ID PEX2_HUMAN Reviewed; 305 AA. AC P28328; Q567S6; Q9BW41; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=Peroxisome biogenesis factor 2 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000269|PubMed:34903883}; DE EC=2.3.2.36 {ECO:0000250|UniProtKB:P32800}; DE AltName: Full=35 kDa peroxisomal membrane protein {ECO:0000303|PubMed:10891359}; DE AltName: Full=Peroxin-2 {ECO:0000305}; DE AltName: Full=Peroxisomal membrane protein 3; DE AltName: Full=Peroxisome assembly factor 1 {ECO:0000303|PubMed:1546315}; DE Short=PAF-1 {ECO:0000303|PubMed:1546315}; DE AltName: Full=RING finger protein 72; GN Name=PEX2 {ECO:0000303|PubMed:10891359, ECO:0000312|HGNC:HGNC:9717}; GN Synonyms=PAF1 {ECO:0000303|PubMed:1546315}, PMP3, PMP35, PXMP3, RNF72; 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], VARIANT ARG-184, AND INVOLVEMENT IN PBD5A. RC TISSUE=Liver; RX PubMed=1546315; DOI=10.1126/science.1546315; RA Shimozawa N., Tsukamoto T., Suzuki Y., Orii T., Shirayoshi Y., Mori T., RA Fujiki Y.; RT "A human gene responsible for Zellweger syndrome that affects peroxisome RT assembly."; RL Science 255:1132-1134(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-184. RX PubMed=10891359; DOI=10.1006/bbrc.2000.3039; RA Biermanns M., Gaertner J.; RT "Genomic organization and characterization of human PEX2 encoding a 35-kDa RT peroxisomal membrane protein."; RL Biochem. Biophys. Res. Commun. 273:985-990(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-184. RC TISSUE=Liver; RA Gartner J.; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-184. RC TISSUE=Kidney, and Liver; 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 [6] RP SUBCELLULAR LOCATION. RX PubMed=12751901; DOI=10.1078/0171-9335-00310; RA Biermanns M., von Laar J., Brosius U., Gaertner J.; RT "The peroxisomal membrane targeting elements of human peroxin 2 (PEX2)."; RL Eur. J. Cell Biol. 82:155-162(2003). RN [7] RP DOMAIN RING FINGER. RX PubMed=1426230; DOI=10.1016/0014-5793(92)81397-5; RA Patarca R., Fletcher M.A.; RT "Ring finger in the peroxisome assembly factor-1."; RL FEBS Lett. 312:1-2(1992). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, 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 [9] RP FUNCTION, PATHWAY, AND IDENTIFICATION IN THE PEX2-PEX10-PEX12 RP RETROTRANSLOCATION CHANNEL. RX PubMed=24662292; DOI=10.1074/jbc.m113.527937; RA Okumoto K., Noda H., Fujiki Y.; RT "Distinct modes of ubiquitination of peroxisome-targeting signal type 1 RT (PTS1) receptor Pex5p regulate PTS1 protein import."; RL J. Biol. Chem. 289:14089-14108(2014). RN [10] RP FUNCTION, AND PATHWAY. RX PubMed=27597759; DOI=10.1083/jcb.201511034; RA Sargent G., van Zutphen T., Shatseva T., Zhang L., Di Giovanni V., RA Bandsma R., Kim P.K.; RT "PEX2 is the E3 ubiquitin ligase required for pexophagy during RT starvation."; RL J. Cell Biol. 214:677-690(2016). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND DISULFIDE BONDS. RX PubMed=34903883; DOI=10.1038/s42255-021-00489-2; RA Ding L., Sun W., Balaz M., He A., Klug M., Wieland S., Caiazzo R., RA Raverdy V., Pattou F., Lefebvre P., Lodhi I.J., Staels B., Heim M., RA Wolfrum C.; RT "Peroxisomal beta-oxidation acts as a sensor for intracellular fatty acids RT and regulates lipolysis."; RL Nat. Metab. 3:1648-1661(2021). RN [12] RP VARIANT PBD5B LYS-55. RX PubMed=10528859; DOI=10.1136/jmg.36.10.779; RA Shimozawa N., Imamura A., Zhang Z., Suzuki Y., Orii T., Tsukamoto T., RA Osumi T., Fujiki Y., Wanders R.J.A., Besley G., Kondo N.; RT "Defective PEX gene products correlate with the protein import, biochemical RT abnormalities, and phenotypic heterogeneity in peroxisome biogenesis RT disorders."; RL J. Med. Genet. 36:779-781(1999). RN [13] RP VARIANTS PBD5A 119-ARG--LEU-305 DEL AND ARG-247, AND VARIANT PBD5B RP 223-TRP--LEU-305 DEL. RX PubMed=14630978; DOI=10.1203/01.pdr.0000106862.83469.8d; RA Gootjes J., Elpeleg O., Eyskens F., Mandel H., Mitanchez D., Shimozawa N., RA Suzuki Y., Waterham H.R., Wanders R.J.; RT "Novel mutations in the PEX2 gene of four unrelated patients with a RT peroxisome biogenesis disorder."; RL Pediatr. Res. 55:431-436(2004). RN [14] RP VARIANT PBD5A 39-GLN--LEU-305 DEL. RX PubMed=17041890; DOI=10.1002/humu.9462; RA Krause C., Rosewich H., Thanos M., Gaertner J.; RT "Identification of novel mutations in PEX2, PEX6, PEX10, PEX12, and PEX13 RT in Zellweger spectrum patients."; RL Hum. Mutat. 