PX11B_HUMAN
ID PX11B_HUMAN Reviewed; 259 AA.
AC O96011; B3KN85; B4DXH9; Q96ET2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9826565; DOI=10.1006/bbrc.1998.9684;
RA Abe I., Fujiki Y.;
RT "cDNA cloning and characterization of a constitutively expressed isoform of
RT the human peroxin Pex11p.";
RL Biochem. Biophys. Res. Commun. 252:529-533(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND FUNCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [8]
RP INTERACTION WITH PEX19, AND SUBCELLULAR LOCATION.
RX PubMed=10704444; DOI=10.1083/jcb.148.5.931;
RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly
RT cytoplasmic, and is required for peroxisome membrane synthesis.";
RL J. Cell Biol. 148:931-944(2000).
RN [9]
RP FUNCTION.
RX PubMed=12618434; DOI=10.1074/jbc.m212031200;
RA Li X., Gould S.J.;
RT "The dynamin-like GTPase DLP1 is essential for peroxisome division and is
RT recruited to peroxisomes in part by PEX11.";
RL J. Biol. Chem. 278:17012-17020(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH FIS1 AND PEX11G, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20826455; DOI=10.1242/jcs.064907;
RA Koch J., Pranjic K., Huber A., Ellinger A., Hartig A., Kragler F.,
RA Brocard C.;
RT "PEX11 family members are membrane elongation factors that coordinate
RT peroxisome proliferation and maintenance.";
RL J. Cell Sci. 123:3389-3400(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INVOLVEMENT IN PBD14B.
RX PubMed=22581968; DOI=10.1136/jmedgenet-2012-100778;
RA Ebberink M.S., Koster J., Visser G., van Spronsen F., Stolte-Dijkstra I.,
RA Smit G.P., Fock J.M., Kemp S., Wanders R.J., Waterham H.R.;
RT "A novel defect of peroxisome division due to a homozygous non-sense
RT mutation in the PEX11beta gene.";
RL J. Med. Genet. 49:307-313(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in peroxisomal proliferation (PubMed:9792670). May
CC regulate peroxisome division by recruiting the dynamin-related GTPase
CC DNM1L to the peroxisomal membrane (PubMed:12618434). Promotes membrane
CC protrusion and elongation on the peroxisomal surface (PubMed:20826455).
CC {ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:20826455,
CC ECO:0000269|PubMed:9792670}.
CC -!- SUBUNIT: Homodimer (PubMed:20826455). Heterodimer with PEX11G
CC (PubMed:20826455). Interacts with PEX19 (PubMed:10704444). Interacts
CC with FIS1 (PubMed:20826455). {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:20826455}.
CC -!- INTERACTION:
CC O96011; P40855: PEX19; NbExp=22; IntAct=EBI-594824, EBI-594747;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670,
CC ECO:0000269|PubMed:9826565}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:9792670,
CC ECO:0000269|PubMed:9826565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O96011-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O96011-2; Sequence=VSP_042860;
CC -!- DISEASE: Peroxisome biogenesis disorder 14B (PBD14B) [MIM:614920]: An
CC autosomal recessive peroxisome biogenesis disorder characterized
CC clinically by mild intellectual disability, congenital cataracts,
CC progressive hearing loss, and polyneuropathy. Additionally, recurrent
CC migraine-like episodes following mental stress or physical exertion,
CC not a common feature in peroxisome disorders, are observed.
CC {ECO:0000269|PubMed:22581968}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
CC -!- CAUTION: PubMed:9792670 states that both the N- and the C-terminus are
CC located in the cytoplasm. {ECO:0000305}.
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DR EMBL; AB018080; BAA34812.1; -; mRNA.
DR EMBL; AF093670; AAC78660.1; -; mRNA.
DR EMBL; CR542047; CAG46844.1; -; mRNA.
DR EMBL; AK023991; BAG51247.1; -; mRNA.
DR EMBL; AK301983; BAG63391.1; -; mRNA.
DR EMBL; AL160282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471244; EAW71422.1; -; Genomic_DNA.
DR EMBL; BC011963; AAH11963.1; -; mRNA.
DR CCDS; CCDS72870.1; -. [O96011-2]
DR CCDS; CCDS72871.1; -. [O96011-1]
DR PIR; JE0326; JE0326.
