KIP3_YEAST
ID KIP3_YEAST Reviewed; 805 AA.
AC P53086; D6VTU0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Kinesin-like protein KIP3;
GN Name=KIP3; OrderedLocusNames=YGL216W;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23001566; DOI=10.1093/hmg/dds393;
RA Cederquist G.Y., Luchniak A., Tischfield M.A., Peeva M., Song Y.,
RA Menezes M.P., Chan W.M., Andrews C., Chew S., Jamieson R.V., Gomes L.,
RA Flaherty M., Grant P.E., Gupta M.L. Jr., Engle E.C.;
RT "An inherited TUBB2B mutation alters a kinesin-binding site and causes
RT polymicrogyria, CFEOM and axon dysinnervation.";
RL Hum. Mol. Genet. 21:5484-5499(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23001566}. Note=Colocalizes with beta-tubulin TUB2
CC at the plus ends of growing microtubules and along the microtubule
CC lattice. {ECO:0000269|PubMed:23001566}.
CC -!- MISCELLANEOUS: Present with 736 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. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; Z72739; CAA96933.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07901.1; -; Genomic_DNA.
DR PIR; S64238; S64238.
DR RefSeq; NP_011299.1; NM_001181081.1.
DR AlphaFoldDB; P53086; -.
DR SMR; P53086; -.
DR BioGRID; 33041; 216.
DR DIP; DIP-6383N; -.
DR IntAct; P53086; 5.
DR MINT; P53086; -.
DR STRING; 4932.YGL216W; -.
DR iPTMnet; P53086; -.
DR MaxQB; P53086; -.
DR PaxDb; P53086; -.
DR PRIDE; P53086; -.
DR EnsemblFungi; YGL216W_mRNA; YGL216W; YGL216W.
DR GeneID; 852655; -.
DR KEGG; sce:YGL216W; -.
DR SGD; S000003184; KIP3.
DR VEuPathDB; FungiDB:YGL216W; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000169309; -.
DR HOGENOM; CLU_001485_21_2_1; -.
DR InParanoid; P53086; -.
DR OMA; CVDDKML; -.
DR BioCyc; YEAST:G3O-30692-MON; -.
DR BRENDA; 5.6.1.3; 984.
DR PRO; PR:P53086; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53086; protein.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005880; C:nuclear microtubule; IDA:SGD.
DR GO; GO:0005634; C:nucleus; 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:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:SGD.
DR GO; GO:0070463; F:tubulin-dependent ATPase activity; IDA:SGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:SGD.
DR GO; GO:0051228; P:mitotic spindle disassembly; IMP:SGD.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:SGD.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR GO; GO:0070462; P:plus-end specific microtubule depolymerization; IDA:SGD.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP: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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..805
FT /note="Kinesin-like protein KIP3"
FT /id="PRO_0000125404"
FT DOMAIN 10..438
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 720..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..481
FT /evidence="ECO:0000255"
FT COMPBIAS 758..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 805 AA; 91090 MW; 6049EF2C13D5C2C7 CRC64;
MNVPETRQSS IVVAIRVRPF TSMEKTRLVN EASGAEANFP GLGDSSLILP MSNNSDSDID
IDAEEGSTRS KRNSLLRRKV IRPEGIRKIV DCVDDRMLIF DPADRNPLNK VSDQVLNSMR
ARATKATASS INNSNATNKF SSQRRRHGGE IKFVFDKLFD ETSSQARVYK ETTSPLLDSV
LDGFNSTVFA YGATGCGKTY TVSGTPSQPG IIFLAMEELF NKITDLKDEK DFEISLSYLE
IYNERIRDLL KPETPSKRLV IREDTQNHIK VANLSYHHPN TVEDVMDLVV QGNINRTTSP
TEANEVSSRS HAVLQIHIMQ TNKLVDLTSQ HTFATLSIID LAGSERAAAT RNRGIRLHEG
ANINRSLLAL GNCINALCLN DGSRSCHIPY RDSKLTRLLK FSLGGNCKTV MIVCISPSSS
HYDETLNTLK YANRAKEIKT KIIRNQQSLS RHVGSYLKMI TEQKRQIEEL REREEKMISL
KLTKYKLNKE KIQLAINECV NRVQQTYAGV ETYQVAKTLK SLILCKRRFL QMVKLEVDNL
ILLFEREEST AAEMQPVISN CRMISGQLYN KIHELEMKFD ETDTLSSVIH QVHSIDLNKL
REMEDWDETY DLVYLESCLN QISELQRNEI LVNSSIMTEK LMSDPGLNSR FKFLSKWLMN
RTPNIESIIQ DLVHIDEEFE SFARTFIANP DSNFTNTNIN IINTTAADLA VPAETLQRQN
FSQKKVKWTS PDLSPSPMIE PQPELEPELH QDQDAIASEV DVSMQDTTFN EQGPSTPSAP
TTAVPRRKMR SSLLTHQSLL ATARK
