ID PEX10_HUMAN Reviewed; 326 AA. AC O60683; B3KWD8; Q5T095; Q9BW90; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 24-JAN-2024, entry version 192. DE RecName: Full=Peroxisome biogenesis factor 10 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000269|PubMed:24662292}; DE AltName: Full=Peroxin-10 {ECO:0000305}; DE AltName: Full=Peroxisomal biogenesis factor 10; DE AltName: Full=Peroxisome assembly protein 10; DE AltName: Full=RING finger protein 69; GN Name=PEX10 {ECO:0000303|PubMed:9683594, ECO:0000312|HGNC:HGNC:8851}; GN Synonyms=RNF69; 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 VARIANT PBD6B GLN-290. RX PubMed=9683594; DOI=10.1086/301963; RA Warren D.S., Morrell J.C., Moser H.W., Valle D., Gould S.J.; RT "Identification of PEX10, the gene defective in complementation group 7 of RT the peroxisome-biogenesis disorders."; RL Am. J. Hum. Genet. 63:347-359(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN PBD6A. RX PubMed=9700193; DOI=10.1093/hmg/7.9.1399; RA Okumoto K., Itoh R., Shimozawa N., Suzuki Y., Tamura S., Kondo N., RA Fujiki Y.; RT "Mutations in PEX10 is the cause of Zellweger peroxisome deficiency RT syndrome of complementation group B."; RL Hum. Mol. Genet. 7:1399-1405(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Caudate nucleus; 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 [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and 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 SUBCELLULAR LOCATION. RX PubMed=9922452; DOI=10.1083/jcb.144.2.255; RA South S.T., Gould S.J.; RT "Peroxisome synthesis in the absence of preexisting peroxisomes."; RL J. Cell Biol. 144:255-266(1999). RN [8] 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 [9] RP INTERACTION WITH PEX19. RX PubMed=11390669; DOI=10.1128/mcb.21.13.4413-4424.2001; RA Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.; RT "Human pex19p binds peroxisomal integral membrane proteins at regions RT distinct from their sorting sequences."; RL Mol. Cell. Biol. 21:4413-4424(2001). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, IDENTIFICATION RP IN THE PEX2-PEX10-PEX12 RETROTRANSLOCATION CHANNEL, MUTAGENESIS OF CYS-273 RP AND CYS-310, VARIANT PBD6B GLN-290, AND CHARACTERIZATION OF VARIANT PBD6B RP GLN-290. 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 [11] RP INVOLVEMENT IN PBD6B. RX PubMed=30022445; DOI=10.1007/s13760-018-0987-8; RA Kaya Oezcora G.D., Miyatake S., Matsumoto N., Canpolat M., Erdogan M., RA Bayramov R., Kumandas S.; RT "PEX10-related autosomal recessive cerebellar ataxia with hearing loss."; RL Acta Neurol. Belg. 120:429-432(2020). RN [12] RP VARIANT PBD6A 244-ARG--ARG-326 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 [13] RP VARIANT ALA-274, AND INVOLVEMENT IN PBD-CG7. RX PubMed=19105186; DOI=10.1002/humu.20932; RA Yik W.Y., Steinberg S.J., Moser A.B., Moser H.W., Hacia J.G.; RT "Identification of novel mutations and sequence variation in the Zellweger RT syndrome spectrum of peroxisome biogenesis disorders."; RL Hum. Mutat. 30:E467-E480(2009). RN [14] RP VARIANTS PBD6B 244-ARG--ARG-326 DEL AND GLN-311. RX PubMed=20695019; DOI=10.1002/ana.22035; RA Regal L., Ebberink M.S., Goemans N., Wanders R.J., De Meirleir L., RA Jaeken J., Schrooten M., Van Coster R., Waterham H.R.; RT "Mutations in PEX10 are a cause of autosomal recessive ataxia."; RL Ann. Neurol. 68:259-263(2010). RN [15] RP VARIANTS PBD6B 244-ARG--ARG-326 DEL; PHE-276 AND GLN-311. RX PubMed=27230853; DOI=10.1007/s00415-016-8167-3; RA Renaud M., Guissart C., Mallaret M., Ferdinandusse S., Cheillan D., RA Drouot N., Muller J., Claustres M., Tranchant C., Anheim M., Koenig M.; RT "Expanding the spectrum of PEX10-related peroxisomal biogenesis disorders: RT slowly progressive recessive ataxia."; RL J. Neurol. 