PEX16_ARATH
ID PEX16_ARATH Reviewed; 367 AA.
AC Q8S8S1; Q682F3; Q9XEG0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Peroxisome biogenesis protein 16 {ECO:0000303|PubMed:16040658};
DE AltName: Full=Peroxin-16 {ECO:0000303|PubMed:16040658};
DE Short=AtPEX16 {ECO:0000303|PubMed:16040658};
DE Short=AtPex16p {ECO:0000303|PubMed:15173561};
DE AltName: Full=Protein SHRUNKEN SEED 1 {ECO:0000303|PubMed:10195899};
GN Name=PEX16 {ECO:0000303|PubMed:16040658};
GN Synonyms=SSE1 {ECO:0000303|PubMed:10195899};
GN OrderedLocusNames=At2g45690 {ECO:0000312|Araport:AT2G45690};
GN ORFNames=F17K2.22 {ECO:0000312|EMBL:AAM14899.1};
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, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10195899; DOI=10.1126/science.284.5412.328;
RA Lin Y., Sun L., Nguyen L.V., Rachubinski R.A., Goodman H.M.;
RT "The Pex16p homolog SSE1 and storage organelle formation in Arabidopsis
RT seeds.";
RL Science 284:328-330(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15173561; DOI=10.1104/pp.103.036772;
RA Lin Y., Cluette-Brown J.E., Goodman H.M.;
RT "The peroxisome deficient Arabidopsis mutant sse1 exhibits impaired fatty
RT acid synthesis.";
RL Plant Physiol. 135:814-827(2004).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND POST-TRANSLATIONAL
RP MODIFICATION.
RX PubMed=16040658; DOI=10.1104/pp.105.061291;
RA Karnik S.K., Trelease R.N.;
RT "Arabidopsis peroxin 16 coexists at steady state in peroxisomes and
RT endoplasmic reticulum.";
RL Plant Physiol. 138:1967-1981(2005).
RN [7]
RP FUNCTION.
RX PubMed=16896794; DOI=10.1007/s00425-006-0337-6;
RA Lin Y., Ulanov A.V., Lozovaya V., Widholm J., Zhang G., Guo J.,
RA Goodman H.M.;
RT "Genetic and transgenic perturbations of carbon reserve production in
RT Arabidopsis seeds reveal metabolic interactions of biochemical pathways.";
RL Planta 225:153-164(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF 221-ARG--ARG-223; 258-ARG--TYR-260;
RP 258-ARG--SER-264 AND 306-ARG--ARG-308, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17431024; DOI=10.1093/jxb/erm018;
RA Karnik S.K., Trelease R.N.;
RT "Arabidopsis peroxin 16 trafficks through the ER and an intermediate
RT compartment to pre-existing peroxisomes via overlapping molecular targeting
RT signals.";
RL J. Exp. Bot. 58:1677-1693(2007).
RN [9]
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 [10]
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 the formation of peroxisomes, lipid bodies and
CC protein bodies. {ECO:0000269|PubMed:10195899,
CC ECO:0000269|PubMed:15173561, ECO:0000269|PubMed:16896794,
CC ECO:0000269|PubMed:17431024, ECO:0000269|PubMed:17478547}.
CC -!- SUBUNIT: Interacts with APEM9 (via both N- and C-terminus).
CC {ECO:0000269|PubMed:24510720}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Moves
CC through an intermediate compartment from endoplasmic reticulum to pre-
CC existing peroxisomes. {ECO:0000269|PubMed:15173561,
CC ECO:0000269|PubMed:16040658, ECO:0000269|PubMed:17431024}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, siliques, seeds, cotyledons,
CC leaves and flowers. Low expression in leaves and roots.
CC {ECO:0000269|PubMed:10195899, ECO:0000269|PubMed:15173561,
CC ECO:0000269|PubMed:16040658}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during seed maturation.
CC {ECO:0000269|PubMed:10195899}.
CC -!- DOMAIN: The internal domain (235-279) containing two internal membrane
CC helices and the intervening residues that include the basic cluster VRS
CC is sufficient for targeting recombinant proteins to endoplasmic
CC reticulum and then to peroxisomes.
