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Database: UniProt
Entry: F7EH57_MACMU
LinkDB: F7EH57_MACMU
Original site: F7EH57_MACMU 
ID   F7EH57_MACMU            Unreviewed;      2565 AA.
AC   F7EH57;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Myosin XVIIIB {ECO:0000313|Ensembl:ENSMMUP00000004443.4};
GN   Name=MYO18B {ECO:0000313|Ensembl:ENSMMUP00000004443.4,
GN   ECO:0000313|VGNC:VGNC:74985};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000004443.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000004443.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000004443.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   STRING; 9544.ENSMMUP00000004443; -.
DR   PaxDb; 9544-ENSMMUP00000004443; -.
DR   Ensembl; ENSMMUT00000004711.4; ENSMMUP00000004443.4; ENSMMUG00000003334.4.
DR   VEuPathDB; HostDB:ENSMMUG00000003334; -.
DR   VGNC; VGNC:74985; MYO18B.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000158067; -.
DR   InParanoid; F7EH57; -.
DR   OMA; AMQLECC; -.
DR   TreeFam; TF339614; -.
DR   Proteomes; UP000006718; Chromosome 10.
DR   Bgee; ENSMMUG00000003334; Expressed in hindlimb stylopod muscle and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR   GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0016461; C:unconventional myosin complex; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   CDD; cd01386; MYSc_Myo18; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036064; MYSc_Myo18.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF8; UNCONVENTIONAL MYOSIN-XVIIIB; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN          571..1333
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          12..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2089..2108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2139..2191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2220..2245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2357..2379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2442..2477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2491..2565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1401..1774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1917..1958
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2021..2083
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        41..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2089..2103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2139..2156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2170..2185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2223..2240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2357..2372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2503..2519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2537..2559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         660..667
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2565 AA;  285150 MW;  F4A6761A35C09946 CRC64;
     MAISSRLALW EQKIREEDKS PPPSSPPPLF SVIPGGFIKQ LVRETEKEAK EARQRKQLAL
