APEM9_ARATH
ID APEM9_ARATH Reviewed; 333 AA.
AC Q8W4B2; Q9LPP1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein APEM9 {ECO:0000303|PubMed:21487094};
DE AltName: Full=ABERRANT PEROXISOME MORPHOLOGY 9 {ECO:0000303|PubMed:21487094};
DE AltName: Full=Protein DAYU {ECO:0000303|PubMed:24510720};
GN Name=APEM9 {ECO:0000303|PubMed:21487094};
GN Synonyms=DAU {ECO:0000303|PubMed:24510720};
GN OrderedLocusNames=At3g10572 {ECO:0000312|Araport:AT3G10572};
GN ORFNames=F18K10.16 {ECO:0000312|EMBL:AAF76360.1};
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 {ECO:0000312|EMBL:AAL32762.1};
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=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, MUTAGENESIS OF GLY-278, SUBCELLULAR LOCATION, INTERACTION WITH
RP PEX6 AND PEX19-1, LACK OF INTERACTION WITH PEX1, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TOPOLOGY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH PEX13 AND PEX16.
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 peroxisome biogenesis and matrix protein import
CC (PubMed:24510720). Required for pollen maturation and in vivo
CC germination via its role in peroxisomal function, which partially
CC involves jasmonic acid biosynthesis (PubMed:24510720). Transported to
CC peroxisomes via the interaction with PEX19-1 (PubMed:21487094).
CC Required for peroxisomal protein import by acting as an anchoring
CC protein for the AAA ATPase complex, which consists of PEX1 and PEX6
CC (PubMed:21487094). {ECO:0000269|PubMed:21487094,
CC ECO:0000269|PubMed:24510720}.
CC -!- SUBUNIT: Interacts with PEX6 and PEX19-1, but not with PEX1
CC (PubMed:21487094). Interacts (via N-terminus) with PEX13, and (via N-
CC terminus and C-terminus) with PEX16 (PubMed:24510720).
CC {ECO:0000269|PubMed:21487094, ECO:0000269|PubMed:24510720}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:21487094}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers, buds
CC and fruits. {ECO:0000269|PubMed:21487094}.
CC -!- DEVELOPMENTAL STAGE: Not detected in microspores before and at stage of
CC pollen mitosis I. Expressed in bicellular, tricellular and mature
CC pollen grains. {ECO:0000269|PubMed:24510720}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality, when homozygous.
CC {ECO:0000269|PubMed:21487094, ECO:0000269|PubMed:24510720}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013428; AAF76360.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74927.1; -; Genomic_DNA.
DR EMBL; AY062684; AAL32762.1; -; mRNA.
DR EMBL; AY093365; AAM13364.1; -; mRNA.
DR RefSeq; NP_850555.1; NM_180224.4.
DR AlphaFoldDB; Q8W4B2; -.
DR SMR; Q8W4B2; -.
DR IntAct; Q8W4B2; 1.
DR STRING; 3702.AT3G10572.1; -.
DR PaxDb; Q8W4B2; -.
DR PRIDE; Q8W4B2; -.
DR ProteomicsDB; 244965; -.
DR EnsemblPlants; AT3G10572.1; AT3G10572.1; AT3G10572.
DR GeneID; 820223; -.
DR Gramene; AT3G10572.1; AT3G10572.1; AT3G10572.
DR KEGG; ath:AT3G10572; -.
DR Araport; AT3G10572; -.
DR TAIR; locus:1005716603; AT3G10572.
DR eggNOG; ENOG502QV2J; Eukaryota.
DR HOGENOM; CLU_044007_0_0_1; -.
DR InParanoid; Q8W4B2; -.
DR OMA; CMFEEAA; -.
DR OrthoDB; 1076056at2759; -.
DR PhylomeDB; Q8W4B2; -.
DR PRO; PR:Q8W4B2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W4B2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0015919; P:peroxisomal membrane transport; IEA:InterPro.
DR GO; GO:0043574; P:peroxisomal transport; IMP:TAIR.
DR InterPro; IPR034571; APEM9.
DR PANTHER; PTHR36361; PTHR36361; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..333
FT /note="Protein APEM9"
FT /id="PRO_0000438625"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24510720"
FT TRANSMEM 91..102
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24510720"
FT TOPO_DOM 103..268
FT /note="Peroxisomal"
FT /evidence="ECO:0000305|PubMed:24510720"
FT TRANSMEM 269..285
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24510720"
FT TOPO_DOM 286..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24510720"
FT MUTAGEN 278
FT /note="G->E: In apem9-1; loss of peroxisomal localization,
FT but no effect on the interaction with PEX6."
FT /evidence="ECO:0000269|PubMed:21487094"
SQ SEQUENCE 333 AA; 37467 MW; B473AABE121A41F7 CRC64;
MEATDIWGEI ERSESYLVCS MYEEAESLSS SILKRIFGNI DVLSDEASQG DHQFHDMLES
AGMVLVQSLH GIGRTVEIVN ELRDVFGEVA AIPVQVLLTG VCLQISNGSY LGVRDILEEF
FRIWVYKDNH YILNDAGVST KGFHAKNCLD IDEYMEVVEL YTFGVLAKFS NDMGLAISWV
EKAALPEERR QGILRRLHSL LSLKTASSFE ENSKDSSYAV VNNKKSLGNE KNDEIDSFLK
LSKQHEPWSL WSSHPLSLKV GNTQFSMSRG KVAVSLVGLI ICYALKRKRA ALIRIIRRQM
ESTRKAIVDF WKLAFSYQVN PLAAIQSIPS TTT
