SMY1_YEAST
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 03-AUG-2022, entry version 174.
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; 216.
DR DIP; DIP-4476N; -.
DR IntAct; P32364; 3.
DR MINT; P32364; -.
DR STRING; 4932.YKL079W; -.
DR iPTMnet; P32364; -.
DR MaxQB; P32364; -.
DR PaxDb; P32364; -.
DR PRIDE; P32364; -.
DR EnsemblFungi; YKL079W_mRNA; YKL079W; YKL079W.
DR GeneID; 853783; -.
DR KEGG; sce:YKL079W; -.
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 BioCyc; YEAST:G3O-31874-MON; -.
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:0003777; F:microtubule motor activity; 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 Gene3D; 3.40.850.10; -; 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; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 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
