PE192_ARATH
ID PE192_ARATH Reviewed; 245 AA.
AC Q94EI3; Q9LF69;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Peroxisome biogenesis protein 19-2;
DE AltName: Full=Peroxin-19-2;
DE Short=AtPEX19-2;
DE AltName: Full=Peroxisomal membrane protein import receptor PEX19-2;
DE Flags: Precursor;
GN Name=PEX19-2; OrderedLocusNames=At5g17550; ORFNames=K10A8.30;
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=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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16923726; DOI=10.1080/09687860600738221;
RA Hadden D.A., Phillipson B.A., Johnston K.A., Brown L.A., Manfield I.W.,
RA El-Shami M., Sparkes I.A., Baker A.;
RT "Arabidopsis PEX19 is a dimeric protein that binds the peroxin PEX10.";
RL Mol. Membr. Biol. 23:325-336(2006).
RN [5]
RP FUNCTION, AND IDENTIFICATION.
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).
CC -!- FUNCTION: Contributes to morphology determination of peroxisomes, but
CC not to import of peroxisomal matrix proteins. Required for proper post-
CC translational import and stabilization of peroxisomal membrane proteins
CC (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them
CC to the docking factor PEX3 at the peroxisomal membrane for subsequent
CC insertion into the membrane. Acts as a chaperone in stabilizing or
CC maintaining PMPs in the lipid bilayer. {ECO:0000269|PubMed:16923726,
CC ECO:0000269|PubMed:17478547}.
CC -!- SUBUNIT: Dimer. Interacts with PEX10 (via C-terminus) (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q94EI3; Q94FB9: ABCD1; NbExp=2; IntAct=EBI-7933092, EBI-7933055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16923726}.
CC Peroxisome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, siliques and
CC stems. Highest expression in roots and leaves.
CC {ECO:0000269|PubMed:16923726}.
CC -!- PTM: May be farnesylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
CC -!- CAUTION: Like its mammalian and yeast counterparts, PEX19-2 might be
CC farnesylated and interacting transiently with the peroxisome membrane.
CC However, this post-translational modification has not been demonstrated
CC and only a trace of PEX19 was found associated with the peroxisome
CC (PubMed:16923726). {ECO:0000305|PubMed:16923726}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01899.1; 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; AL391151; CAC01899.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92442.1; -; Genomic_DNA.
DR EMBL; AF410297; AAK95283.1; -; mRNA.
DR EMBL; AY149931; AAN31085.1; -; mRNA.
DR PIR; T51459; T51459.
DR RefSeq; NP_568351.1; NM_121761.3.
DR AlphaFoldDB; Q94EI3; -.
DR SMR; Q94EI3; -.
DR BioGRID; 16897; 1.
DR IntAct; Q94EI3; 1.
DR MINT; Q94EI3; -.
DR STRING; 3702.AT5G17550.1; -.
DR iPTMnet; Q94EI3; -.
DR PaxDb; Q94EI3; -.
DR PRIDE; Q94EI3; -.
DR ProteomicsDB; 236807; -.
DR EnsemblPlants; AT5G17550.1; AT5G17550.1; AT5G17550.
DR GeneID; 831621; -.
DR Gramene; AT5G17550.1; AT5G17550.1; AT5G17550.
DR KEGG; ath:AT5G17550; -.
DR Araport; AT5G17550; -.
DR TAIR; locus:2151386; AT5G17550.
DR eggNOG; KOG3133; Eukaryota.
DR HOGENOM; CLU_043063_4_0_1; -.
DR InParanoid; Q94EI3; -.
DR OMA; DPMMEDW; -.
DR OrthoDB; 1282367at2759; -.
DR PhylomeDB; Q94EI3; -.
DR PRO; PR:Q94EI3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94EI3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IBA:GO_Central.
DR GO; GO:0006625; P:protein targeting to peroxisome; IGI:TAIR.
DR Gene3D; 1.20.120.900; -; 1.
DR InterPro; IPR006708; Pex19.
DR InterPro; IPR038322; Pex19_C_sf.
DR PANTHER; PTHR12774; PTHR12774; 1.
DR Pfam; PF04614; Pex19; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipoprotein; Membrane; Methylation; Peroxisome;
KW Peroxisome biogenesis; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..242
FT /note="Peroxisome biogenesis protein 19-2"
FT /id="PRO_0000404532"
FT PROPEP 243..245
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000404533"
FT REGION 17..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 242
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 27841 MW; DB132D99422D78D1 CRC64;
MANDTHTDDL DELLDSALDD FKDLNLTQRN GGVKKEEGDK KETESLPSGV QGLGMGLPDM
RSKKKGKKKI AKEDHVTEAL DKLREQTRET VKGLESLSSK QQPTGSDDAM VEDWIKQFEN
LTGSNDLESI VDTMMQQLLS KDILHEPMKE IGARYPKWLE EHESSLNKEE FDRYSRQYEL
IKELNLVYEN EPNNSTKIME IMQKMQECGQ PPSDIVQEMD PGFDFASLGQ MSPDMLESSP
NCCVM
