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KN5C_ARATH
ID   KN5C_ARATH              Reviewed;        1009 AA.
AC   P82266;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Kinesin-like protein KIN-5C {ECO:0000305};
DE   AltName: Full=AtKRP125b {ECO:0000303|PubMed:11472632};
GN   Name=KIN5C {ECO:0000305};
GN   OrderedLocusNames=At2g36200 {ECO:0000312|Araport:AT2G36200};
GN   ORFNames=F2H17.19 {ECO:0000312|EMBL:AAD21445.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 969-1009.
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=11472632; DOI=10.1186/1471-2164-2-2;
RA   Reddy A.S., Day I.S.;
RT   "Kinesins in the Arabidopsis genome: a comparative analysis among
RT   eukaryotes.";
RL   BMC Genomics 2:2-2(2001).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16448571; DOI=10.1186/1471-2164-7-18;
RA   Richardson D.N., Simmons M.P., Reddy A.S.;
RT   "Comprehensive comparative analysis of kinesins in photosynthetic
RT   eukaryotes.";
RL   BMC Genomics 7:18-18(2006).
RN   [6]
RP   REVIEW.
RX   PubMed=16530461; DOI=10.1016/j.tplants.2006.02.004;
RA   Vanstraelen M., Inze D., Geelen D.;
RT   "Mitosis-specific kinesins in Arabidopsis.";
RL   Trends Plant Sci. 11:167-175(2006).
RN   [7]
RP   REVIEW.
RX   PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
RA   Zhu C., Dixit R.;
RT   "Functions of the Arabidopsis kinesin superfamily of microtubule-based
RT   motor proteins.";
RL   Protoplasma 249:887-899(2012).
CC   -!- FUNCTION: Responsible for microtubule translocation. May be important
CC       for the organization of phragmoplast-specific arrays of microtubules
CC       (By similarity). Plays an essential role in stabilizing the mitotic
CC       spindle. Required during mitotic cytokinesis (By similarity).
CC       {ECO:0000250|UniProtKB:F4IIS5, ECO:0000250|UniProtKB:O23826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:F4IIS5}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:F4IIS5}. Note=Microtubule-associated.
CC       {ECO:0000250|UniProtKB:F4IIS5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P82266-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-5/BimC subfamily.
CC       {ECO:0000303|PubMed:16448571}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD21445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BX819626; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AC006921; AAD21445.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09215.1; -; Genomic_DNA.
DR   EMBL; BX819626; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; H84777; H84777.
DR   RefSeq; NP_181162.2; NM_129178.3. [P82266-1]
DR   AlphaFoldDB; P82266; -.
DR   SMR; P82266; -.
DR   STRING; 3702.AT2G36200.2; -.
DR   iPTMnet; P82266; -.
DR   PaxDb; P82266; -.
DR   PRIDE; P82266; -.
DR   ProteomicsDB; 238401; -. [P82266-1]
DR   EnsemblPlants; AT2G36200.1; AT2G36200.1; AT2G36200. [P82266-1]
DR   GeneID; 818192; -.
DR   Gramene; AT2G36200.1; AT2G36200.1; AT2G36200. [P82266-1]
DR   KEGG; ath:AT2G36200; -.
DR   Araport; AT2G36200; -.
DR   eggNOG; KOG0243; Eukaryota.
DR   InParanoid; P82266; -.
DR   OMA; HCRMEVL; -.
DR   PhylomeDB; P82266; -.
DR   PRO; PR:P82266; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P82266; baseline and differential.
DR   Genevisible; P82266; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR   GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR   Gene3D; 3.40.850.10; -; 1.
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   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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1009
FT                   /note="Kinesin-like protein KIN-5C"
FT                   /id="PRO_0000125376"
FT   DOMAIN          12..359
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          862..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          987..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..526
FT                   /evidence="ECO:0000255"
FT   BINDING         98..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1009 AA;  113683 MW;  B7554EEFF04676F4 CRC64;
     MSSRHDKEKG VNVQVLLRCR PFSDDELRSN APQVLTCNDL QREVAVSQNI AGKHIDRVFT
     FDKVFGPSAQ QKDLYDQAVV PIVNEVLEGF NCTIFAYGQT GTGKTYTMEG ECRRSKSAPC
     GGLPAEAGVI PRAVKQIFDT LEGQQAEYSV KVTFLELYNE EITDLLAPED LSRVAAEEKQ
     KKPLPLMEDG KGGVLVRGLE EEIVTSANEI FTLLERGSSK RRTAETFLNK QSSRSHSLFS
     ITIHIKEATP EGEELIKCGK LNLVDLAGSE NISRSGARDG RAREAGEINK SLLTLGRVIS
     ALVEHLGHVP YRDSKLTRLL RDSLGGRTKT CIIATVSPAV HCLEETLSTL DYAHRAKNIR
     NKPEVNQKMM KSTLIKDLYG EIERLKAEVY ASREKNGVYM PKERYYQEES ERKVMAEQIE
     QMGGQIENYQ KQLEELQDKY VGQVRECSDL TTKLDITEKN LSQTCKVLAS TNEELKKSQY
     AMKEKDFIIS EQKKSENVLV QQACILQSNL EKATKDNSSL HQKIGREDKL SADNRKVVDN
     YQVELSEQIS NLFNRVASCL SQQNVHLQGV NKLSQSRLEA HNKAILEMKK KVKASRDLYS
     SHLEAVQNVV RLHKANANAC LEEVSALTTS SACSIDEFLA SGDETTSSLF DELQSALSSH
     QGEMALFARE LRQRFHTTME QTQEMSEYTS TFFQKLMEES KNAETRAAEA NDSQINSIID
     FQKTYEAQSK SDTDKLIADL TNLVSSHIRR QHELVDSRLH NFKDAVSSNK TFLDEHVSAV
     NNLTKDAKRK WETFSMQAEN EAREGADFSA AKHCRMELLL QQSVGHAESA FKHCKITHES
     LKEMTSKQVT DVSSLVRSAC DSNEQHDAEV DSARTAAEKD VTKNSDDIIQ QIERMSEDEK
     ASVSKILENV RSHEKTLESF QQDQCCQARC IEDKAQETFQ QQYMEYEPTG ATPTKNEPEI
     PTKATIESLR AMPIETLVEE FRENNSYESF ATKETKPQQL TRSPLSQVN
 
 
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