CC -!- PTM: The detection of an additional immunorelated polypeptide of 52 kDa
CC suggests a post-translational modification of PEX16.
CC -!- DISRUPTION PHENOTYPE: Not viable shrunken seeds. Starch accumulation in
CC mature embryos, cotyledon and hypocotyl cells. Developmental delay
CC during early embryo morphogenesis. {ECO:0000269|PubMed:10195899}.
CC -!- MISCELLANEOUS: Travels from the cytosol to peroxisomes via the
CC reticular and perinuclear endoplasmic reticulum (ER) and an ER-
CC peroxisome intermediate compartment (ERPIC).
CC -!- SIMILARITY: Belongs to the peroxin-16 family. {ECO:0000305}.
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DR EMBL; AF085354; AAD30661.1; -; mRNA.
DR EMBL; AC003680; AAM14899.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10587.1; -; Genomic_DNA.
DR EMBL; AK175396; BAD43159.1; -; mRNA.
DR EMBL; AK175414; BAD43177.1; -; mRNA.
DR RefSeq; NP_566053.1; NM_130132.4.
DR AlphaFoldDB; Q8S8S1; -.
DR BioGRID; 4513; 1.
DR STRING; 3702.AT2G45690.1; -.
DR TCDB; 9.A.17.1.3; the integral membrane peroxisomal protein importer-2 (ppi2) family.
DR iPTMnet; Q8S8S1; -.
DR PaxDb; Q8S8S1; -.
DR PRIDE; Q8S8S1; -.
DR ProteomicsDB; 236428; -.
DR EnsemblPlants; AT2G45690.1; AT2G45690.1; AT2G45690.
DR GeneID; 819177; -.
DR Gramene; AT2G45690.1; AT2G45690.1; AT2G45690.
DR KEGG; ath:AT2G45690; -.
DR Araport; AT2G45690; -.
DR TAIR; locus:2043674; AT2G45690.
DR eggNOG; KOG4546; Eukaryota.
DR HOGENOM; CLU_036533_0_0_1; -.
DR InParanoid; Q8S8S1; -.
DR OMA; GQRSWKQ; -.
DR OrthoDB; 908842at2759; -.
DR PhylomeDB; Q8S8S1; -.
DR PRO; PR:Q8S8S1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8S1; baseline and differential.
DR Genevisible; Q8S8S1; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR InterPro; IPR013919; Pex16.
DR PANTHER; PTHR13299; PTHR13299; 1.
DR Pfam; PF08610; Pex16; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Peroxisome; Peroxisome biogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="Peroxisome biogenesis protein 16"
FT /id="PRO_0000403363"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 135..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 221..223
FT /note="RRR->GGG: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:17431024"
FT MUTAGEN 258..264
FT /note="RKYGVRS->GGGGGGG: Loss of targeting to peroxisome."
FT /evidence="ECO:0000269|PubMed:17431024"
FT MUTAGEN 258..260
FT /note="RKY->GGG: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:17431024"
FT MUTAGEN 306..308
FT /note="RRR->GGG: No effect on targeting."
FT /evidence="ECO:0000269|PubMed:17431024"
FT CONFLICT 51
FT /note="S -> T (in Ref. 1; AAD30661)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> T (in Ref. 4; BAD43177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41611 MW; 9667E97388D55EB9 CRC64;
MEAYKQWVWR NREYVQSFGS FANGLTWLLP EKFSASEIGP EAVTAFLGIF STINEHIIEN
APTPRGHVGS SGNDPSLSYP LLIAILKDLE TVVEVAAEHF YGDKKWNYII LTEAMKAVIR
LALFRNSGYK MLLQGGETPN EEKDSNQSES QNRAGNSGRN LGPHGLGNQN HHNPWNLEGR
AMSALSSFGQ NARTTTSSTP GWSRRIQHQQ AVIEPPMIKE RRRTMSELLT EKGVNGALFA
IGEVLYITRP LIYVLFIRKY GVRSWIPWAI SLSVDTLGMG LLANSKWWGE KSKQVHFSGP
EKDELRRRKL IWALYLMRDP FFTKYTRQKL ESSQKKLELI PLIGFLTEKI VELLEGAQSR
YTYISGS
