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KAKU4_ARATH
ID   KAKU4_ARATH             Reviewed;         485 AA.
AC   Q949W6; F4JS05; O49592;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Protein KAKU4 {ECO:0000303|PubMed:24824484};
GN   Name=KAKU4 {ECO:0000303|PubMed:24824484};
GN   OrderedLocusNames=At4g31430 {ECO:0000312|Araport:AT4G31430};
GN   ORFNames=F3L17.8 {ECO:0000312|EMBL:CAB79861.1},
GN   F8F16 {ECO:0000312|EMBL:CAA16546.1};
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 {ECO:0000312|EMBL:AAK92781.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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] (ISOFORM 1).
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   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CRWN1 AND CRWN4,
RP   SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX   PubMed=24824484; DOI=10.1105/tpc.113.122168;
RA   Goto C., Tamura K., Fukao Y., Shimada T., Hara-Nishimura I.;
RT   "The novel nuclear envelope protein KAKU4 modulates nuclear morphology in
RT   Arabidopsis.";
RL   Plant Cell 26:2143-2155(2014).
CC   -!- FUNCTION: Required for nucleus structure organization (e.g. size and
CC       shape). {ECO:0000269|PubMed:24824484}.
CC   -!- SUBUNIT: Core component of the LINC complex which is composed of inner
CC       nuclear membrane SUN domain-containing proteins coupled to outer
CC       nuclear membrane WIP proteins, the nucleoskeletal CRWN/LINC proteins,
CC       and, possibly, KAKU4. Interacts with CRWN1 and CRWN4.
CC       {ECO:0000269|PubMed:24824484}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000269|PubMed:24824484}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=KAKU4.1 {ECO:0000303|PubMed:24824484}, KAKU4.3
CC       {ECO:0000303|PubMed:24824484};
CC         IsoId=Q949W6-1; Sequence=Displayed;
CC       Name=2; Synonyms=KAKU4.2 {ECO:0000303|PubMed:24824484};
CC         IsoId=Q949W6-2; Sequence=VSP_057576;
CC   -!- DISRUPTION PHENOTYPE: Aberrant nuclear morphology.
CC       {ECO:0000269|PubMed:24824484}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA16546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL021633; CAA16546.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161579; CAB79861.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85910.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85911.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85912.1; -; Genomic_DNA.
DR   EMBL; AY050846; AAK92781.1; -; mRNA.
DR   EMBL; AY142592; AAN13161.1; -; mRNA.
DR   PIR; T04510; T04510.
DR   RefSeq; NP_001031764.1; NM_001036687.1. [Q949W6-1]
DR   RefSeq; NP_567876.1; NM_119292.1. [Q949W6-1]
DR   RefSeq; NP_974653.1; NM_202924.2. [Q949W6-2]
DR   AlphaFoldDB; Q949W6; -.
DR   IntAct; Q949W6; 6.
DR   STRING; 3702.AT4G31430.2; -.
DR   iPTMnet; Q949W6; -.
DR   PaxDb; Q949W6; -.
DR   PRIDE; Q949W6; -.
DR   ProteomicsDB; 250611; -. [Q949W6-1]
DR   EnsemblPlants; AT4G31430.1; AT4G31430.1; AT4G31430. [Q949W6-1]
DR   EnsemblPlants; AT4G31430.2; AT4G31430.2; AT4G31430. [Q949W6-2]
DR   EnsemblPlants; AT4G31430.3; AT4G31430.3; AT4G31430. [Q949W6-1]
DR   GeneID; 829270; -.
DR   Gramene; AT4G31430.1; AT4G31430.1; AT4G31430. [Q949W6-1]
DR   Gramene; AT4G31430.2; AT4G31430.2; AT4G31430. [Q949W6-2]
DR   Gramene; AT4G31430.3; AT4G31430.3; AT4G31430. [Q949W6-1]
DR   KEGG; ath:AT4G31430; -.
DR   Araport; AT4G31430; -.
DR   TAIR; locus:2128176; AT4G31430.
DR   eggNOG; ENOG502QPXJ; Eukaryota.
DR   OMA; EIHGDDM; -.
DR   OrthoDB; 507535at2759; -.
DR   PRO; PR:Q949W6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q949W6; baseline and differential.
DR   Genevisible; Q949W6; AT.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0071763; P:nuclear membrane organization; IMP:TAIR.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Membrane; Nucleus; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Protein KAKU4"
FT                   /id="PRO_0000432818"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           22..25
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000303|PubMed:24824484"
FT   COMPBIAS        80..103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         465..485
FT                   /note="GYGRSTKTHTTRRNQGFSAYS -> SPAVMEGQPKPTPPEETKASQPIAEIH
FT                   GDDMTVGNGSDGAINNESNDSHSSASNSSSTHEEEWLPGDQSLPNSNSASSSPGNTKVL
FT                   AYSRRGRGRGRGRGRGGRGKGRAK (in isoform 2)"
FT                   /id="VSP_057576"
SQ   SEQUENCE   485 AA;  52148 MW;  A7FD825621BD35E5 CRC64;
     MDSVSGYAAG AGQPRVGGKI VRPRRTAVVR TPCERPVQRS RDPPQQNPSW ISRLVYKPAS
     VIASGAGKFI SSVVFSDSSS SSEEDEDSSS DIDGDEDVEK NNPDFTEEDL LSAQQPSIQR
     LSSKRVIEQL LLQETFAREE GDRLIDIIKA RVVDHPSVPS AIETSHDDYG LTSDVNVGEM
     SNTAVMEARK WLEEKKSGSS SKYKATEDGA GSPVDVAKSY MRARLPWGSP AANNLDFRSP
     SSARVQGTPL PYSAGNFSSS KLKRKSGSNQ SWNIQDEIRK VRAKATEEML KSPSSVASLE
     PKYSPYVLAT DMLKGNASSL NADGAVRNEQ SRALPNSAIP TSEHNQTTEA NQAVKETGVL
     HTRSRGVGLE ETFISTQGVK PSEDTNTAPQ SGTAVDDFND QDGDFIQPTS TIGNTTNAVL
     ALGATLDPTG NSCIPKDVFE TSKEADEIGA SRHTSNGFPS SSPSGYGRST KTHTTRRNQG
     FSAYS
 
 
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