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KN14K_ARATH
ID   KN14K_ARATH             Reviewed;         975 AA.
AC   F4JX00; Q9FHD2;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Kinesin-like protein KIN-14K {ECO:0000305};
GN   Name=KIN14K {ECO:0000305};
GN   OrderedLocusNames=At5g41310 {ECO:0000312|Araport:AT5G41310};
GN   ORFNames=K1O13.11 {ECO:0000312|EMBL:BAB11107.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [3]
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   [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=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   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-14 subfamily.
CC       {ECO:0000303|PubMed:16448571}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AED94663.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB11107.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB019225; BAB11107.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB006707; BAB11107.1; JOINED; Genomic_DNA.
DR   EMBL; CP002688; AED94663.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_198947.1; NM_123496.2.
DR   AlphaFoldDB; F4JX00; -.
DR   SMR; F4JX00; -.
DR   STRING; 3702.AT5G41310.1; -.
DR   PaxDb; F4JX00; -.
DR   PeptideAtlas; F4JX00; -.
DR   PRIDE; F4JX00; -.
DR   GeneID; 834132; -.
DR   KEGG; ath:AT5G41310; -.
DR   Araport; AT5G41310; -.
DR   TAIR; locus:2155095; AT5G41310.
DR   eggNOG; KOG0239; Eukaryota.
DR   HOGENOM; CLU_001485_1_1_1; -.
DR   InParanoid; F4JX00; -.
DR   OrthoDB; 364605at2759; -.
DR   PRO; PR:F4JX00; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4JX00; baseline and differential.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   Gene3D; 1.10.418.10; -; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
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; PF00307; CH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Microtubule; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..975
FT                   /note="Kinesin-like protein KIN-14K"
FT                   /id="PRO_0000438046"
FT   DOMAIN          40..143
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          436..746
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          289..345
FT                   /evidence="ECO:0000255"
FT   COILED          757..788
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         520..527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   975 AA;  109700 MW;  4A86B3D3096B63D8 CRC64;
     MKNRIKKGSS MIGVYGRSDG SSSIQSSNGS ESRESIDDNK QGHQSLVEWL NETLPYLNLP
     WEASEEELRA CLVDGTVLCN LLNQLSPGSM RMGGSFEPGC VNIERFLAAM DEMTLPRFEV
     SDLEQGDMIR VIQSLKALKA SFSDDGYDKN TLSARRRWSL PADHSKGVDS NFNDGGSQFI
     EASEINTSHH SLQNTSTRSL FDMLDRLLDE SSQKMNVSHV YVSILRGIVQ VVEQRISNQA
     ENLKNQNILF RVREEKYRSR INVLETLASG TTDENEVRRK RCAPNRKGKE RSNAELSKLK
     QELEIVKETH EKQFLELKLN AQKAKVELER QVKNSELRVV EAKELEKLCE TKTKRWEKKE
     QTYKRFINHQ TEALQELKAT SMSLKHDVLK IGENYFLDLT YYGIKLRGVA HAAKNYQIII
     EENRRLYNEV QELKGNIRVY CRIRPFLQGQ NKKQTSIEYT GENGELVVAN PLKQGKDTYR
     LFKFNKVFGP ESTQEEVFLD TRPMIRSILD GYNVCIFAYG QTGSGKTYTM SGPSITSEED
     RGVNYRALND LFHLTQSRQN SVMYEVGVQM VEIYNEQVRD LLSQDVPDAS MHSVRSTEDV
     LELMNIGLMN RTVGATTLNE KSSRSHSVLS VHVRGVDVKT ESVLRGSLHL VDLAGSERVG
     RSEVTGERLK EAQHINKSLS ALGDVIFALA HKNPHVPYRN SKLTQVLQNS LGGQAKTLMF
     VQINPDEDSY AETVSTLKFA ERVSGVELGA ARSYKEGRDV RQLMEQVSNL KDMIAKKDEE
     LQKFQNINGI QKRGLSKLRI VSPPRRHSLG GALTNSPRRR QGPGLLGRTT SDIHRHQNES
     RSSSKFSGGA KDNNIFEDTE LLGFEESNNE ERLSDISDSC LSMGTETDGS ISSGAMELTL
     FPETSNPPEM FEQSEQNDKA HVGVGPSKPL KHTPKPDISK PSRLSISTTS SKALTSSKRP
     VTGISSSVKP LNRKR
 
 
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