27:1157-1157(2006). RN [15] RP INVOLVEMENT IN PBD5B. RX PubMed=21392394; DOI=10.1186/1750-1172-6-8; RA Sevin C., Ferdinandusse S., Waterham H.R., Wanders R.J., Aubourg P.; RT "Autosomal recessive cerebellar ataxia caused by mutations in the PEX2 RT gene."; RL Orphanet J. Rare Dis. 6:8-8(2011). RN [16] RP VARIANT PBD5B 119-ARG--LEU-305 DEL. RX PubMed=23430938; DOI=10.1007/8904_2011_102; RA Mignarri A., Vinciguerra C., Giorgio A., Ferdinandusse S., Waterham H., RA Wanders R., Bertini E., Dotti M.T., Federico A.; RT "Zellweger spectrum disorder with mild phenotype caused by PEX2 gene RT mutations."; RL JIMD Rep. 6:43-46(2012). CC -!- FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation CC channel required for peroxisome organization by mediating export of the CC PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 CC recycling (PubMed:24662292). The retrotranslocation channel is composed CC of PEX2, PEX10 and PEX12; each subunit contributing transmembrane CC segments that coassemble into an open channel that specifically allows CC the passage of PEX5 through the peroxisomal membrane (By similarity). CC PEX2 also regulates peroxisome organization by acting as a E3 CC ubiquitin-protein ligase (By similarity). PEX2 ubiquitinates PEX5 CC during its passage through the retrotranslocation channel: catalyzes CC monoubiquitination of PEX5 at 'Cys-11', a modification that acts as a CC signal for PEX5 extraction into the cytosol (By similarity). Required CC for pexophagy in response to starvation by mediating ubiquitination of CC peroxisomal proteins, such as PEX5 and ABCD3/PMP70 (PubMed:27597759). CC Also involved in the response to reactive oxygen species (ROS) by CC mediating 'Lys-48'-linked polyubiquitination and subsequent degradation CC of PNPLA2/ATGL, thereby regulating lipolysis (PubMed:34903883). CC {ECO:0000250|UniProtKB:P32800, ECO:0000269|PubMed:24662292, CC ECO:0000269|PubMed:27597759, ECO:0000269|PubMed:34903883}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + CC [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36; CC Evidence={ECO:0000250|UniProtKB:P32800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:34903883}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:24662292, ECO:0000269|PubMed:27597759}. CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel, CC composed of PEX2, PEX10 and PEX12. {ECO:0000269|PubMed:24662292}. CC -!- INTERACTION: CC P28328; P40855: PEX19; NbExp=3; IntAct=EBI-713978, EBI-594747; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane CC {ECO:0000269|PubMed:12751901}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- DOMAIN: The three subunits of the retrotranslocation channel (PEX2, CC PEX10 and PEX12) coassemble in the membrane into a channel with an open CC 10 Angstrom pore (By similarity). The RING-type zinc-fingers that CC catalyze PEX5 receptor ubiquitination are positioned above the pore on CC the cytosolic side of the complex (By similarity). CC {ECO:0000250|UniProtKB:G2Q1C9}. CC -!- PTM: Forms intramolecular and intermolecular disulfide bonds in CC response to reactive oxygen species (ROS), promoting higher stability. CC {ECO:0000269|PubMed:34903883}. CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 5 (PBD- CC CG5) [MIM:614866]: A peroxisomal disorder arising from a failure of CC protein import into the peroxisomal membrane or matrix. The peroxisome CC biogenesis disorders (PBD group) are genetically heterogeneous with at CC least 14 distinct genetic groups as concluded from complementation CC studies. Include disorders are: Zellweger syndrome (ZWS), neonatal CC adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and CC classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and CC IRD are distinct from RCDP and constitute a clinical continuum of CC overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS). CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 5A (PBD5A) [MIM:614866]: A CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease CC spectrum and clinically characterized by