PEX12_ARATH
ID PEX12_ARATH Reviewed; 393 AA.
AC Q9M841; Q8GYG2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peroxisome biogenesis protein 12;
DE AltName: Full=Peroxin-12;
DE Short=AtPEX12;
DE AltName: Full=Pex12p;
DE AltName: Full=Protein ABERRANT PEROXISOME MORPHOLOGY 4;
GN Name=PEX12; Synonyms=APM4; OrderedLocusNames=At3g04460; ORFNames=T27C4.11;
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=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 [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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 92-393.
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16113209; DOI=10.1104/pp.105.066811;
RA Fan J., Quan S., Orth T., Awai C., Chory J., Hu J.;
RT "The Arabidopsis PEX12 gene is required for peroxisome biogenesis and is
RT essential for development.";
RL Plant Physiol. 139:231-239(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-170.
RX PubMed=16813573; DOI=10.1111/j.1365-313x.2006.02809.x;
RA Mano S., Nakamori C., Nito K., Kondo M., Nishimura M.;
RT "The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and
RT PTS2-dependent protein transport to peroxisomes.";
RL Plant J. 47:604-618(2006).
RN [7]
RP FUNCTION.
RX PubMed=17478547; DOI=10.1093/pcp/pcm053;
RA Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.;
RT "Functional classification of Arabidopsis peroxisome biogenesis factors
RT proposed from analyses of knockdown mutants.";
RL Plant Cell Physiol. 48:763-774(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH PEX7.
RX PubMed=19594707; DOI=10.1111/j.1365-313x.2009.03970.x;
RA Singh T., Hayashi M., Mano S., Arai Y., Goto S., Nishimura M.;
RT "Molecular components required for the targeting of PEX7 to peroxisomes in
RT Arabidopsis thaliana.";
RL Plant J. 60:488-498(2009).
RN [9]
RP FUNCTION.
RX PubMed=20679226; DOI=10.1073/pnas.1009174107;
RA Prestele J., Hierl G., Scherling C., Hetkamp S., Schwechheimer C.,
RA Isono E., Weckwerth W., Wanner G., Gietl C.;
RT "Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2,
RT and PEX12 in peroxisome formation and matrix protein import.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14915-14920(2010).
RN [10]
RP INTERACTION WITH DSK2A AND DSK2B, AND FUNCTION.
RX PubMed=23336935; DOI=10.1111/jipb.12014;
RA Kaur N., Zhao Q., Xie Q., Hu J.;
RT "Arabidopsis RING peroxins are E3 ubiquitin ligases that interact with two
RT homologous ubiquitin receptor proteins(F).";
RL J. Integr. Plant Biol. 55:108-120(2013).
CC -!- FUNCTION: Required for peroxisome biogenesis and for PTS1- and PTS2-
CC dependent protein import into peroxisomes. Essential for the
CC peroxisomal targeting of PEX7. Required for the export/release of
CC receptors on the peroxisome membrane. Acts as an E3 ubiquitin-protein
CC ligase involved in monoubiquitination of PEX5.
CC {ECO:0000269|PubMed:16113209, ECO:0000269|PubMed:16813573,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:19594707,
CC ECO:0000269|PubMed:20679226, ECO:0000269|PubMed:23336935}.
CC -!- SUBUNIT: Interacts (via C-terminus) with PEX7. Interacts with DSK2a and
CC DSK2b. {ECO:0000269|PubMed:19594707, ECO:0000269|PubMed:23336935}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, roots, leaves, seeds
CC and flowers. {ECO:0000269|PubMed:16113209}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at the heart stage.
CC {ECO:0000269|PubMed:16113209}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42305.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BX824646; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC022287; AAF63777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74085.1; -; Genomic_DNA.
DR EMBL; BX824646; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK117651; BAC42305.1; ALT_INIT; mRNA.
DR RefSeq; NP_187096.2; NM_111317.4.
DR AlphaFoldDB; Q9M841; -.
DR SMR; Q9M841; -.
DR BioGRID; 4937; 2.
DR IntAct; Q9M841; 7.
DR STRING; 3702.AT3G04460.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR PaxDb; Q9M841; -.
DR PRIDE; Q9M841; -.
DR ProteomicsDB; 236429; -.
DR EnsemblPlants; AT3G04460.1; AT3G04460.1; AT3G04460.
DR GeneID; 819602; -.
DR Gramene; AT3G04460.1; AT3G04460.1; AT3G04460.
DR KEGG; ath:AT3G04460; -.
DR Araport; AT3G04460; -.
DR TAIR; locus:2100890; AT3G04460.
DR eggNOG; KOG0826; Eukaryota.
DR HOGENOM; CLU_031067_1_1_1; -.
DR InParanoid; Q9M841; -.
DR OMA; NPAIIET; -.
DR PhylomeDB; Q9M841; -.
DR PRO; PR:Q9M841; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M841; baseline and differential.
DR Genevisible; Q9M841; AT.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IBA:GO_Central.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:TAIR.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017375; PEX12.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12888; PTHR12888; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR PIRSF; PIRSF038074; Peroxisome_assembly_p12; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="Peroxisome biogenesis protein 12"
FT /id="PRO_0000218615"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 339..378
FT /note="RING-type; degenerate"
FT MUTAGEN 170
FT /note="R->K: In apm4; reduced protein transport to
FT peroxisome and repressed plant growth."
FT /evidence="ECO:0000269|PubMed:16813573"
FT CONFLICT 96
FT /note="A -> S (in Ref. 3; BX824646)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="D -> E (in Ref. 3; BX824646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44400 MW; BEF9C580A93F52A7 CRC64;
MLFQVGGEGT RPTFFEMAAA QQLPASLRAA LTYSLGVFAL RRSFLHKILD YEDEFFAALM
LILEGHSLRT TDGSFAESLY GLRRKSARLR LRKDSARKDS SEEVQHSGLE KRQRILSVVF
LVVLPYFKSK LHAIYNKERE ARLRESLWGA EDQGFDEADF FTGDDSIVSR EPSGNEELSV
RVQLATKIKK FIAVCYPWIH ASSEGLSFTY QLLYLLDATG FYSLGLQALG IQVCRATGQE
LMDTSSRISK IRNHERERLR GPPWLKTVQG ALLSCSYAVL DYAQTGLIAA VFIFKMMEWW
YQSAEERLSA PTVYPPPPPP PAPKMAKEGI PLPPDRSLCA LCLQKRANPS VVTVSGFVFC
YSCVFKYVSK YKRCPVTLIP ASVDQIRRLF QDT
