PE191_ARATH
ID PE191_ARATH Reviewed; 248 AA.
AC Q9SRQ3; Q680B5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Peroxisome biogenesis protein 19-1 {ECO:0000303|PubMed:16923726};
DE AltName: Full=Peroxin-19-1 {ECO:0000303|PubMed:16923726};
DE Short=AtPEX19-1 {ECO:0000303|PubMed:16923726};
DE AltName: Full=Peroxisomal membrane protein import receptor PEX19-1 {ECO:0000303|PubMed:16923726};
DE Flags: Precursor;
GN Name=PEX19-1 {ECO:0000303|PubMed:16923726};
GN OrderedLocusNames=At3g03490 {ECO:0000312|Araport:AT3G03490};
GN ORFNames=T21P5.9 {ECO:0000312|EMBL:AAF01586.1};
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, SUBUNIT, AND INTERACTION WITH PEX10.
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 [2]
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 [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].
RA Shinn P., Chen H., Cheuk R., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 146-248.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH APEM9.
RX PubMed=21487094; DOI=10.1105/tpc.110.080770;
RA Goto S., Mano S., Nakamori C., Nishimura M.;
RT "Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the
RT PEX1-PEX6 complex to peroxisomes.";
RL Plant Cell 23:1573-1587(2011).
CC -!- FUNCTION: Contributes to morphology determination of peroxisomes, but
CC not to import of peroxisomal matrix proteins (PubMed:16923726,
CC PubMed:17478547). Required for proper post-translational import and
CC stabilization of peroxisomal membrane proteins (PMPs) (PubMed:16923726,
CC PubMed:17478547). Acts as a cytosolic import receptor for PMPs and
CC delivers them to the docking factor PEX3 at the peroxisomal membrane
CC for subsequent insertion into the membrane (PubMed:17478547). Required
CC for transport of APEM9 to peroxisome membranes (PubMed:21487094). Acts
CC as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer
CC (PubMed:17478547). {ECO:0000269|PubMed:16923726,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:21487094}.
CC -!- SUBUNIT: Dimer (PubMed:16923726). Interacts with PEX10 (via C-terminus)
CC (PubMed:16923726). Interacts with APEM9 (PubMed:21487094).
CC {ECO:0000269|PubMed:16923726, ECO:0000269|PubMed:21487094}.
CC -!- INTERACTION:
CC Q9SRQ3; Q94FB9: ABCD1; NbExp=2; IntAct=EBI-1151789, EBI-7933055;
CC Q9SRQ3; Q9SYU4: PEX10; NbExp=2; IntAct=EBI-1151789, EBI-1151983;
CC Q9SRQ3; Q9SRQ3: PEX19-1; NbExp=2; IntAct=EBI-1151789, EBI-1151789;
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 stems and flowers.
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, PEX19-1 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}.
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DR EMBL; AJ564199; CAD91898.1; -; mRNA.
DR EMBL; AC009895; AAF01586.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73950.1; -; Genomic_DNA.
DR EMBL; BT012633; AAT06452.1; -; mRNA.
DR EMBL; AK175952; BAD43715.1; -; mRNA.
DR RefSeq; NP_186999.1; NM_111220.4.
DR AlphaFoldDB; Q9SRQ3; -.
DR SMR; Q9SRQ3; -.
DR BioGRID; 6581; 3.
DR IntAct; Q9SRQ3; 2.
DR MINT; Q9SRQ3; -.
DR STRING; 3702.AT3G03490.1; -.
DR iPTMnet; Q9SRQ3; -.
DR PaxDb; Q9SRQ3; -.
DR PRIDE; Q9SRQ3; -.
DR ProteomicsDB; 236409; -.
DR EnsemblPlants; AT3G03490.1; AT3G03490.1; AT3G03490.
DR GeneID; 821248; -.
DR Gramene; AT3G03490.1; AT3G03490.1; AT3G03490.
DR KEGG; ath:AT3G03490; -.
DR Araport; AT3G03490; -.
DR TAIR; locus:2099694; AT3G03490.
DR eggNOG; KOG3133; Eukaryota.
DR HOGENOM; CLU_043063_4_0_1; -.
DR InParanoid; Q9SRQ3; -.
DR OMA; PQNSHND; -.
DR OrthoDB; 1282367at2759; -.
DR PhylomeDB; Q9SRQ3; -.
DR PRO; PR:Q9SRQ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRQ3; baseline and differential.
DR Genevisible; Q9SRQ3; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 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 Coiled coil; Cytoplasm; Lipoprotein; Membrane; Methylation; Peroxisome;
KW Peroxisome biogenesis; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..245
FT /note="Peroxisome biogenesis protein 19-1"
FT /id="PRO_0000404530"
FT PROPEP 246..248
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000404531"
FT REGION 22..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..49
FT /evidence="ECO:0000255"
FT COMPBIAS 22..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 245
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 224
FT /note="P -> H (in Ref. 5; BAD43715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28289 MW; 90A873E635361140 CRC64;
MANSHTDDLD ELLDSALDDF KDLNLSHQRN QREAQEEEEK KRKEETVLLP SGVQGLGMGL
PDMRSKKRGK QKVSKEDHVA EALDKLREQT RETVKGLESI SSKQLPASDD DGMVEDFLKQ
FEDLAGSKDL ESIVETMMQQ LLSKDILHEP MKELGARYPK WLKENEASLS KEDYKRYSQQ
YKLIEELNAV YENEPNNSSK IMEIMQKMQE CGQPPSDIVK EIDPGFDFAS LGQISPEMLE
SSPNCCIM
