KN12B_ARATH
ID KN12B_ARATH Reviewed; 1313 AA.
AC Q8L7Y8; Q9LUG0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Kinesin-like protein KIN-12B {ECO:0000305};
DE AltName: Full=Phragmoplast-associated kinesin-related protein 1-like protein {ECO:0000303|PubMed:15258761};
DE Short=AtPAKRP1L {ECO:0000303|PubMed:15258761};
GN Name=KIN12B {ECO:0000305}; Synonyms=PAKRP1L {ECO:0000312|EMBL:AAN16470.1};
GN OrderedLocusNames=At3g23670 {ECO:0000312|Araport:AT3G23670};
GN ORFNames=MDB19.16 {ECO:0000312|EMBL:BAB02786.1};
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, SUBUNIT,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15258761; DOI=10.1007/s00425-004-1324-4;
RA Pan R., Lee Y.R., Liu B.;
RT "Localization of two homologous Arabidopsis kinesin-related proteins in the
RT phragmoplast.";
RL Planta 220:156-164(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17720869; DOI=10.1105/tpc.107.050716;
RA Lee Y.R., Li Y., Liu B.;
RT "Two Arabidopsis phragmoplast-associated kinesins play a critical role in
RT cytokinesis during male gametogenesis.";
RL Plant Cell 19:2595-2605(2007).
RN [8]
RP INTERACTION WITH TIO.
RX PubMed=22709276; DOI=10.1111/j.1365-313x.2012.05077.x;
RA Oh S.A., Allen T., Kim G.J., Sidorova A., Borg M., Park S.K., Twell D.;
RT "Arabidopsis Fused kinase and the Kinesin-12 subfamily constitute a
RT signalling module required for phragmoplast expansion.";
RL Plant J. 72:308-319(2012).
RN [9]
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: Plus-end directed kinesin-like motor enzyme that plays a
CC critical role in the organization of phragmoplast microtubules during
CC cytokinesis. Constitutes a signaling module in association with
CC serine/threonine-protein kinase TIO that is required to support
CC phragmoplast expansion and cell-plate growth in plant cells.
CC {ECO:0000269|PubMed:17720869}.
CC -!- SUBUNIT: Homodimer and heterodimer with KIN12A. Interacts with TIO.
CC {ECO:0000269|PubMed:15258761, ECO:0000269|PubMed:22709276}.
CC -!- INTERACTION:
CC Q8L7Y8; Q9LDN0: KIN12A; NbExp=2; IntAct=EBI-6280461, EBI-6280428;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:15258761}. Note=Localized to the midline of the
CC nascent phragmoplast (late anaphase) and remains associated with the
CC expanding phragmoplast ring.
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=Q8L7Y8-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Kin12a and kin12b double
CC mutant display defective pollen grains leading to the production of
CC fewer seeds. {ECO:0000269|PubMed:15258761,
CC ECO:0000269|PubMed:17720869}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02786.1; Type=Erroneous gene model prediction; Evidence={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; AF540489; AAN16470.1; -; mRNA.
DR EMBL; AF540490; AAN16471.1; -; Genomic_DNA.
DR EMBL; AB023036; BAB02786.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76798.1; -; Genomic_DNA.
DR EMBL; AY124006; AAM74514.1; -; mRNA.
DR RefSeq; NP_189009.2; NM_113271.4. [Q8L7Y8-1]
DR AlphaFoldDB; Q8L7Y8; -.
DR SMR; Q8L7Y8; -.
DR BioGRID; 7279; 1.
DR IntAct; Q8L7Y8; 2.
DR STRING; 3702.AT3G23670.1; -.
DR PaxDb; Q8L7Y8; -.
DR PRIDE; Q8L7Y8; -.
DR ProteomicsDB; 237093; -. [Q8L7Y8-1]
DR EnsemblPlants; AT3G23670.1; AT3G23670.1; AT3G23670. [Q8L7Y8-1]
DR GeneID; 821947; -.
DR Gramene; AT3G23670.1; AT3G23670.1; AT3G23670. [Q8L7Y8-1]
DR KEGG; ath:AT3G23670; -.
DR Araport; AT3G23670; -.
DR TAIR; locus:2088065; AT3G23670.
