PX11A_RAT
ID PX11A_RAT Reviewed; 246 AA.
AC O70597; Q6P749;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Peroxisomal membrane protein 11A;
DE AltName: Full=28 kDa peroxisomal integral membrane protein;
DE Short=PMP28;
DE AltName: Full=Peroxin-11A;
DE AltName: Full=Peroxisomal biogenesis factor 11A;
DE AltName: Full=Peroxisomal coatomer receptor;
DE AltName: Full=Peroxisomal membrane protein 26;
DE Short=Pmp26p;
DE AltName: Full=Protein PEX11 homolog alpha;
DE Short=PEX11-alpha;
DE AltName: Full=RnPEX11p;
GN Name=Pex11a; Synonyms=Pex11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION,
RP MUTAGENESIS OF 242-LYS--LYS-244, AND INTERACTION WITH COPB2 AND COPA.
RC TISSUE=Liver;
RX PubMed=9548716; DOI=10.1083/jcb.141.2.373;
RA Passreiter M., Anton M., Lay D., Frank R., Harter C., Wieland F.T.,
RA Gorgas K., Just W.W.;
RT "Peroxisome biogenesis: involvement of ARF and coatomer.";
RL J. Cell Biol. 141:373-383(1998).
RN [2]
RP INDUCTION.
RC TISSUE=Liver;
RX PubMed=9714566; DOI=10.1016/s0014-5793(98)00815-1;
RA Abe I., Okumoto K., Tamura S., Fujiki Y.;
RT "Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is
RT encoded by PEX11.";
RL FEBS Lett. 431:468-472(1998).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9792670; DOI=10.1074/jbc.273.45.29607;
RA Schrader M., Reuber B.E., Morrell J.C., Jimenez-Sanchez G., Obie C.,
RA Stroh T.A., Valle D., Schroer T.A., Gould S.J.;
RT "Expression of PEX11beta mediates peroxisome proliferation in the absence
RT of extracellular stimuli.";
RL J. Biol. Chem. 273:29607-29614(1998).
CC -!- FUNCTION: May be involved in peroxisomal proliferation and may regulate
CC peroxisomes division. May mediate binding of coatomer proteins to the
CC peroxisomal membrane (PubMed:9548716). Promotes membrane protrusion and
CC elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O75192,
CC ECO:0000269|PubMed:9548716}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer with PEX11G (By
CC similarity). Probably interacts with COPB2 and COPA (PubMed:9548716).
CC Interacts with PEX19 (By similarity). Interacts with FIS1 (By
CC similarity). {ECO:0000250|UniProtKB:O75192,
CC ECO:0000269|PubMed:9548716}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9548716};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9548716}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, liver, lung,
CC brain, and testis and at low levels in heart, spleen and skeletal
CC muscle. {ECO:0000269|PubMed:9792670}.
CC -!- INDUCTION: Induced by clofibrate and di(2-ethylhexyl)phtalate (DEHP).
CC {ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AJ224120; CAA11838.1; -; mRNA.
DR RefSeq; NP_445939.1; NM_053487.2.
DR AlphaFoldDB; O70597; -.
DR IntAct; O70597; 1.
DR MINT; O70597; -.
DR STRING; 10116.ENSRNOP00000020229; -.
DR PaxDb; O70597; -.
DR PRIDE; O70597; -.
DR Ensembl; ENSRNOT00000020229; ENSRNOP00000020229; ENSRNOG00000015003.
DR GeneID; 85249; -.
DR KEGG; rno:85249; -.
DR UCSC; RGD:619842; rat.
DR CTD; 8800; -.
DR RGD; 619842; Pex11a.
DR eggNOG; KOG4186; Eukaryota.
DR GeneTree; ENSGT00390000014273; -.
DR HOGENOM; CLU_049216_2_0_1; -.
DR InParanoid; O70597; -.
DR OMA; AAKRTMQ; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; O70597; -.
DR TreeFam; TF325704; -.
DR PRO; PR:O70597; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015003; Expressed in kidney and 19 other tissues.
DR Genevisible; O70597; RN.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0016559; P:peroxisome fission; ISO:RGD.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; IDA:RGD.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0044375; P:regulation of peroxisome size; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR InterPro; IPR008733; PEX11.
DR Pfam; PF05648; PEX11; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..246
FT /note="Peroxisomal membrane protein 11A"
FT /id="PRO_0000105966"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..217
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 218..238
FT /note="Required for homodimerization, interaction with
FT PEX11G, and peroxisomal localization"
FT /evidence="ECO:0000250|UniProtKB:O75192"
FT MUTAGEN 242..244
FT /note="KLK->SLS: Loss of interactions with COPA and COPB2."
FT /evidence="ECO:0000269|PubMed:9548716"
FT MUTAGEN 244
FT /note="K->S: Loss of interactions with COPA and COPB2."
SQ SEQUENCE 246 AA; 27923 MW; A4D1951ADE21B04E CRC64;
MDAFIRVANQ SQGRDRLFRA TQHACMLLRY LLESKAGKEA VVTKLKNLET SVSTGRKWFR
LGNVLHAIQA TEQSIQATDL VPRLCLTLAN LNRVVYYICD TVLWAKSVGL TSGINREKWQ
MRAARHYYYF LLLSLVRDLY EVLLHMGQVA RDRAKREKSS GDPPKYSVAN EESEWLQSFL
LLLFQSLKRN PPLFLDTVKN FCDILIPLNQ LGIYKSNLGV VGFGGLVSSV AGLITVVYPQ
LKLKAR
