KN7A_TOBAC
ID KN7A_TOBAC Reviewed; 959 AA.
AC Q8S950;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Kinesin-like protein NACK1;
DE AltName: Full=NPK1-activating kinesin-1;
GN Name=NACK1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH NPK1, AND INDUCTION.
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=11955449; DOI=10.1016/s0092-8674(02)00691-8;
RA Nishihama R., Soyano T., Ishikawa M., Araki S., Tanaka H., Asada T.,
RA Irie K., Ito M., Terada M., Banno H., Yamazaki Y., Machida Y.;
RT "Expansion of the cell plate in plant cytokinesis requires a kinesin-like
RT protein/MAPKKK complex.";
RL Cell 109:87-99(2002).
RN [2]
RP INTERACTION WITH NPK1.
RX PubMed=12472693; DOI=10.1046/j.1365-313x.2002.01469.x;
RA Ishikawa M., Soyano T., Nishihama R., Machida Y.;
RT "The NPK1 mitogen-activated protein kinase kinase kinase contains a
RT functional nuclear localization signal at the binding site for the NACK1
RT kinesin-like protein.";
RL Plant J. 32:789-798(2002).
RN [3]
RP FUNCTION, INTERACTION WITH NPK1, AND PHOSPHORYLATION AT THR-145; THR-675
RP AND THR-690.
RX PubMed=22006334; DOI=10.1073/pnas.1110174108;
RA Sasabe M., Boudolf V., De Veylder L., Inze D., Genschik P., Machida Y.;
RT "Phosphorylation of a mitotic kinesin-like protein and a MAPKKK by cyclin-
RT dependent kinases (CDKs) is involved in the transition to cytokinesis in
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17844-17849(2011).
CC -!- FUNCTION: Probable plus end-directed motor protein that functions in
CC the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway, which
CC is essential for somatic cell cytokinesis, especially for the cell-
CC plate formation and its expansion. Regulates the activity and the
CC localization of NPK1 by association through the non-catalytic region of
CC the kinase. {ECO:0000269|PubMed:11955449, ECO:0000269|PubMed:22006334}.
CC -!- SUBUNIT: Interacts (via C-terminus) with NPK1 (via C-terminus).
CC {ECO:0000269|PubMed:11955449, ECO:0000269|PubMed:12472693,
CC ECO:0000269|PubMed:22006334}.
CC -!- INTERACTION:
CC Q8S950; Q40541: NPK1; NbExp=6; IntAct=EBI-639977, EBI-639963;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11955449}. Nucleus
CC {ECO:0000269|PubMed:11955449}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:11955449}. Note=In interphase and prophase,
CC detected in the nucleus. From prometaphase to metaphase, found in the
CC cytoplasm in patches. At anaphase, distributed around the spindle
CC midzone and on the phragmoplast equator at telophase.
CC -!- INDUCTION: During the M phase of the cell cycle (at protein level).
CC {ECO:0000269|PubMed:11955449}.
CC -!- PTM: Phosphorylated at Thr-145, Thr-675 and Thr-690 by CDKAs and CDKBs.
CC The phosphorylation occurs before metaphase and inhibits the
CC interaction with NPK1 preventing the transition to cytokinesis.
CC {ECO:0000269|PubMed:22006334}.
CC -!- MISCELLANEOUS: Expression of a truncated protein lacking the motor
CC domain causes inhibition of phragmoplast expansion and multinucleate
CC cells. {ECO:0000305|PubMed:11955449}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-7 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB071435; BAB86283.1; -; mRNA.
DR RefSeq; NP_001312228.1; NM_001325299.1.
DR RefSeq; XP_016456327.1; XM_016600841.1.
DR AlphaFoldDB; Q8S950; -.
DR SMR; Q8S950; -.
DR IntAct; Q8S950; 1.
DR STRING; 4097.Q8S950; -.
DR iPTMnet; Q8S950; -.
DR PRIDE; Q8S950; -.
DR GeneID; 107780313; -.
DR KEGG; nta:107780313; -.
DR OMA; WIMGWNP; -.
DR OrthoDB; 122200at2759; -.
DR PhylomeDB; Q8S950; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0000919; P:cell plate assembly; IGI:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; IPR021881; NACK_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF11995; DUF3490; 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; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..959
FT /note="Kinesin-like protein NACK1"
FT /id="PRO_0000422318"
FT DOMAIN 30..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..756
FT /note="Required for the binding to NPK1"
FT /evidence="ECO:0000269|PubMed:12472693"
FT COILED 362..429
FT /evidence="ECO:0000255"
FT COILED 557..598
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22006334"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22006334"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22006334"
SQ SEQUENCE 959 AA; 108604 MW; 331EE6E49FB7D764 CRC64;
MTVRTPGTPA SKIDKTPATT PNGHRGREEK IVVTVRLRPL NKRELSAKDH AAWECIDDHT
IIYRPVPQER AAQPASSFTF DKVFGPDSIT EAVYEEGVKN VALSSLMGIN ATIFAYGQTS
SGKTYTMRGI TEKAVNDIYA HIMSTPEREF RIRISGLEIY NENVRDLLNS ESGRSLKLLD
DPEKGTVVEK LVEETASNDQ HLRHLISICE AQRQVGETAL NDTSSRSHQI IRLTIESTLR
ESSDCVRSYV ASLNFVDLAG SERASQTNAD GARLREGCHI NLSLMTLTTV IRKLSVGKRS
GHIPYRDSKL TRILQHSLGG NARTAIICTL SPASSHVEQS RNTLYFATRA KEVTNNAQVN
MVVSDKQLVK HLQKEVARLE AELRTPDPAN EKDWKIQQME MEIEELKRQR DLAQSQVDEL
RRKLQEEQGP KPSESVSPVV KKCLSFSGTL SPNLEEKAPV RSERTRNTMG RQSMRQSLAA
PFTLMHEIRK LEHLQEQLGD EANRALEVLQ KEVACHRLGN QDAAETIAKL QAEIREMRSI
RPLPKEVEVG SVVAVNKSVS ANLKEEIARL HSQGSTIADL EEQLENVQKS LDKLVMSLPS
NNDQQSNNDT TQKAKHPSKK KKLLPLTSSN SINRQNFLKS PCSPLSTARQ VLDCEVENRA
PDSDDLSCEI QPDETPTKSD GGDVSSKEGT PYRRSSSVNM RKMQKMFQEA AEENVRNIRS
YVTELKERVA KLQYQKQLLV CQVLELEANE AAGYNLEDDE NIHQIPEESP VSWQITFKEQ
RQQIIDLWDV CYVSIIHRSQ FYLLFKGDPA DEIYLEVELR RLTWLQQHLA ELGNATPARV
GNEPTVSLSS SIRALKRERE FLAKRLTTRL TAEERDYLYI KWEVPLEGKQ RRMQFINKLW
TNPHDAKHVH ESAEIVAKLV GFCEGGNMSR EMFELNFVLP SDRRPWFAGW NQISDLLHI