DR eggNOG; KOG4280; Eukaryota.
DR InParanoid; Q8L7Y8; -.
DR OMA; PPCRVEE; -.
DR OrthoDB; 130600at2759; -.
DR PhylomeDB; Q8L7Y8; -.
DR PRO; PR:Q8L7Y8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L7Y8; baseline and differential.
DR Genevisible; Q8L7Y8; AT.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0007112; P:male meiosis cytokinesis; IGI:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0080175; P:phragmoplast microtubule organization; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1313
FT /note="Kinesin-like protein KIN-12B"
FT /id="PRO_0000419696"
FT DOMAIN 96..431
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..302
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 331..337
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 380..384
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 429..467
FT /note="Neck"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 685..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 932..1003
FT /evidence="ECO:0000255"
FT COILED 1062..1130
FT /evidence="ECO:0000255"
FT COILED 1167..1241
FT /evidence="ECO:0000255"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1313 AA; 146612 MW; 517278F83CABAC95 CRC64;
MKHFMMPRNA ILRDIGESQS PNPSLTKSKS QRKIKSSKEN APPPDLNSLI PDHRSSPAKL
KSPLPPRPPS SNPLKRKLIA EATADNGVAI GVSDSGVKVI VRMKPPSKGE EEEMIVKKIS
NDALTINEQT FTFDSIADPE STQDEIFQLV GAPLVENCLA GFNSSVFAYG QTGSGKTYTM
WGPANGLLEE HLSGDQRGLT PRVFELLFAR LSEEQAKHAE RQLKYQCRCS FLEIYNEQIT
DLLDPSLKNL MIREDVKSGV YVENLTEEYV KNLKDLSKLL VKGLANRRTG ATSVNAESSR
SHCVFTCVVE SHCKSVADGL SSFKTSRINL VDLAGSERQK LTGAAGDRLK EAGNINRSLS
QLGNLINILA EISQTGKQRH IPYRDSRLTF LLQESLGGNA KLAMVCAVSP SQSCRSETFS
TLRFAQRAKA IQNKAIVNEV MQDDVNFLRE VIRQLRDELQ RVKDDKGNNP TNPNAAYTTS
WNARRSLSLL RSFGLGHPKS LPNGDDDGDT EMEIDEEAVE RLCAQMGLSP PAEDNNQEMS
RVEKINSSLQ TVVLKDESYN NSHLKSSEAT DVNMEDACCQ TENNGSETDN ALTVAETMDD
GSSVQPDSIT NSLHSCISDT NQGNSPSKAE NIPSCQDLVI EADVSAIVSV ADTSNNTEQV
SVNPVSPCLS VAPVSVSPVL IPPTESASPK IRNSRKSLRT TSMSTASQKD IERANQLTPE
VVEPSPAMST EVLNLYSALS TKKSEAFPVP TRQLAASLHR GMKLLDSYRQ STALRRSTFR
LSYKALECKP STVLSKADVG VQTYPQADEI AEDNSKEVLC SRCKCRAECD AQEISDTSNL
QLVPIDNSEG SEKSNFQVPK AVEKVLAGSI RREMAMEEFC TKQASEISQL NRLVQQYKHE
RECNAIIGQT REDKIVRLES LMDGVLSKDD FLDEEFASLM HEHKLLKDMY ENHPEVLQTR
IELKRVQEEL ESFKNFYGDM GEREVLLEEI HDLKAQLQCY TDSSLTSARR RGSLLKLTYA
CDPNQAPQLN TIPESVDEGP EKTLEQERLR WTEAESNWIS LAEELRTELD TNRLLMEKQK
RELDTEKRCA EELTEAMQMA MQGHARMIEQ YADLEEKHIQ LLARHRRIRE GIDDVKKAAA
RAGVKGAESR FINALAAEIS ALKVQREKEV RYFRDENKSL QSQLRDTAEA VQAAGELLVR
FKEAEEGLTF AQKRAMDAEY EASEAYKKVD KLKRKYETEI STVNQQHNAE PQNPIESLQA
SCNDDAMAKY DEPSASDGDN QWREEFQPFY KKDEELSKLA EPSWFSGYDR CNI
