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   27-MAR-2024, entry version 221.
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; 337.
DR   DIP; DIP-46631N; -.
DR   IntAct; Q92614; 197.
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; 9606-ENSP00000437073; -.
DR   PeptideAtlas; 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   Pumba; Q92614; -.
DR   ABCD; Q92614; 1 sequenced antibody.
DR   Antibodypedia; 7183; 103 antibodies from 23 providers.
DR   DNASU; 399687; -.
DR   Ensembl; ENST00000527372.7; ENSP00000437073.1; ENSG00000196535.20. [Q92614-1]
DR   Ensembl; ENST00000531253.5; ENSP00000434228.1; ENSG00000196535.20. [Q92614-4]
DR   Ensembl; ENST00000533112.5; ENSP00000435932.1; ENSG00000196535.20. [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   AGR; HGNC:31104; -.
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; LSQIFFR; -.
DR   OrthoDB; 3687088at2759; -.
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; 33 hits in 1155 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 95 other cell types or tissues.
DR   ExpressionAtlas; Q92614; baseline and differential.
DR   GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
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   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 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; SSF90257; Myosin rod fragments; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; Q92614; HS.
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
//