NEK5_ARATH
ID NEK5_ARATH Reviewed; 956 AA.
AC Q0WPH8; A9CP44; Q9LXP3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine/threonine-protein kinase Nek5;
DE EC=2.7.11.1;
DE AltName: Full=NimA-related protein kinase 5;
DE Short=AtNEK6;
DE Short=AtNek5;
GN Name=NEK5; Synonyms=NEK6; OrderedLocusNames=At3g44200; ORFNames=F26G5.150;
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 [MRNA], FUNCTION, AND INTERACTION WITH ARK1; ARK2 AND
RP ARK3.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17971038; DOI=10.1111/j.1365-313x.2007.03327.x;
RA Sakai T., van der Honing H., Nishioka M., Uehara Y., Takahashi M.,
RA Fujisawa N., Saji K., Seki M., Shinozaki K., Jones M.A., Smirnoff N.,
RA Okada K., Wasteneys G.O.;
RT "Armadillo repeat-containing kinesins and a NIMA-related kinase are
RT required for epidermal-cell morphogenesis in Arabidopsis.";
RL Plant J. 53:157-171(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17886359; DOI=10.1111/j.1365-313x.2007.03161.x;
RA Vigneault F., Lachance D., Cloutier M., Pelletier G., Levasseur C.,
RA Seguin A.;
RT "Members of the plant NIMA-related kinases are involved in organ
RT development and vascularization in poplar, Arabidopsis and rice.";
RL Plant J. 51:575-588(2007).
CC -!- FUNCTION: Involved in epidermal-cell morphogenesis in hypocotyls and
CC roots. May act on the microtubule function. May have a secondary role
CC in trichome branching. {ECO:0000269|PubMed:17971038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with ARK1, ARK2 and ARK3 (via C-terminus).
CC {ECO:0000269|PubMed:17971038}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88428.1; 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; AB290931; BAF95588.1; -; mRNA.
DR EMBL; AL353814; CAB88428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77875.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65741.1; -; Genomic_DNA.
DR EMBL; AK229091; BAF00971.1; -; mRNA.
DR PIR; T49136; T49136.
DR RefSeq; NP_001327688.1; NM_001339123.1.
DR RefSeq; NP_190006.2; NM_114288.4.
DR AlphaFoldDB; Q0WPH8; -.
DR SMR; Q0WPH8; -.
DR BioGRID; 8862; 6.
DR IntAct; Q0WPH8; 1.
DR STRING; 3702.AT3G44200.1; -.
DR iPTMnet; Q0WPH8; -.
DR PaxDb; Q0WPH8; -.
DR PRIDE; Q0WPH8; -.
DR ProteomicsDB; 238853; -.
DR EnsemblPlants; AT3G44200.1; AT3G44200.1; AT3G44200.
DR EnsemblPlants; AT3G44200.2; AT3G44200.2; AT3G44200.
DR GeneID; 823542; -.
DR Gramene; AT3G44200.1; AT3G44200.1; AT3G44200.
DR Gramene; AT3G44200.2; AT3G44200.2; AT3G44200.
DR KEGG; ath:AT3G44200; -.
DR Araport; AT3G44200; -.
DR TAIR; locus:2081383; AT3G44200.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_000288_128_0_1; -.
DR InParanoid; Q0WPH8; -.
DR OMA; CHIHATS; -.
DR OrthoDB; 219308at2759; -.
DR PhylomeDB; Q0WPH8; -.
DR PRO; PR:Q0WPH8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WPH8; baseline and differential.
DR Genevisible; Q0WPH8; AT.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0007017; P:microtubule-based process; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..956
FT /note="Serine/threonine-protein kinase Nek5"
FT /id="PRO_0000314041"
FT DOMAIN 8..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 276..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 347
FT /note="A -> T (in Ref. 1; BAF95588)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="V -> I (in Ref. 1; BAF95588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106390 MW; 7102CA855C683976 CRC64;
MESRMDQYEL MEQIGRGAFG AAILVHHKAE RKKYVLKKIR LARQTERCRR SAHQEMSLIA
RVQHPYIVEF KEAWVEKGCY VCIVTGYCEG GDMAELMKKS NGVYFPEEKL CKWFTQLLLA
VEYLHSNYVL HRDLKCSNIF LTKDQDVRLG DFGLAKTLKA DDLTSSVVGT PNYMCPELLA
DIPYGFKSDI WSLGCCIYEM AAYRPAFKAF DMAGLISKVN RSSIGPLPPC YSPSLKALIK
GMLRKNPEYR PNASEILKHP YLQPYVEQYR PTLSAASITP EKPLNSREGR RSMAESQNSN
SSSEKDNFYV SDKNIRYVVP SNGNKVTETD SGFVDDEDIL DHVQQSAENG NLQSVSATKP
DGHGILKPVH SDQRPDVIQP RHPKTIRNIM MVLKEEKARE NGSPMRSNRS RPSSVPTQKN
NVETPSKIPK LGDIAHSSKT NASTPIPPSK LASDSARTPG SFPPKHHMPV IDSSPKLKPR
NDRISPSPAA KHEAEEAMSV KRRQRTPPTL PRRTSLIAHQ SRQLGADISN MAAKETAKLH
PSVPSESETN SHQSRVHASP VSTTPEPKRT SVGSAKGMQS ESSNSISSSL SMQAFELCDD
ASTPYIDMTE HTTPDDHRRS CHSEYSYSFP DISSEMMIRR DEHSTSMRLT EIPDSVSGVQ
NTIAHHQPER EQGSCPTVLK DDSPATLQSY EPNTSQHQHG DDKFTVKEFV SSVPGPAPLP
LHVEPSHQVN SHSDNKTSVM SQNSALEKNN SHSHPHPVVD DVIHVIRHSS FRVGSDQPVM
ESVEVGVQNV DMGKLINVVR DEMEVRKGAT PSESPTTRSI ISEPDSRTEP RPKEPDPITN
YSETKSFNSC SDSSPAETRT NSFVPEEETT PTPPVKETLD IKSFRQRAEA LEGLLELSAD
LLEQSRLEEL AIVLQPFGKN KVSPRETAIW LAKSLKGMMI EDINNNNSSG SSRNCS
