MYO52_SCHPO
ID MYO52_SCHPO Reviewed; 1516 AA.
AC O94477; P78899; Q9US73;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Myosin-52;
DE AltName: Full=Myosin type V-2;
GN Name=myo52; ORFNames=SPCC1919.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1001-1516.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1280-1383, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11112691; DOI=10.1242/jcs.114.1.69;
RA Win T.Z., Gachet Y., Mulvihill D.P., May K.M., Hyams J.S.;
RT "Two type V myosins with non-overlapping functions in the fission yeast
RT Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and
RT cytokinesis, Myo51 is a component of the cytokinetic actin ring.";
RL J. Cell Sci. 114:69-79(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1065 AND SER-1072, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in cell wall deposition where it has a role in the
CC localization of mok1. {ECO:0000269|PubMed:11112691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:11112691}. Note=Localized at the cell poles and
CC septum.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22641.1; -; Genomic_DNA.
DR EMBL; D89250; BAA13911.1; ALT_SEQ; mRNA.
DR EMBL; AB028001; BAA87305.1; -; Genomic_DNA.
DR PIR; T41235; T41235.
DR PIR; T43173; T43173.
DR RefSeq; NP_588492.1; NM_001023482.2.
DR AlphaFoldDB; O94477; -.
DR SMR; O94477; -.
DR BioGRID; 275427; 31.
DR STRING; 4896.SPCC1919.10c.1; -.
DR iPTMnet; O94477; -.
DR MaxQB; O94477; -.
DR PaxDb; O94477; -.
DR PRIDE; O94477; -.
DR EnsemblFungi; SPCC1919.10c.1; SPCC1919.10c.1:pep; SPCC1919.10c.
DR GeneID; 2538846; -.
DR KEGG; spo:SPCC1919.10c; -.
DR PomBase; SPCC1919.10c; myo52.
DR VEuPathDB; FungiDB:SPCC1919.10c; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; O94477; -.
DR OMA; WRGHRAF; -.
DR PhylomeDB; O94477; -.
DR Reactome; R-SPO-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SPO-9013425; RHOT1 GTPase cycle.
DR PRO; PR:O94477; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:PomBase.
DR GO; GO:0061572; P:actin filament bundle organization; IMP:PomBase.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:1904601; P:protein localization to actin fusion focus; IMP:PomBase.
DR GO; GO:1990896; P:protein localization to cell cortex of cell tip; IMP:PomBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IMP:PomBase.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
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; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1516
FT /note="Myosin-52"
FT /id="PRO_0000123483"
FT DOMAIN 7..62
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 73..766
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 793..813
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 818..838
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 840..865
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 866..886
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 888..917
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1163..1431
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 647..669
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT COILED 926..1034
FT /evidence="ECO:0000255"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1072
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1516 AA; 175155 MW; 0D25F6FB65B19B39 CRC64;
MTSGIYYKGL QCWIPDEQSQ WIPGSIKDCR VEGEKAFLTV QDENENETVI TVKPDDLNYE
GRNGLPFLRS INSDADDLTD LSYLNEPSVL DALSTRYNQL QIYTYSGIVL IAVNPFQRLP
NLYTHEIVRA YSEKSRDELD PHLYAIAEDS YKCMNQEHKN QTIIISGESG AGKTVSARYI
MRYFASVQAL IQSTDSNFHE APQLTAVENE ILATNPIMEA FGNSKTSRND NSSRFGKYIQ
ILFDGNATII GAKIQTYLLE RSRLVFQPNQ ERNYHIFYQI LAGSSSEQLE KWKLVENSQE
FNYLKQGNCS TIEGVNDKEE FKATVDALKT VGIDNDTCEC IFSLLAALLH IGNIEVKHSR
NDAYIDSKNE NLINATSLLG VDPSSLVKWL TKRKIKMASE GILKPLNEFQ AVVARDSVAK
FLYASLFDWL VATINKALMY SADKSNQTAK SFIGVLDIYG FEHFKKNSFE QFCINYANEK
LQQEFYRHVF KLEQEEYAAE GLNWSYIDYQ DNQQCISMIE SRLGILSLLD EECRMPTNSD
ENWVSKLNDA FSKPEFKNSY QKSRFGNKEF TIKHYALDVV YCAEGFIDKN RDTISDELLE
LFTNSDVPFV KDLVLFRLEQ TAPPADTKKI KTKPKSNTLG SMFKSSLVSL MSTINETNAH
YIRCIKPNEE KEAWKFDNQM VVSQLRACGV LETIKISCAG FPSRWTFDEF VSRYYMLVPS
AVRTTESLTF SKAILEKHAD PTKYQIGKTK IFFRSGVTPL LESARDKALK HAAHLLYEAF
AVNYYRTRFL LSRKRVRSFQ AVAHGFLSRR HTEYELLSSN IIKLQSLWRT ALKRKEFIQT
KNSILKVQSI IRGFLLRQTL EEKTKHDATL IIQSLWLTFK AHKHYKELQY YAVRIQSLWR
MKLAKRQLTE LKIESTKASH LKQVSYRLES RLFEISKQLD NSEQENNKFR ERIAELESHL
SNYAEAKLAQ ERELEQTRVL ISDQSQDGEL KELLEEKENA LIMMEEEMRQ VNDANTELLR
VNATLKSQLK NYDMIIVEQT SQLKEKNRII ASLTKATKIL NSASSIEQSR NSEEKSRRDS
SLMEMRTQKE MLVLLMNDGL KHDLDKLTEY AGRTFTTLKT LLLKDNDVEA QKLDHLFLAK
LLFIIISQMW KSNLCQESVA LVERYCVHTL EYVFQKTSSA NERPDIGFWV ANTHALLAFV
YTKQQAFKHS SAFTLLSTES HESVQTIFEM IESHLSKIFF EWVRQVNNFL KPLIVQAMII
TGTNTDAGDE NRKLRIKFFE KPKYKITDVI HVLNKVHDSC QAYKVNYEIY NALIRSIYRF
INVEAFNSLF IDERGSWKRG TNISYNYHVL KDWCLESGVP EAYLQLEELL QTSKILQFVK
DDPNYVARVR DFYALNFLQI KTLLHRYDYA DYEAHVPKKT MSELSKNIVA EGINQREQLT
YEVLDYRLQD SFEESPSLEK IKIPDDCNVT YLRRIIDLAS AEESVEQALI TVGNVADNDV
QNSSDEENQV PNGIKV