severe neurologic dysfunction CC with profound psychomotor retardation, severe hypotonia and neonatal CC seizures, craniofacial abnormalities, liver dysfunction, and CC biochemically by the absence of peroxisomes. Additional features CC include cardiovascular and skeletal defects, renal cysts, ocular CC abnormalities, and hearing impairment. Most severely affected CC individuals with the classic form of the disease (classic Zellweger CC syndrome) die within the first year of life. CC {ECO:0000269|PubMed:14630978, ECO:0000269|PubMed:1546315, CC ECO:0000269|PubMed:17041890}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 5B (PBD5B) [MIM:614867]: A CC peroxisome biogenesis disorder that includes neonatal CC adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two CC milder manifestations of the Zellweger disease spectrum. The clinical CC course of patients with the NALD and IRD presentation is variable and CC may include developmental delay, hypotonia, liver dysfunction, CC sensorineural hearing loss, retinal dystrophy and vision impairment. CC Children with the NALD presentation may reach their teens, while CC patients with the IRD presentation may reach adulthood. The clinical CC conditions are often slowly progressive in particular with respect to CC loss of hearing and vision. The biochemical abnormalities include CC accumulation of phytanic acid, very long chain fatty acids (VLCFA), CC di- and trihydroxycholestanoic acid and pipecolic acid. CC {ECO:0000269|PubMed:10528859, ECO:0000269|PubMed:14630978, CC ECO:0000269|PubMed:21392394, ECO:0000269|PubMed:23430938}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M86852; AAC12785.1; -; mRNA. DR EMBL; AF133826; AAF97687.1; -; Genomic_DNA. DR EMBL; M85038; AAA60141.1; -; mRNA. DR EMBL; AC090810; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000661; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC005375; AAH05375.1; -; mRNA. DR EMBL; BC093043; AAH93043.1; -; mRNA. DR CCDS; CCDS6221.1; -. DR PIR; A41812; A41812. DR RefSeq; NP_000309.1; NM_000318.2. DR RefSeq; NP_001073336.1; NM_001079867.1. DR RefSeq; NP_001165557.1; NM_001172086.1. DR RefSeq; NP_001165558.1; NM_001172087.1. DR AlphaFoldDB; P28328; -. DR SMR; P28328; -. DR BioGRID; 111786; 22. DR ComplexPortal; CPX-2649; PEX2-PEX10-PEX12 E3 ubiquitin ligase complex. DR IntAct; P28328; 11. DR MINT; P28328; -. DR STRING; 9606.ENSP00000349543; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR iPTMnet; P28328; -. DR PhosphoSitePlus; P28328; -. DR BioMuta; PEX2; -. DR DMDM; 281185478; -. DR EPD; P28328; -. DR jPOST; P28328; -. DR MassIVE; P28328; -. DR MaxQB; P28328; -. DR PaxDb; 9606-ENSP00000349543; -. DR PeptideAtlas; P28328; -. DR ProteomicsDB; 54465; -. DR Pumba; P28328; -. DR Antibodypedia; 2570; 256 antibodies from 33 providers. DR DNASU; 5828; -. DR Ensembl; ENST00000357039.9; ENSP00000349543.4; ENSG00000164751.15. DR Ensembl; ENST00000520103.5; ENSP00000428590.1; ENSG00000164751.15. DR Ensembl; ENST00000522527.5; ENSP00000428638.1; ENSG00000164751.15. DR GeneID; 5828; -. DR KEGG; hsa:5828; -. DR MANE-Select; ENST00000357039.9; ENSP00000349543.4; NM_000318.3; NP_000309.2. DR UCSC; uc003yax.4; human. DR AGR; HGNC:9717; -. DR CTD; 5828; -. DR DisGeNET; 5828; -. DR GeneCards; PEX2; -. DR GeneReviews; PEX2; -. DR HGNC; HGNC:9717; PEX2. DR HPA; ENSG00000164751; Low tissue specificity. DR MalaCards; PEX2; -. DR MIM; 170993; gene. DR MIM; 614866; phenotype. DR MIM; 614867; phenotype. DR neXtProt; NX_P28328; -. DR OpenTargets; ENSG00000164751; -. DR Orphanet; 642965; Autosomal recessive ataxia due to PEX2 deficiency. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA34060; -. DR VEuPathDB; HostDB:ENSG00000164751; -. DR eggNOG; KOG2879; Eukaryota. DR GeneTree; ENSGT00390000001846; -. DR HOGENOM; CLU_024591_3_1_1; -. DR InParanoid; P28328; -. DR OMA; YLICTVG; -. DR OrthoDB; 64567at2759; -. DR PhylomeDB; P28328; -. DR TreeFam; TF105312; -. DR PathwayCommons; P28328; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; P28328; -. DR SIGNOR; P28328; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 5828; 35 hits in 1194 CRISPR screens. DR ChiTaRS; PEX2; human. DR GeneWiki; PXMP3; -. DR GenomeRNAi; 5828; -. DR Pharos; P28328; Tbio. DR PRO; PR:P28328; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P28328; Protein. DR Bgee; ENSG00000164751; Expressed in seminal vesicle and 203 other cell types or tissues. DR ExpressionAtlas; P28328; baseline and differential. DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProt. DR GO; GO:0008320; F:protein transmembrane transporter activity; ISS:UniProt. