CD48E_ARATH
ID CD48E_ARATH Reviewed; 810 AA.
AC Q9LZF6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cell division control protein 48 homolog E;
DE Short=AtCDC48e;
DE AltName: Full=Transitional endoplasmic reticulum ATPase E;
GN Name=CDC48E; OrderedLocusNames=At5g03340; ORFNames=F12E4_70;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
CC -!- FUNCTION: Probably functions in cell division and growth processes.
CC Interacts with certain SNAREs as part of specialized membrane fusion
CC events where vesicles from the same organelle fuse (homotypic fusion)
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC phragmoplast {ECO:0000250}. Note=Primarily localized to the nucleus
CC and, during cytokinesis, to the phragmoplast, a site where membrane
CC vesicles are targeted in the deposition of new cell wall materials.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB83290.1; 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; AL162751; CAB83290.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90587.1; -; Genomic_DNA.
DR EMBL; AK117125; BAC41803.1; -; mRNA.
DR EMBL; AK118571; BAC43171.1; -; mRNA.
DR EMBL; BT006485; AAP21293.1; -; mRNA.
DR RefSeq; NP_568114.1; NM_120412.3.
DR AlphaFoldDB; Q9LZF6; -.
DR SMR; Q9LZF6; -.
DR BioGRID; 17146; 66.
DR IntAct; Q9LZF6; 1.
DR STRING; 3702.AT5G03340.1; -.
DR iPTMnet; Q9LZF6; -.
DR PaxDb; Q9LZF6; -.
DR PRIDE; Q9LZF6; -.
DR ProteomicsDB; 223939; -.
DR EnsemblPlants; AT5G03340.1; AT5G03340.1; AT5G03340.
DR GeneID; 831870; -.
DR Gramene; AT5G03340.1; AT5G03340.1; AT5G03340.
DR KEGG; ath:AT5G03340; -.
DR Araport; AT5G03340; -.
DR TAIR; locus:2831844; AT5G03340.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; Q9LZF6; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q9LZF6; -.
DR PRO; PR:Q9LZF6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZF6; baseline and differential.
DR Genevisible; Q9LZF6; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P54609"
FT CHAIN 2..810
FT /note="Cell division control protein 48 homolog E"
FT /id="PRO_0000084583"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 521..528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P54609"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54609"
SQ SEQUENCE 810 AA; 89958 MW; 1E8D08C6C5FA5F68 CRC64;
MSNEPESSDS KTKKDFSTAI LERKKSPNRL VVDEAINDDN SVVSLHPTTM EKLQLFRGDT
ILIKGKKRKD TVCIALADET CEEPKIRMNK VVRSNLRVRL GDVISVHQCP DVKYGKRVHI
LPVDDTVEGV TGNLFDAYLK PYFLEAYRPV RKGDLFLVRG GMRSVEFKVI ETDPAEYCVV
APDTEIFCEG EPVKREDEER LDEVGYDDVG GVRKQMAQIR ELVELPLRHP QLFKSIGVKP
PKGILLYGPP GSGKTLIARA VANETGAFFF CINGPEIMSK LAGESESNLR KAFEEAEKNA
PSIIFIDEID SIAPKREKTN GEVERRIVSQ LLTLMDGLKS RAHVIVMGAT NRPNSIDPAL
RRFGRFDREI DIGVPDEIGR LEVLRIHTKN MKLAEDVDLE RISKDTHGYV GADLAALCTE
AALQCIREKM DVIDLEDDSI DAEILNSMAV SNEHFHTALG NSNPSALRET VVEVPNVSWE
DIGGLENVKR ELQETVQYPV EHPEKFEKFG MSPSKGVLFY GPPGCGKTLL AKAIANECQA
NFISVKGPEL LTMWFGESEA NVREIFDKAR QSAPCVLFFD ELDSIATQRG NSAGDAGGAA
DRVLNQLLTE MDGMNAKKTV FIIGATNRPD IIDSALLRPG RLDQLIYIPL PDEDSRLNIF
KACLRKSPVA KDVDVTALAK YTQGFSGADI TEICQRACKY AIRENIEKDI ENERRRSQNP
EAMEEDMVDD EVSEIRAAHF EESMKYARRS VSDADIRKYQ AFAQTLQQSR GFGSEFRFDS
TAGVGRTTGV AAADPFATSA AAADDDDLYS
