PX11B_MOUSE
ID PX11B_MOUSE Reviewed; 259 AA.
AC Q9Z210; Q8C4G1; Q9D090;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peroxisomal membrane protein 11B;
DE AltName: Full=Peroxin-11B;
DE AltName: Full=Peroxisomal biogenesis factor 11B;
DE AltName: Full=Protein PEX11 homolog beta;
DE Short=PEX11-beta;
GN Name=Pex11b;
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; TISSUE=Cerebellum, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; 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 [4]
RP FUNCTION.
RX PubMed=11839773; DOI=10.1083/jcb.200112028;
RA Li X., Gould S.J.;
RT "PEX11 promotes peroxisome division independently of peroxisome
RT metabolism.";
RL J. Cell Biol. 156:643-651(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12024045; DOI=10.1128/mcb.22.12.4358-4365.2002;
RA Li X., Baumgart E., Morrell J.C., Jimenez-Sanchez G., Valle D., Gould S.J.;
RT "PEX11 beta deficiency is lethal and impairs neuronal migration but does
RT not abrogate peroxisome function.";
RL Mol. Cell. Biol. 22:4358-4365(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Involved in peroxisomal proliferation. May regulate
CC peroxisome division by recruiting the dynamin-related GTPase DNM1L to
CC the peroxisomal membrane. Promotes membrane protrusion and elongation
CC on the peroxisomal surface. {ECO:0000250|UniProtKB:O96011,
CC ECO:0000269|PubMed:11839773, ECO:0000269|PubMed:12024045}.
CC -!- SUBUNIT: Homodimer. Heterodimer with PEX11G. Interacts with PEX19.
CC Interacts with FIS1. {ECO:0000250|UniProtKB:O96011}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:O96011}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O96011}.
CC -!- DISRUPTION PHENOTYPE: Mice have a marked decrease in peroxisome
CC abundance. They share several phenotypes with Zellweger syndrome mouse
CC models, including neuronal migration defects, hypotonia, a
CC developmental delay, and neonatal lethality but no detectable defect in
CC peroxisomal protein import and only mild defects in peroxisomal
CC metabolic function. {ECO:0000269|PubMed:12024045}.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AF093671; AAC78661.1; -; mRNA.
DR EMBL; AK011709; BAB27791.1; -; mRNA.
DR EMBL; AK082279; BAC38453.1; -; mRNA.
DR EMBL; BC013812; AAH13812.1; -; mRNA.
DR EMBL; BC054414; AAH54414.1; -; mRNA.
DR CCDS; CCDS17643.1; -.
DR RefSeq; NP_001155859.1; NM_001162387.1.
DR RefSeq; NP_035199.3; NM_011069.3.
DR AlphaFoldDB; Q9Z210; -.
DR SMR; Q9Z210; -.
DR BioGRID; 202116; 7.
DR STRING; 10090.ENSMUSP00000113365; -.
DR iPTMnet; Q9Z210; -.
DR PhosphoSitePlus; Q9Z210; -.
DR SwissPalm; Q9Z210; -.
DR EPD; Q9Z210; -.
DR jPOST; Q9Z210; -.
DR MaxQB; Q9Z210; -.
DR PaxDb; Q9Z210; -.
DR PeptideAtlas; Q9Z210; -.
DR PRIDE; Q9Z210; -.
DR ProteomicsDB; 301835; -.
DR Antibodypedia; 33960; 122 antibodies from 26 providers.
DR DNASU; 18632; -.
DR Ensembl; ENSMUST00000048766; ENSMUSP00000037962; ENSMUSG00000028102.
DR Ensembl; ENSMUST00000118557; ENSMUSP00000113365; ENSMUSG00000028102.
DR GeneID; 18632; -.
DR KEGG; mmu:18632; -.
DR UCSC; uc008qnn.2; mouse.
DR CTD; 8799; -.
DR MGI; MGI:1338882; Pex11b.
DR VEuPathDB; HostDB:ENSMUSG00000028102; -.
DR eggNOG; KOG4186; Eukaryota.
DR GeneTree; ENSGT00390000014273; -.
DR HOGENOM; CLU_049216_2_0_1; -.
DR InParanoid; Q9Z210; -.
DR OMA; RFWAMGL; -.
DR OrthoDB; 1394894at2759; -.
DR TreeFam; TF325704; -.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 18632; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z210; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z210; protein.
DR Bgee; ENSMUSG00000028102; Expressed in spermatocyte and 229 other tissues.
DR ExpressionAtlas; Q9Z210; baseline and differential.
DR Genevisible; Q9Z210; MM.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0016559; P:peroxisome fission; 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 Acetylation; Membrane; Peroxisome; Peroxisome biogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Peroxisomal membrane protein 11B"
FT /id="PRO_0000105968"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 211..259
FT /note="Interaction with PEX19, PEX11G and FIS1 and
FT peroxisome targeting"
FT /evidence="ECO:0000250|UniProtKB:O96011"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O96011"
FT CONFLICT 119
FT /note="W -> R (in Ref. 2; BAC38453)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> N (in Ref. 2; BAB27791)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> F (in Ref. 2; BAB27791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28710 MW; C0E1BF979E325EB2 CRC64;
MDAWVRFSAQ SQARERLCRA AQYACSLLGH ALQRHGASPE LQKQIRQLEG HLSLGRKLLR
LGNSTDALES AKRAVHLSDV VLRFCITVSH LNRALYFACD NVLWAGKSGL APRVDQEKWA
QRSFRYYLFS LIMNLSRDAY EIRLLMEQET SAYSRRMKVS GVGVSGGVET VGPGGPGTPG
GSLPQLALKF RLRILLLARV LRGHPPLLLD VLRNACDLFI PLDKLGLWRC GPGIVGLCGL
ISSILSILTL ICPWLRLKP