DR RefSeq; NP_001171724.1; NM_001184795.1. [O96011-2]
DR RefSeq; NP_003837.1; NM_003846.2. [O96011-1]
DR AlphaFoldDB; O96011; -.
DR SMR; O96011; -.
DR BioGRID; 114327; 34.
DR IntAct; O96011; 13.
DR MINT; O96011; -.
DR STRING; 9606.ENSP00000358312; -.
DR iPTMnet; O96011; -.
DR PhosphoSitePlus; O96011; -.
DR SwissPalm; O96011; -.
DR BioMuta; PEX11B; -.
DR EPD; O96011; -.
DR jPOST; O96011; -.
DR MassIVE; O96011; -.
DR MaxQB; O96011; -.
DR PaxDb; O96011; -.
DR PeptideAtlas; O96011; -.
DR PRIDE; O96011; -.
DR ProteomicsDB; 51190; -. [O96011-1]
DR ProteomicsDB; 51191; -. [O96011-2]
DR Antibodypedia; 33960; 122 antibodies from 26 providers.
DR DNASU; 8799; -.
DR Ensembl; ENST00000369306.8; ENSP00000358312.3; ENSG00000131779.11. [O96011-1]
DR Ensembl; ENST00000537888.1; ENSP00000437510.1; ENSG00000131779.11. [O96011-2]
DR GeneID; 8799; -.
DR KEGG; hsa:8799; -.
DR MANE-Select; ENST00000369306.8; ENSP00000358312.3; NM_003846.3; NP_003837.1.
DR UCSC; uc001eny.3; human. [O96011-1]
DR CTD; 8799; -.
DR DisGeNET; 8799; -.
DR GeneCards; PEX11B; -.
DR GeneReviews; PEX11B; -.
DR HGNC; HGNC:8853; PEX11B.
DR HPA; ENSG00000131779; Low tissue specificity.
DR MalaCards; PEX11B; -.
DR MIM; 603867; gene.
DR MIM; 614920; phenotype.
DR neXtProt; NX_O96011; -.
DR OpenTargets; ENSG00000131779; -.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA33195; -.
DR VEuPathDB; HostDB:ENSG00000131779; -.
DR eggNOG; KOG4186; Eukaryota.
DR GeneTree; ENSGT00390000014273; -.
DR HOGENOM; CLU_049216_2_0_1; -.
DR InParanoid; O96011; -.
DR OMA; RFWAMGL; -.
DR PhylomeDB; O96011; -.
DR TreeFam; TF325704; -.
DR PathwayCommons; O96011; -.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; O96011; -.
DR BioGRID-ORCS; 8799; 38 hits in 1076 CRISPR screens.
DR ChiTaRS; PEX11B; human.
DR GeneWiki; PEX11B; -.
DR GenomeRNAi; 8799; -.
DR Pharos; O96011; Tbio.
DR PRO; PR:O96011; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O96011; protein.
DR Bgee; ENSG00000131779; Expressed in prefrontal cortex and 197 other tissues.
DR ExpressionAtlas; O96011; baseline and differential.
DR Genevisible; O96011; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB.
DR GO; GO:0044375; P:regulation of peroxisome size; IDA:UniProtKB.
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; Alternative splicing; Membrane; Peroxisome;
KW Peroxisome biogenesis; Peroxisome biogenesis disorder; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Peroxisomal membrane protein 11B"
FT /id="PRO_0000105967"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..259
FT /note="Interaction with PEX19, PEX11G and FIS1 and
FT peroxisome targeting"
FT /evidence="ECO:0000269|PubMed:10704444,
FT ECO:0000269|PubMed:20826455"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..18
FT /note="MDAWVRFSAQSQARERLC -> MGKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042860"
FT CONFLICT 98
FT /note="A -> V (in Ref. 7; AAH11963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28431 MW; DC26CE30021C7B8D CRC64;
MDAWVRFSAQ SQARERLCRA AQYACSLLGH ALQRHGASPE LQKQIRQLES HLSLGRKLLR
LGNSADALES AKRAVHLSDV VLRFCITVSH LNRALYFACD NVLWAGKSGL APRVDQEKWA
QRSFRYYLFS LIMNLSRDAY EIRLLMEQES SACSRRLKGS GGGVPGGSET GGLGGPGTPG
GGLPQLALKL RLQVLLLARV LRGHPPLLLD VVRNACDLFI PLDKLGLWRC GPGIVGLCGL
VSSILSILTL IYPWLRLKP