263:1552-1558(2016). RN [16] RP VARIANT PBD6B ARG-177. RX PubMed=28784167; DOI=10.1186/s13256-017-1365-5; RA Blomqvist M., Ahlberg K., Lindgren J., Ferdinandusse S., Asin-Cayuela J.; RT "Identification of a novel mutation in PEX10 in a patient with attenuated RT Zellweger spectrum disorder: a case report."; RL J. Med. Case Rep. 11:218-218(2017). RN [17] RP VARIANT PBD6A PHE-296. RX PubMed=32069232; DOI=10.1515/jpem-2019-0194; RA Havali C., Dorum S., Akbas Y., Goeruekmez O., Hirfanoglu T.; RT "Two different missense mutations of PEX genes in two similar patients with RT severe Zellweger syndrome: an argument on the genotype-phenotype RT correlation."; RL J. Pediatr. Endocrinol. Metab. 33:437-441(2020). 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 PEX10 also regulates PEX5 recycling by acting as a E3 ubiquitin-protein CC ligase (PubMed:24662292). When PEX5 recycling is compromised, PEX10 CC catalyzes polyubiquitination of PEX5 during its passage through the CC retrotranslocation channel, leading to its degradation (By similarity). CC {ECO:0000250|UniProtKB:Q05568, ECO:0000269|PubMed:24662292}. 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:24662292}; CC -!- ACTIVITY REGULATION: The E3 ubiquitin-protein ligase activity is CC stimulated by PEX12. {ECO:0000269|PubMed:24662292}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:24662292}. CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel, CC composed of PEX2, PEX10 and PEX12 (PubMed:24662292). Interacts with CC PEX19 (PubMed:10704444, PubMed:11390669). {ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:24662292}. CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9922452}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60683-1; Sequence=Displayed; CC Name=2; CC IsoId=O60683-2; Sequence=VSP_005771; 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:G2Q0E2}. CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 7 (PBD- CC CG7) [MIM:614870]: 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 {ECO:0000269|PubMed:19105186}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 6A (PBD6A) [MIM:614870]: 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:17041890, ECO:0000269|PubMed:32069232, CC ECO:0000269|PubMed:9700193}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 6B (PBD6B) [MIM:614871]: 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:20695019, ECO:0000269|PubMed:24662292, CC ECO:0000269|PubMed:27230853, ECO:0000269|PubMed:28784167, CC ECO:0000269|PubMed:30022445, ECO:0000269|PubMed:9683594}. 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 -!- WEB RESOURCE: Name=dbPEX, PEX Gene Database; CC URL="https://databases.lovd.nl/shared/genes/PEX10"; 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; AF060502; AAC18133.1; -; mRNA. DR EMBL; AB013818; BAA87895.1; -; mRNA. DR EMBL; AK124816; BAG54100.1; -; mRNA. DR EMBL; AL513477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471183; EAW56105.1; -; Genomic_DNA. DR EMBL; BC000543; AAH00543.1; -; mRNA. DR EMBL; BC018198; AAH18198.1; -; mRNA. DR CCDS; CCDS41.1; -. [O60683-2] DR CCDS; CCDS44045.1; -. [O60683-1] DR RefSeq; NP_002608.1; NM_002617.3. [O60683-1] DR RefSeq; NP_722540.1; NM_153818.1. [O60683-2] DR AlphaFoldDB; O60683; -. DR SMR; O60683; -. DR BioGRID; 111215; 33. DR ComplexPortal; CPX-2649; PEX2-PEX10-PEX12 E3 ubiquitin ligase complex. DR IntAct; O60683; 10. DR STRING; 9606.ENSP00000288774; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR iPTMnet; O60683; -. DR PhosphoSitePlus; O60683; -. DR BioMuta; PEX10; -. DR EPD; O60683; -. DR jPOST; O60683; -. DR MassIVE; O60683; -. DR MaxQB; O60683; -. DR PaxDb; 9606-ENSP00000288774; -. DR PeptideAtlas; O60683; -. DR ProteomicsDB; 49525; -. [O60683-1] DR ProteomicsDB; 49526; -. [O60683-2] DR Pumba; O60683; -. DR Antibodypedia; 26727; 202 antibodies from 27 providers. DR DNASU; 5192; -. DR Ensembl; ENST00000288774.8; ENSP00000288774.3; ENSG00000157911.11. [O60683-2] DR Ensembl; ENST00000447513.7; ENSP00000407922.2; ENSG00000157911.11. [O60683-1] DR GeneID; 5192; -. DR KEGG; hsa:5192; -. DR MANE-Select; ENST00000447513.7; ENSP00000407922.2; NM_002617.4; NP_002608.1. DR UCSC; uc001ajg.4; human. [O60683-1] DR AGR; HGNC:8851; -. DR CTD; 5192; -. DR DisGeNET; 5192; -. DR GeneCards; PEX10; -. DR GeneReviews; PEX10; -. DR HGNC; HGNC:8851; PEX10. DR HPA; ENSG00000157911; Low tissue specificity. DR MalaCards; PEX10; -. DR MIM; 602859; gene. DR MIM; 614870; phenotype. DR MIM; 614871; phenotype. DR neXtProt; NX_O60683; -. DR OpenTargets; ENSG00000157911; -. DR Orphanet; 247815; Autosomal recessive ataxia due to PEX10 deficiency. