SECE1_ARATH
ID SECE1_ARATH Reviewed; 177 AA.
AC O23342;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Preprotein translocase subunit SECE1;
DE Flags: Precursor;
GN Name=SECE1; OrderedLocusNames=At4g14870; ORFNames=dl3475w, FCAALL.408;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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 SUBCELLULAR LOCATION, AND INTERACTION WITH SCY1.
RX PubMed=10207046; DOI=10.1074/jbc.274.17.12177;
RA Schuenemann D., Amin P., Hartmann E., Hoffman N.E.;
RT "Chloroplast SecY is complexed to SecE and involved in the translocation of
RT the 33-kDa but not the 23-kDa subunit of the oxygen-evolving complex.";
RL J. Biol. Chem. 274:12177-12182(1999).
RN [6]
RP FUNCTION.
RX PubMed=11389897; DOI=10.1016/s0014-5793(01)02494-2;
RA Froderberg L., Rohl T., van Wijk K.J., de Gier J.W.;
RT "Complementation of bacterial SecE by a chloroplastic homologue.";
RL FEBS Lett. 498:52-56(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12054533; DOI=10.1016/s0006-291x(02)00285-1;
RA Steiner J.M., Kocher T., Nagy C., Loffelhardt W.;
RT "Chloroplast SecE: evidence for spontaneous insertion into the thylakoid
RT membrane.";
RL Biochem. Biophys. Res. Commun. 293:747-752(2002).
RN [8]
RP INTERACTION WITH SCY1 AND ALB3.
RX PubMed=15988575; DOI=10.1007/s00253-005-0029-3;
RA Pasch J.C., Nickelsen J., Schunemann D.;
RT "The yeast split-ubiquitin system to study chloroplast membrane protein
RT interactions.";
RL Appl. Microbiol. Biotechnol. 69:440-447(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21051552; DOI=10.1104/pp.110.166546;
RA Skalitzky C.A., Martin J.R., Harwood J.H., Beirne J.J., Adamczyk B.J.,
RA Heck G.R., Cline K., Fernandez D.E.;
RT "Plastids contain a second sec translocase system with essential
RT functions.";
RL Plant Physiol. 155:354-369(2011).
CC -!- FUNCTION: Involved in the import/insertion pathway in the thylakoids.
CC The signal recognition particle is not involved in the insertion of
CC SECE1 in the thylakoid membrane. {ECO:0000269|PubMed:11389897,
CC ECO:0000269|PubMed:21051552}.
CC -!- SUBUNIT: Part of the Sec protein translocation apparatus. Interacts
CC with SCY1 and ALB3. {ECO:0000269|PubMed:10207046,
CC ECO:0000269|PubMed:15988575}.
CC -!- INTERACTION:
CC O23342; Q38885: SCY1; NbExp=3; IntAct=EBI-1806811, EBI-1806802;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10207046, ECO:0000269|PubMed:12054533}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10207046,
CC ECO:0000269|PubMed:12054533}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal. Albino seedlings with yellow and
CC translucent (glassy) lateral organs when grown heterotrophically.
CC {ECO:0000269|PubMed:21051552}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000305}.
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DR EMBL; Z97337; CAB10266.1; -; Genomic_DNA.
DR EMBL; AL161540; CAB78529.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83511.1; -; Genomic_DNA.
DR EMBL; AY045827; AAK76501.1; -; mRNA.
DR EMBL; AY096484; AAM20124.1; -; mRNA.
DR PIR; H71411; H71411.
DR RefSeq; NP_567446.1; NM_117573.2.
DR AlphaFoldDB; O23342; -.
DR IntAct; O23342; 2.
DR STRING; 3702.AT4G14870.1; -.
DR TCDB; 3.A.5.4.2; the general secretory pathway (sec) family.
DR iPTMnet; O23342; -.
DR PaxDb; O23342; -.
DR PRIDE; O23342; -.
DR ProteomicsDB; 232926; -.
DR EnsemblPlants; AT4G14870.1; AT4G14870.1; AT4G14870.
DR GeneID; 827144; -.
DR Gramene; AT4G14870.1; AT4G14870.1; AT4G14870.
DR KEGG; ath:AT4G14870; -.
DR Araport; AT4G14870; -.
DR TAIR; locus:2130409; AT4G14870.
DR eggNOG; ENOG502S47G; Eukaryota.
DR HOGENOM; CLU_132876_0_0_1; -.
DR InParanoid; O23342; -.
DR OMA; QKEPDFW; -.
DR OrthoDB; 1598566at2759; -.
DR PhylomeDB; O23342; -.
DR PRO; PR:O23342; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23342; baseline and differential.
DR Genevisible; O23342; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR Gene3D; 1.20.5.1030; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR005807; SecE_bac.
DR InterPro; IPR038379; SecE_sf.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR Pfam; PF00584; SecE; 1.
DR TIGRFAMs; TIGR00964; secE_bact; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..177
FT /note="Preprotein translocase subunit SECE1"
FT /id="PRO_0000414226"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 60..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 19121 MW; 31401FAB30BBA8C8 CRC64;
MSLTAQFSPP VTGITRSLRD TKPSLSNLRV FPVYTEIRTM TTSNLRKSAC FVAKAIEQRR
DTAGSESESE ATPSPAEESG SGEDKEVEIS AIGAEIKAAM EQRKTAEEEK GKNEFLSGVA
EEVKEIEWPA FQKVLGTTGV VLGVIAGSSV VLLTVNFLLA ELSDRVFIGR GVQDFFS
