PX11A_HUMAN
ID PX11A_HUMAN Reviewed; 247 AA.
AC O75192; B4DV88;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peroxisomal membrane protein 11A;
DE Short=HsPEX11p;
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=Protein PEX11 homolog alpha;
DE Short=PEX11-alpha;
GN Name=PEX11A; Synonyms=PEX11;
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), SUBCELLULAR LOCATION, MUTAGENESIS
RP OF ASN-9 AND 243-LYS--LYS-245, AND TOPOLOGY.
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 [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] (ISOFORM 2).
RC TISSUE=Small intestine;
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP INTERACTION WITH PEX19.
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 [8]
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).
CC -!- FUNCTION: May be involved in peroxisomal proliferation and may regulate
CC peroxisomes division (PubMed:9792670). May mediate binding of coatomer
CC proteins to the peroxisomal membrane (By similarity). Promotes membrane
CC protrusion and elongation on the peroxisomal surface (PubMed:20826455).
CC {ECO:0000250|UniProtKB:O70597, ECO:0000269|PubMed:20826455,
CC ECO:0000269|PubMed:9792670}.
CC -!- SUBUNIT: Homodimer (PubMed:20826455). Heterodimer with PEX11G
CC (PubMed:20826455). Probably interacts with COPB2 and COPA (By
CC similarity). Interacts with PEX19 (PubMed:10704444). Interacts with
CC FIS1 (PubMed:20826455). {ECO:0000250|UniProtKB:O70597,
CC ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:20826455}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:20826455,
CC ECO:0000269|PubMed:9714566, ECO:0000269|PubMed:9792670}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9714566,
CC ECO:0000269|PubMed:9792670}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75192-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75192-2; Sequence=VSP_054753;
CC -!- PTM: Seems not to be N-glycosylated.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AB015594; BAA32533.1; -; mRNA.
DR EMBL; AF093668; AAC78658.1; -; mRNA.
DR EMBL; CR542046; CAG46843.1; -; mRNA.
DR EMBL; CR542075; CAG46872.1; -; mRNA.
DR EMBL; AK300978; BAG62600.1; -; mRNA.
DR EMBL; AC013787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009697; AAH09697.1; -; mRNA.
DR CCDS; CCDS10354.1; -. [O75192-1]
DR CCDS; CCDS61751.1; -. [O75192-2]
DR RefSeq; NP_001258501.1; NM_001271572.1. [O75192-2]
DR RefSeq; NP_003838.1; NM_003847.2. [O75192-1]
DR AlphaFoldDB; O75192; -.
DR BioGRID; 114328; 14.
DR IntAct; O75192; 3.
DR STRING; 9606.ENSP00000300056; -.
DR TCDB; 1.A.101.1.2; the peroxisomal pore-forming pex11 (pex11) family.
DR GlyGen; O75192; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75192; -.
DR PhosphoSitePlus; O75192; -.
DR BioMuta; PEX11A; -.
DR EPD; O75192; -.
DR jPOST; O75192; -.
DR MassIVE; O75192; -.
DR MaxQB; O75192; -.
DR PaxDb; O75192; -.
DR PeptideAtlas; O75192; -.
DR PRIDE; O75192; -.
DR ProteomicsDB; 49864; -. [O75192-1]
DR ProteomicsDB; 5253; -.
DR Antibodypedia; 28643; 161 antibodies from 25 providers.
DR DNASU; 8800; -.
DR Ensembl; ENST00000300056.8; ENSP00000300056.3; ENSG00000166821.9. [O75192-1]
DR Ensembl; ENST00000561257.1; ENSP00000453492.1; ENSG00000166821.9. [O75192-2]
DR GeneID; 8800; -.
DR KEGG; hsa:8800; -.
DR MANE-Select; ENST00000300056.8; ENSP00000300056.3; NM_003847.3; NP_003838.1.
DR UCSC; uc002boi.5; human. [O75192-1]
DR CTD; 8800; -.
DR DisGeNET; 8800; -.
DR GeneCards; PEX11A; -.
DR HGNC; HGNC:8852; PEX11A.
DR HPA; ENSG00000166821; Low tissue specificity.
DR MIM; 603866; gene.
DR neXtProt; NX_O75192; -.
DR OpenTargets; ENSG00000166821; -.
DR PharmGKB; PA33194; -.
DR VEuPathDB; HostDB:ENSG00000166821; -.
DR eggNOG; KOG4186; Eukaryota.
DR GeneTree; ENSGT00390000014273; -.
DR HOGENOM; CLU_049216_2_0_1; -.
DR InParanoid; O75192; -.
DR OMA; AAKRTMQ; -.
DR PhylomeDB; O75192; -.
DR TreeFam; TF325704; -.
DR PathwayCommons; O75192; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR SignaLink; O75192; -.
DR BioGRID-ORCS; 8800; 9 hits in 1070 CRISPR screens.
DR GeneWiki; PEX11A; -.
DR GenomeRNAi; 8800; -.
DR Pharos; O75192; Tbio.
DR PRO; PR:O75192; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75192; protein.
DR Bgee; ENSG00000166821; Expressed in jejunal mucosa and 185 other tissues.
DR ExpressionAtlas; O75192; baseline and differential.
DR Genevisible; O75192; HS.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; IEA:Ensembl.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0044375; P:regulation of peroxisome size; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR InterPro; IPR008733; PEX11.
DR Pfam; PF05648; PEX11; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Peroxisome; Peroxisome biogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..247
FT /note="Peroxisomal membrane protein 11A"
FT /id="PRO_0000105964"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..219
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 220..239
FT /note="Required for homodimerization, interaction with
FT PEX11G, and peroxisomal localization"
FT /evidence="ECO:0000269|PubMed:20826455"
FT VAR_SEQ 58..89
FT /note="WFRLGNVVHAIQATEQSIHATDLVPRLCLTLA -> S (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054753"
FT MUTAGEN 9
FT /note="N->D: No effect on peroxisomal location."
FT /evidence="ECO:0000269|PubMed:9714566"
FT MUTAGEN 243..245
FT /note="KLK->SLS: No effect on peroxisomal location."
FT /evidence="ECO:0000269|PubMed:9714566"
SQ SEQUENCE 247 AA; 28353 MW; D904EC715271FF87 CRC64;
MDAFTRFTNQ TQGRDRLFRA TQYTCMLLRY LLEPKAGKEK VVMKLKKLES SVSTGRKWFR
LGNVVHAIQA TEQSIHATDL VPRLCLTLAN LNRVIYFICD TILWVRSVGL TSGINKEKWR
TRAAHHYYYS LLLSLVRDLY EISLQMKRVT CDRAKKEKSA SQDPLWFSVA EEETEWLQSF
LLLLFRSLKQ HPPLLLDTVK NLCDILNPLD QLGIYKSNPG IIGLGGLVSS IAGMITVAYP
QMKLKTR