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProt. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB. DR GO; GO:0000425; P:pexophagy; IDA:UniProtKB. DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB. DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB. DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IDA:UniProtKB. DR GO; GO:0044721; P:protein import into peroxisome matrix, substrate release; ISS:UniProt. DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProt. DR GO; GO:1990928; P:response to amino acid starvation; IDA:UniProtKB. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB. DR CDD; cd16526; RING-HC_PEX2; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR025654; PEX2/10. DR InterPro; IPR006845; Pex_N. DR InterPro; IPR045859; RING-HC_PEX2. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR48178; PEROXISOME BIOGENESIS FACTOR 2; 1. DR PANTHER; PTHR48178:SF1; PEROXISOME BIOGENESIS FACTOR 2; 1. DR Pfam; PF04757; Pex2_Pex12; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; P28328; HS. PE 1: Evidence at protein level; KW Acetylation; Disease variant; Disulfide bond; Membrane; Metal-binding; KW Peroxisome; Peroxisome biogenesis; Peroxisome biogenesis disorder; KW Protein transport; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation pathway; KW Zellweger syndrome; Zinc; Zinc-finger. FT CHAIN 1..305 FT /note="Peroxisome biogenesis factor 2" FT /id="PRO_0000056369" FT TOPO_DOM 1..15 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TRANSMEM 16..42 FT /note="Helical; Name=TM1" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TOPO_DOM 43..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TRANSMEM 49..74 FT /note="Helical; Name=TM2" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TOPO_DOM 75..98 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TRANSMEM 99..125 FT /note="Helical; Name=TM3" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TOPO_DOM 126..133 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TRANSMEM 134..160 FT /note="Helical; Name=TM4" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TOPO_DOM 161..187 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TRANSMEM 188..211 FT /note="Helical; Name=TM5" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT TOPO_DOM 212..305 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT ZN_FING 244..284 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 280 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT BINDING 283 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q1C9" FT MOD_RES 84 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 39..305 FT /note="Missing (in PBD5A)" FT /evidence="ECO:0000269|PubMed:17041890" FT /id="VAR_087141" FT VARIANT 55 FT /note="E -> K (in PBD5B; infantile Refsum disease; FT dbSNP:rs61752119)" FT /evidence="ECO:0000269|PubMed:10528859" FT /id="VAR_011389" FT VARIANT 119..305 FT /note="Missing (in PBD5B and PBD5A)" FT /evidence="ECO:0000269|PubMed:14630978, FT ECO:0000269|PubMed:23430938" FT /id="VAR_087142" FT VARIANT 184 FT /note="C -> R (in dbSNP:rs10087163)" FT /evidence="ECO:0000269|PubMed:10891359, FT ECO:0000269|PubMed:1546315, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.3" FT /id="VAR_060784" FT VARIANT 223..305 FT /note="Missing (in PBD5B)" FT /evidence="ECO:0000269|PubMed:14630978" FT /id="VAR_087143" FT VARIANT 247 FT /note="C -> R (in PBD5A)" FT /evidence="ECO:0000269|PubMed:14630978" FT /id="VAR_087144" SQ SEQUENCE 305 AA; 34843 MW; F624F93C613FF2DB CRC64; MASRKENAKS ANRVLRISQL DALELNKALE QLVWSQFTQC FHGFKPGLLA RFEPEVKACL WVFLWRFTIY SKNATVGQSV LNIKYKNDFS PNLRYQPPSK NQKIWYAVCT IGGRWLEERC YDLFRNHHLA SFGKVKQCVN FVIGLLKLGG LINFLIFLQR GKFATLTERL LGIHSVFCKP QNICEVGFEY MNRELLWHGF AEFLIFLLPL INVQKLKAKL SSWCIPLTGA PNSDNTLATS GKECALCGEW PTMPHTIGCE HIFCYFCAKS SFLFDVYFTC PKCGTEVHSL QPLKSGIEMS EVNAL //