PEX13_ARATH
ID PEX13_ARATH Reviewed; 304 AA.
AC Q9SRR0; C0Z2M3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Peroxisomal membrane protein 13 {ECO:0000303|PubMed:16813573};
DE AltName: Full=ABSTINENCE BY MUTUAL CONSENT {ECO:0000303|PubMed:18160292};
DE AltName: Full=Peroxin-13 {ECO:0000303|PubMed:16813573};
DE Short=AtPEX13 {ECO:0000303|PubMed:16813573};
DE AltName: Full=Peroxisome biogenesis protein 13 {ECO:0000303|PubMed:16813573};
DE AltName: Full=Pex13p {ECO:0000303|PubMed:16813573};
DE AltName: Full=Protein ABERRANT PEROXISOME MORPHOLOGY 2 {ECO:0000303|PubMed:16813573};
DE AltName: Full=Protein AMC {ECO:0000303|PubMed:18160292};
GN Name=PEX13 {ECO:0000303|PubMed:16813573};
GN Synonyms=AMC {ECO:0000303|PubMed:18160292},
GN APM2 {ECO:0000303|PubMed:16813573};
GN OrderedLocusNames=At3g07560 {ECO:0000312|Araport:AT3G07560};
GN ORFNames=F21O3.27 {ECO:0000312|EMBL:AAF02160.1};
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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 263-GLN--ASN-304, AND
RP INTERACTION WITH PEX5; PEX7 AND PEX14.
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 [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, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18160292; DOI=10.1016/j.cub.2007.11.067;
RA Boisson-Dernier A., Frietsch S., Kim T.H., Dizon M.B., Schroeder J.I.;
RT "The peroxin loss-of-function mutation abstinence by mutual consent
RT disrupts male-female gametophyte recognition.";
RL Curr. Biol. 18:63-68(2008).
RN [8]
RP FUNCTION.
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 INTERACTION WITH APEM9.
RX PubMed=24510720; DOI=10.1105/tpc.113.121087;
RA Li X.R., Li H.J., Yuan L., Liu M., Shi D.Q., Liu J., Yang W.C.;
RT "Arabidopsis DAYU/ABERRANT PEROXISOME MORPHOLOGY9 is a key regulator of
RT peroxisome biogenesis and plays critical roles during pollen maturation and
RT germination in planta.";
RL Plant Cell 26:619-635(2014).
CC -!- FUNCTION: Involved in PTS1- and PTS2-dependent protein import into
CC peroxisomes (PubMed:16813573, PubMed:17478547). Required for PTS1-
CC dependent protein import into pollen peroxisomes (PubMed:18160292).
CC Acts as a docking factor on peroxisomal membranes (PubMed:16813573).
CC Required for the proper targeting of PEX7 to the peroxisome
CC (PubMed:19594707). Required for the export/release of receptors on the
CC peroxisome membrane (PubMed:19594707). Essential for pollen-tube
CC discharge that take place only in the presence of functional
CC peroxisomes in either the male or the female gametophyte
CC (PubMed:18160292). {ECO:0000269|PubMed:16813573,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:18160292,
CC ECO:0000269|PubMed:19594707}.
CC -!- SUBUNIT: Interacts (via N-terminus) with PEX7, but not with PEX5 or
CC PEX14 (PubMed:16813573). Interacts with APEM9 (via N-terminus)
CC (PubMed:24510720). {ECO:0000269|PubMed:16813573,
CC ECO:0000269|PubMed:24510720}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000305|PubMed:16813573}; Peripheral membrane protein
CC {ECO:0000305|PubMed:16813573}. Peroxisome
CC {ECO:0000269|PubMed:18160292}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SRR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SRR0-2; Sequence=VSP_040377;
CC -!- TISSUE SPECIFICITY: Highly expressed in pollen. Detected in shoots,
CC roots, stems, leaves, inflorescences and emasculated postils. Strongly
CC expressed in both male and female gametophytes during fertilization.
CC {ECO:0000269|PubMed:18160292}.
CC -!- DISRUPTION PHENOTYPE: Lethal, when homozygous.
CC {ECO:0000269|PubMed:18160292}.
CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}.
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DR EMBL; AC009853; AAF02160.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74561.1; -; Genomic_DNA.
DR EMBL; AY075689; AAL77696.1; -; mRNA.
DR EMBL; AY093745; AAM10369.1; -; mRNA.
DR EMBL; AK318837; BAH56952.1; -; mRNA.
DR RefSeq; NP_187412.1; NM_111634.6. [Q9SRR0-1]
DR AlphaFoldDB; Q9SRR0; -.
DR BioGRID; 5280; 2.
DR IntAct; Q9SRR0; 1.
DR STRING; 3702.AT3G07560.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q9SRR0; -.
DR PaxDb; Q9SRR0; -.
DR PRIDE; Q9SRR0; -.
DR EnsemblPlants; AT3G07560.1; AT3G07560.1; AT3G07560. [Q9SRR0-1]
DR GeneID; 819945; -.
DR Gramene; AT3G07560.1; AT3G07560.1; AT3G07560. [Q9SRR0-1]
DR KEGG; ath:AT3G07560; -.
DR Araport; AT3G07560; -.
DR TAIR; locus:2079621; AT3G07560.
DR eggNOG; ENOG502QSVT; Eukaryota.
DR HOGENOM; CLU_056096_0_0_1; -.
DR InParanoid; Q9SRR0; -.
DR OMA; IDQNTHA; -.
DR PhylomeDB; Q9SRR0; -.
DR PRO; PR:Q9SRR0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRR0; baseline and differential.
DR Genevisible; Q9SRR0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:TAIR.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR InterPro; IPR035463; Pex13.
DR PANTHER; PTHR19332; PTHR19332; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Peroxisome; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..304
FT /note="Peroxisomal membrane protein 13"
FT /id="PRO_0000403359"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 130..293
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040377"
FT MUTAGEN 263..304
FT /note="Missing: In apm2; reduced protein transport to
FT peroxisome and repressed plant growth."
FT /evidence="ECO:0000269|PubMed:16813573"
SQ SEQUENCE 304 AA; 31286 MW; 246722710D2D3D6C CRC64;
MASQPAGGSP PKPWEKEGNT SGPNPFRPPS NTSTAGSVEA SGTANPGEVV PPPVNRPNTA
ANMNSLSRPV PARPWEQQNY GSTMGGGYGS NLGMTSGYGS GTYGSALGGY GSSYGGGMYG
GSSMYRGGYG GGGLYGSSGM YGGGAMGGYG GTMGGYGMGM GTGMGMGMGM GMGGPYGSQD
PNDPFNQPPS PPGFWISFLR VMQGAVNFFG RVAMLIDQNT QAFHMFMSAL LQLFDRGGML
YGELARFVLR MLGVRTRPRK MQQPPQGPNG LPLPHQPHGN QNYLEGPKTA APGGGGGWDN
VWGN