     ASLERETPEI SISEPNSKSS SGTRSGSQQI SQDNQSSSPG SSDILSKESE GVGSPDPERM
     TSINGEKAQE LGSSATPAKK TLPFKRGMRR GDVLLMVAKL DPDSAKPERT HPHDTPPCKT
     PPPATDTGKE KKGETSGAPC GPQASTEILA PKAEKTRTGG LGDAGQGTVA LKKGEKGQSI
     VGKGGGTPKT KELKEAEPQG KDRQGTRPQA QGPGEGVRPG KAEKEGGEPT SPVEKENISK
     NVGSEGKHVG PQIPERKWGS FLGRRSKWDG PQNKKDKEGV LLSKAEKTGE PQTQTEKKNQ
     MQGELGDDLR MGEKAGELRS MTGKAGESWD KKEKIGQPQG KSGKAGEARS QTEKGCEAPK
     EVSTMVESPV AAGKGGWSGR SGQEAERPCS REDVGSGALE TELEGPSQPA LEKDAERPRI
     QKENQDGLAP QEAGKGGQSR NSEQAPEDRW YEAEKVWLAQ KDGFTLATVL KPDEGTADLP
     AGRVRLCIDA DKSITEVDEE HVHRANPPEL DQAEDLASLI SVNESSVLNT LLQRYRAQRP
     HTCTGPDLIV LQPRGPSVPS AGKVPKGRRD GLPAHIGSMA QRAYWALLNQ RRDQSVVALG
     RSGAGKTACC EQVLEHLVGM AGSVDGKVSV EKIRATFTVL RAFGSVSMAH SCSATRFSMV
     MSLDFNATGR ITAAQLQTML LEKSRVARQP EGESNFQVFS QMLAGLDLDL RTELNLHQMA
     DSSSFGMGVW SKPEDKQKAA AAFAQLQGAM ETLGISESEQ RAIWRVLAAI YHLGAAGACK
     VGRKQFMRFE WANYAAEALG CEYEELNTAT FKHHLRQIIQ QMTFGPSQRG LEDEETSSGL
     KMTGVECVEG MASGLYQELF AAVVSLINRS FSSHHLSMAS IMVVDSPGFQ NPRHQGKDRA
     ATFEELCHNY AHERLQLLFY QRTFVSTLQR YREEGVPVQF DLPEPSPGTT VAAVDHNPSQ
     VRLPAGGGAQ DAKGLFWVLD EEVRVEGSSD SVVLERLCAA FEKKGAGTEG SSALRTCEQP
     LQCEIFHQLG WDPVRYDLTG WLHRAKPNLS ALDAPQVLQQ SKREELRSLF QARAKLPPVC
     RAVAGLEGTS QQALQRNRMV RRTFASSLAA VRRKAPCSQI KLQMDALTSM IKRSRLHFIH
     CLVLNPVVES RSEQESPTPP QPGRDKPGAG APLALDIPAL RVQLAGFHIL EALRLHRTGY
     ADHMGLTHFR RQFQVLDPPL LKKLMSTSEG IDERKAVEEL LETLDLEKKA VALGHSQVFL
     KAGVISRLER QREKLVSQSI ILFQAACKGF LSRQEFKKLK IRRLAAQCIQ KNVAVFLAVK
     DWPWWQLLGS LRPLLSATIG NEQLRAKEEE LTTLRRKLEK SEKLRNELRQ NTDLLESKIA
     DLTTELADER FKGDVACQVL ESERAERLQA FREVQELKSK HEQVQKKLGD VNKQLEEAQQ
     KIQLNDLERN PAGGADEWQM RFDCAQMENE FLRKRLQQCE ERLDSELTAR KELEQKLGEL
     QSAYDGAKKM AHQLKRKCHH LTCDLEDTRV LLENQQSRNH ELEKKQKKFD LQLAQALGES
     VFEKGLREKV TQENTSVRWE LGQLQQQLKQ KEQEASQLKQ EVEMLQDHKR ELLGSPSLGE
     NCVASLKERL WKLESSAVEQ QKVQSQQENT IKQLEQLRQR FELEIERMKQ MHQKDREDKE
     EELEDVRQSC QKRLRQLEMQ LEQEYEEKQM VLHEKQDLEG LIGTLCDQIG HRDFDVEKRL
     RRDLRRTHAL LSDVQLLLGT MEDGKTSVSK EELEKVHSQL EQSEAKCEEA LKTQKVLTAD
     LESMHSELEN MTRNKSLVDE QLYRLQFEKT DLLKRIDEDQ DDLYELMQKH KDLIAQSAAD
     IGQIQELQLQ LEEAKKEKHK LQEQLQVAQM RIEYLEQSTV DRAIVSRQEA VICDLENKTE
     FQKVQIKRFE VLVIRLRDSL IKMGEELSQA ATSESQQRES SQYYQRRLEE LKADMEELVQ
     REAEASRRCM ELEKYVEELG TVRQTLQTDL ETSIRRIADL QAALEEVASS DSDTESVQTA
     VDCGSSGKKE MDNVSILSSQ PEGSLQSWLS CTLSMATDTM RTPSRQSATS SRILSPRINE
     EAGDAERTQS APSRAWSTDV RSKTSGDKPV SPHFIRRQKY CHFGDGEGLA VQRKATERLE
     AASSPLASRS TNTSPLSREK LPSPSAALSE FVEGLRRKRA QRGQGSTLGL EDWPTLPIYQ
     TTGASTLRRG RAGSDEGNLS LRVGAKSPLE IEGAAGGLLR STSLKCISSD GVGGTTLLPE
     KAKTRFSSCE SLLESRPSMG RKLSSPTTPR DMLLSPTLRP RRRCLESSVD DAGCPDLGKE
     PLVFQNRQFA HLMEEPLGSD PFSWKLPSLD YERKTKVDFD DFLPAIRKPQ TPTSLAGGAK
     GGQDGSQRSS VHFETEEADR SFLSGIKTIL KKSPEPKEDP AHLSDSSSSS SSIVSFKSAD
     SIKSRPGIQR LAGDGGEGTS PEHREPGAGR KDDDVASIMK KYLQK
//
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