PMP22_ARATH
ID PMP22_ARATH Reviewed; 190 AA.
AC Q9ZS51;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Peroxisomal membrane protein PMP22;
DE AltName: Full=22 kDa peroxisomal membrane protein;
GN Name=PMP22; OrderedLocusNames=At4g04470; ORFNames=T26N6.9;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10318708; DOI=10.1104/pp.120.1.309;
RA Tugal H.B., Pool M., Baker A.;
RT "Arabidopsis 22-kilodalton peroxisomal membrane protein. Nucleotide
RT sequence analysis and biochemical characterization.";
RL Plant Physiol. 120:309-320(1999).
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, TOPOLOGY, AND MUTAGENESIS OF 7-LYS-LYS-8;
RP 14-TYR--LEU-18; 22-PRO--LYS-26; 49-LYS--ARG-54; 82-LYS--LYS-85 AND
RP 92-LYS-LYS-93.
RX PubMed=12972647; DOI=10.1104/pp.103.027870;
RA Murphy M.A., Phillipson B.A., Baker A., Mullen R.T.;
RT "Characterization of the targeting signal of the Arabidopsis 22-kD integral
RT peroxisomal membrane protein.";
RL Plant Physiol. 133:813-828(2003).
CC -!- FUNCTION: May be involved in the metabolism of reactive oxygen species.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10318708,
CC ECO:0000269|PubMed:12972647}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10318708, ECO:0000269|PubMed:12972647}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, higher levels in flowers
CC and green siliques (at protein level). {ECO:0000269|PubMed:10318708}.
CC -!- DEVELOPMENTAL STAGE: Accumulates after seeds imbibition (at protein
CC level). {ECO:0000269|PubMed:10318708}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000305}.
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DR EMBL; AJ006053; CAA06834.1; -; mRNA.
DR EMBL; AF076243; AAD29759.1; -; Genomic_DNA.
DR EMBL; AL161500; CAB77915.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82392.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67056.1; -; Genomic_DNA.
DR EMBL; BT003055; AAO23620.1; -; mRNA.
DR PIR; T51590; T51590.
DR RefSeq; NP_001319865.1; NM_001340483.1.
DR RefSeq; NP_192356.1; NM_116685.5.
DR AlphaFoldDB; Q9ZS51; -.
DR SMR; Q9ZS51; -.
DR STRING; 3702.AT4G04470.1; -.
DR PaxDb; Q9ZS51; -.
DR PRIDE; Q9ZS51; -.
DR ProteomicsDB; 226212; -.
DR EnsemblPlants; AT4G04470.1; AT4G04470.1; AT4G04470.
DR EnsemblPlants; AT4G04470.2; AT4G04470.2; AT4G04470.
DR GeneID; 825777; -.
DR Gramene; AT4G04470.1; AT4G04470.1; AT4G04470.
DR Gramene; AT4G04470.2; AT4G04470.2; AT4G04470.
DR KEGG; ath:AT4G04470; -.
DR Araport; AT4G04470; -.
DR TAIR; locus:2137124; AT4G04470.
DR eggNOG; KOG1944; Eukaryota.
DR HOGENOM; CLU_049109_9_0_1; -.
DR InParanoid; Q9ZS51; -.
DR OMA; RDPGYEK; -.
DR OrthoDB; 1324608at2759; -.
DR PhylomeDB; Q9ZS51; -.
DR PRO; PR:Q9ZS51; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZS51; baseline and differential.
DR Genevisible; Q9ZS51; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007248; Mpv17_PMP22.
DR PANTHER; PTHR11266; PTHR11266; 1.
DR Pfam; PF04117; Mpv17_PMP22; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..190
FT /note="Peroxisomal membrane protein PMP22"
FT /id="PRO_0000218935"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..96
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..154
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 7..8
FT /note="KK->GG: Impaired in targeting to peroxisomes.
FT Localized in endoplasmic reticulum instead of peroxisome;
FT when associated with 14-GLSQG-18; 22-GLRTG-26, 49-GIQLGG-54
FT and 82-GGGG-85."
FT /evidence="ECO:0000269|PubMed:12972647"
FT MUTAGEN 14..18
FT /note="YLSQL->GLSQG: Impaired in targeting to peroxisomes.
FT Localized in endoplasmic reticulum instead of peroxisome;
FT when associated with 7-GG-8; 22-GLRTG-26; 49-GIQLGG-54 and
FT 82-GGGG-85."
FT /evidence="ECO:0000269|PubMed:12972647"
FT MUTAGEN 22..26
FT /note="PLRTK->GLRTG: Impaired in targeting to peroxisomes.
FT Localized in endoplasmic reticulum instead of peroxisome;
FT when associated with 7-GG-8; 14-GLSQG-18; 49-GIQLGG-54 and
FT 82-GGGG-85."
FT /evidence="ECO:0000269|PubMed:12972647"
FT MUTAGEN 49..54
FT /note="KIQLRR->GIQLGG: Impaired in targeting to
FT peroxisomes. Localized in endoplasmic reticulum instead of
FT peroxisome; when associated with 7-GG-8; 14-GLSQG-18; 22-
FT GLRTG-26 and 82-GGGG-85."
FT /evidence="ECO:0000269|PubMed:12972647"
FT MUTAGEN 82..85
FT /note="KGKK->GGGG: Impaired in targeting to peroxisomes.
FT Localized in endoplasmic reticulum instead of peroxisome;
FT when associated with 7-GG-8; 14-GLSQG-18; 22-GLRTG-26 and
FT 49-GIQLGG-54."
FT /evidence="ECO:0000269|PubMed:12972647"
FT MUTAGEN 92..93
FT /note="KK->GG: No effect on targeting to peroxisomes."
FT /evidence="ECO:0000269|PubMed:12972647"
SQ SEQUENCE 190 AA; 21719 MW; BB9121A97051129C CRC64;
MGSSPPKKTT LQRYLSQLQQ HPLRTKAITA GVLSGVSDVV SQKLSGIQKI QLRRVLLKVI
FAGGFLGPAG HFFHTYLDKF FKGKKDTQTV AKKVILEQLT LSPLNHLLFM IYYGVVIERT
PWTLVRERIK KTYPTVQLTA WTFFPVVGWI NYKYVPLHFR VILHSLVAFF WGIFLTLRAR
SMTLALAKAK
