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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//