFR AMVAFREAGK
RNIHRKTGHD DTAPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD
LQGMNALNEK NQHDTFDIAW NGRTGIRQSR LSSGTSLLDK DGIFANSTSS KLLERAHGIL
TRNKNFKSKP ALPKHLLEVN SLKHLTRLTL QDRITKSLLH LHKKKKPPSI SAQFQASLSK
LMETLGQAEP YFVKCIRSNA EKLPLRFSDV LVLRQLRYTG MLETVRIRQS GYSSKYSFQD
FVSHFHVLLP RNIIPSKFNI QDFFRKINLN PDNYQVGKTM VFLKEQERQH LQDLLHQEVL
RRIILLQRWF RVLLCRQHFL HLRQASVIIQ RFWRNYLNQK QVRDAAVQKD AFVMASAAAL
LQASWRAHLE RQRYLELRAA AIVIQQKWRD YYRRRHMAAI CIQARWKAYR ESKRYQEQRK
KIILLQSTCR GFRARQRFKA LKEQRLRETK PEVGLVNIKG YGSLEIQGSD PSGWEDCSFD
NRIKAIEECK SVIESNRISR ESSVDCLKES PNKQQERAQS QSGVDLQEDV LVRERPRSLE
DLHQKKVGRA KRESRRMREL EQAIFSLELL KVRSLGGISP SEDRRWSTEL VPEGLQSPRG
TPDSESSQGS LELLSYEESQ KSKLESVISD EGDLQFPSPK ISSSPKFDSR DNALSASNET
SSAEHLKDGT MKEMVVCSSE SITCKPQLKD SFISNSLPTF FYIPQQDPLK TNSQLDTSIQ
RNKLLENEDT AGEALTLDIN RETRRYHCSG KDQIVPSLNT ESSNPVLKKL EKLNTEKEER
QKQLQQQNEK EMMEQIRQQT DILEKERKAF KTIEKPRIGE CLVAPSSYQS KQRVERPSSL
LSLNTSNKGE LNVLGSLSLK DAALAQKDSS SAHLPPKDRP VTVFFERKGS PCQSSTVKEL
SKTDRMGTQL NVACKLSNNR ISKREHFRPT QSYSHNSDDL SREGNARPIF FTPKDNMSIP
LVSKEALNSK NPQLHKEDEP AWKPVKLAGP GQRETSQRFS SVDEQAKLHK TMSQGEITKL
AVRQKASDSD IRPQRAKMRF WAKGKQGEKK TTRVKPTTQS EVSPLFAGTD VIPAHQFPDE
LAAYHPTPPL SPELPGSCRK EFKENKEPSP KAKRKRSVKI SNVALDSMHW QNDSVQIIAS
VSDLKSMDEF LLKKVNDLDN EDSKKDTLVD VVFKKALKEF RQNIFSFYSS ALAMDDGKSI
RYKDLYALFE QILEKTMRLE QRDSLGESPV RVWVNTFKVF LDEYMNEFKT SDCTATKVPK
TERKKRRKKE TDLVEEHNGH IFKATQYSIP TYCEYCSSLI WIMDRASVCK LCKYACHKKC
CLKTTAKCSK KYDPELSSRQ FGVELSRLTS EDRTVPLVVE KLINYIEMHG LYTEGIYRKS
GSTNKIKELR QGLDTDAESV NLDDYNIHVI ASVFKQWLRD LPNPLMTFEL YEEFLRAMGL
QERKETIRGV YSVIDQLSRT HLNTLERLIF HLVRIALQED TNRMSANALA IVFAPCILRC
PDTTDPLQSV QDISKTTTCV ELIVVEQMNK YKARLKDISS LEFAENKAKT RLSLIRRSMG
KGRIRRGNYP GPSSPVVVRL PSVSDVSEET LTSEAAMETD ITEQQQAAMQ QEERVLTEQI
ENLQKEKEEL TFEMLVLEPR ASDDETLESE ASIGTADSSE NLNMESEYAI SEKSERSLAL
SSLKTAGKSE PSSKLRKQLK KQQDSLDVVD SSVSSLCLSN TASSHGTRKL FQIYSKSPFY
RAASGNEALG MEGPLGQTKF LEDKPQFISR GTFNPEKGKQ KLKNVKNSPQ KTKETPEGTV
MSGRRKTVDP DCTSNQQLAL FGNNEFMV
