PX11A_MOUSE
ID PX11A_MOUSE Reviewed; 246 AA.
AC Q9Z211; Q8C5B8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Peroxisomal membrane protein 11A;
DE AltName: Full=Peroxin-11A;
DE AltName: Full=Peroxisomal biogenesis factor 11A;
DE AltName: Full=Protein PEX11 homolog alpha;
DE Short=PEX11-alpha;
GN Name=Pex11a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-246.
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12417726; DOI=10.1128/mcb.22.23.8226-8240.2002;
RA Li X., Baumgart E., Dong G.-X., Morrell J.C., Jimenez-Sanchez G., Valle D.,
RA Smith K.D., Gould S.J.;
RT "PEX11alpha is required for peroxisome proliferation in response to 4-
RT phenylbutyrate but is dispensable for peroxisome proliferator-activated
RT receptor alpha-mediated peroxisome proliferation.";
RL Mol. Cell. Biol. 22:8226-8240(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Promotes membrane protrusion and
CC elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O70597,
CC ECO:0000250|UniProtKB:O75192, ECO:0000269|PubMed:12417726}.
CC -!- SUBUNIT: Homodimer. Heterodimer with PEX11G. Probably interacts with
CC COPB2 and COPA. Interacts with PEX19. Interacts with FIS1.
CC {ECO:0000250|UniProtKB:O70597, ECO:0000250|UniProtKB:O75192}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:O75192}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O75192}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in liver and at lower levels in
CC heart, brain, kidney and testis. {ECO:0000269|PubMed:12417726}.
CC -!- INDUCTION: By ciprofibrate. {ECO:0000269|PubMed:12417726}.
CC -!- DISRUPTION PHENOTYPE: Mice have no detectable defect in constitutive
CC peroxisome division and display a normal peroxisome proliferation
CC response when exposed to PPARalpha-activating drugs. However, they are
CC defective in peroxisome proliferation induced by 4-phenylbutyrate (4-
CC PBA). {ECO:0000269|PubMed:12417726}.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AF093669; AAC78659.1; -; mRNA.
DR EMBL; BC023439; AAH23439.1; -; mRNA.
DR EMBL; AK078954; BAC37477.1; -; mRNA.
DR CCDS; CCDS21386.1; -.
DR RefSeq; NP_035198.1; NM_011068.1.
DR AlphaFoldDB; Q9Z211; -.
DR STRING; 10090.ENSMUSP00000032761; -.
DR iPTMnet; Q9Z211; -.
DR PhosphoSitePlus; Q9Z211; -.
DR SwissPalm; Q9Z211; -.
DR jPOST; Q9Z211; -.
DR MaxQB; Q9Z211; -.
DR PaxDb; Q9Z211; -.
DR PRIDE; Q9Z211; -.
DR ProteomicsDB; 301834; -.
DR Antibodypedia; 28643; 161 antibodies from 25 providers.
DR DNASU; 18631; -.
DR Ensembl; ENSMUST00000032761; ENSMUSP00000032761; ENSMUSG00000030545.
DR GeneID; 18631; -.
DR KEGG; mmu:18631; -.
DR UCSC; uc009hyy.1; mouse.
DR CTD; 8800; -.
DR MGI; MGI:1338788; Pex11a.
DR VEuPathDB; HostDB:ENSMUSG00000030545; -.
DR eggNOG; KOG4186; Eukaryota.
DR GeneTree; ENSGT00390000014273; -.
DR HOGENOM; CLU_049216_2_0_1; -.
DR InParanoid; Q9Z211; -.
DR OMA; AAKRTMQ; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; Q9Z211; -.
DR TreeFam; TF325704; -.
DR BioGRID-ORCS; 18631; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9Z211; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z211; protein.
DR Bgee; ENSMUSG00000030545; Expressed in gonadal fat pad and 246 other tissues.
DR Genevisible; Q9Z211; MM.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0016559; P:peroxisome fission; ISO:MGI.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0044375; P:regulation of peroxisome size; ISO:MGI.
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_0000105965"
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"
SQ SEQUENCE 246 AA; 28153 MW; A11BAC5406D55D2B CRC64;
MDAFIRVANQ SQGRDRLFRA TQHACMLLRY LLESKADKEA VVLKLKRLET SVSTGRKWFR
LGNVFHAIQA TEQSIQAADL APRLCLTLAN LNRVVYYICD TVLWAKSVGL TSGVNREKWQ
RWAARHYYYF LLLSLVRDLY EILLQMGQVA RDRAKREKSS RDPPKYSVAN EETEWLQSFL
LLLFQSLKRH PPLLLDTVKN FCDILIPLNQ LGIYKSNLGV VGLGGLISSL AGLLTVVYPQ
LKLKAR
