ID   SMY1_YEAST              Reviewed;         656 AA.
AC   P32364; D6VXK8;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Kinesin-related protein SMY1;
DE   AltName: Full=Suppressor protein SMY1;
GN   Name=SMY1; OrderedLocusNames=YKL079W; ORFNames=YKL409;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1549181; DOI=10.1038/356358a0;
RA   Lillie S.H., Brown S.S.;
RT   "Suppression of a myosin defect by a kinesin-related gene.";
RL   Nature 356:358-362(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8203165; DOI=10.1002/yea.320100211;
RA   James C.M., Gent M.E., Indge K.J., Oliver S.G.;
RT   "Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies
RT   the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor
RT   and vacuolar ATPase subunit C plus a number of unidentified open reading
RT   frames.";
RL   Yeast 10:247-255(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185.
RX   PubMed=1730668; DOI=10.1016/s0021-9258(18)48351-2;
RA   Beltran C., Kopecky J., Pan Y.-C.E., Nelson H., Nelson N.;
RT   "Cloning and mutational analysis of the gene encoding subunit C of yeast
RT   vacuolar H(+)-ATPase.";
RL   J. Biol. Chem. 267:774-779(1992).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-583, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Possible microtubule-based motor that can interact or
CC       substitute with myosin 2 (MYO2).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; M77143; AAA34441.1; -; Genomic_DNA.
DR   EMBL; M69021; AAA35056.1; -; Genomic_DNA.
DR   EMBL; X75560; CAA53238.1; -; Genomic_DNA.
DR   EMBL; Z28079; CAA81916.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09078.1; -; Genomic_DNA.
DR   PIR; S25732; S25732.
DR   RefSeq; NP_012844.1; NM_001179645.1.
DR   PDB; 6IXQ; X-ray; 3.06 A; B=615-650.
DR   PDBsum; 6IXQ; -.
DR   AlphaFoldDB; P32364; -.
DR   SMR; P32364; -.
DR   BioGRID; 34053; 220.
DR   DIP; DIP-4476N; -.
DR   IntAct; P32364; 3.
DR   MINT; P32364; -.
DR   STRING; 4932.YKL079W; -.
DR   GlyGen; P32364; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P32364; -.
DR   MaxQB; P32364; -.
DR   PaxDb; 4932-YKL079W; -.
DR   PeptideAtlas; P32364; -.
DR   EnsemblFungi; YKL079W_mRNA; YKL079W; YKL079W.
DR   GeneID; 853783; -.
DR   KEGG; sce:YKL079W; -.
DR   AGR; SGD:S000001562; -.
DR   SGD; S000001562; SMY1.
DR   VEuPathDB; FungiDB:YKL079W; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   GeneTree; ENSGT00940000175167; -.
DR   HOGENOM; CLU_001485_32_0_1; -.
DR   InParanoid; P32364; -.
DR   OMA; HSSAYRE; -.
DR   OrthoDB; 5476186at2759; -.
DR   BioCyc; YEAST:G3O-31874-MONOMER; -.
DR   BioGRID-ORCS; 853783; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32364; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P32364; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IMP:SGD.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IGI:SGD.
DR   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115:SF817; KINESIN-LIKE PROTEIN KIF15; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Kinesin-related protein SMY1"
FT                   /id="PRO_0000125454"
FT   DOMAIN          27..364
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   BINDING         114..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         583
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   656 AA;  73799 MW;  EC070EADE9EC88BC CRC64;
     MHWNIISKEQ SSSSVSLPTL DSSEPCHIEV ILRAIPEKGL QNNESTFKID PYENTVLFRT
     NNPLHETTKE THSTFQFDKV FDANATQEDV QKFLVHPIIN DVLNGYNGTV ITYGPSFSGK
     SYSLIGSKES EGILPNICKT LFDTLEKNEE TKGDSFSVSV LAFEIYMEKT YDLLVPLPER
     KPLKLHRSSS KMDLEIKDIC PAHVGSYEDL RSYIQAVQNV GNRMACGDKT ERSRSHLVFQ
     LHVEQRNRKD DILKNSSLYL VDLHGAEKFD KRTESTLSQD ALKKLNQSIE ALKNTVRSLS
     MKERDSAYSA KGSHSSAYRE SQLTEVLKDS LGGNRKTKVI LTCFLSNVPT TLSTLEFGDS
     IRQINNKVTD NTTGLNLKKK MDLFIQDMKI KDDNYVAQIN ILKAEIDSLK SLHNKSLPED
     DEKKMLENTK KENIKLKLQL DSITQLLSSS TNEDPNNRID EEVSEILTKR CEQIAQLELS
     FDRQMNSNSK LQQELEYKKS KEEALESMNV RLLEQIQLQE REIQELLTTN AILKGELETH
     TKLTETRSER IKSLESSVKE LSLNKSAIPS PRRGSMSSSS GNTMLHIEEG SEISNSPWSA
     NTSSKPLVWG ARKVSSSSIA TTGSQESFVA RPFKKGLNLH SIKVTSSTPK SPSSGS
//