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA33193; -. DR VEuPathDB; HostDB:ENSG00000157911; -. DR eggNOG; KOG0317; Eukaryota. DR GeneTree; ENSGT00510000048446; -. DR HOGENOM; CLU_041707_1_0_1; -. DR InParanoid; O60683; -. DR OMA; YCDVVQL; -. DR OrthoDB; 38742at2759; -. DR PhylomeDB; O60683; -. DR TreeFam; TF326491; -. DR PathwayCommons; O60683; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; O60683; -. DR SIGNOR; O60683; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 5192; 67 hits in 1197 CRISPR screens. DR ChiTaRS; PEX10; human. DR GeneWiki; PEX10; -. DR GenomeRNAi; 5192; -. DR Pharos; O60683; Tbio. DR PRO; PR:O60683; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O60683; Protein. DR Bgee; ENSG00000157911; Expressed in parotid gland and 185 other cell types or tissues. DR ExpressionAtlas; O60683; baseline and differential. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:MGI. 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; NAS:UniProtKB. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProt. DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProt. DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA: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:0000209; P:protein polyubiquitination; IDA:UniProt. DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProt. DR CDD; cd16527; RING-HC_PEX10; 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; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR23350; PEROXISOME ASSEMBLY PROTEIN 10; 1. DR PANTHER; PTHR23350:SF0; PEROXISOME BIOGENESIS FACTOR 10; 1. DR Pfam; PF04757; Pex2_Pex12; 1. DR Pfam; PF13639; zf-RING_2; 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; O60683; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Membrane; Metal-binding; Peroxisome; KW Peroxisome biogenesis; Peroxisome biogenesis disorder; Protein transport; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; KW Transport; Ubl conjugation pathway; Zellweger syndrome; Zinc; Zinc-finger. FT CHAIN 1..326 FT /note="Peroxisome biogenesis factor 10" FT /id="PRO_0000056376" FT TOPO_DOM 1..7 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TRANSMEM 8..37 FT /note="Helical; Name=TM1" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TOPO_DOM 38 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TRANSMEM 39..60 FT /note="Helical; Name=TM2" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TOPO_DOM 61..89 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TRANSMEM 90..122 FT /note="Helical; Name=TM3" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TOPO_DOM 123..147 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TRANSMEM 148..185 FT /note="Helical; Name=TM4" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TOPO_DOM 186..216 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TRANSMEM 217..236 FT /note="Helical; Name=TM5" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT TOPO_DOM 237..326 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT ZN_FING 273..311 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:24662292" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 288 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 290 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 307 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:G2Q0E2" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000305|PubMed:24662292" FT VAR_SEQ 200 FT /note="Y -> YQALRPDPLRVLMSVAPSALQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_005771" FT VARIANT 177 FT /note="L -> R (in PBD6B)" FT /evidence="ECO:0000269|PubMed:28784167" FT /id="VAR_087145" FT VARIANT 244..326 FT /note="Missing (in PBD6B and PBD6A)" FT /evidence="ECO:0000269|PubMed:17041890, FT ECO:0000269|PubMed:20695019, ECO:0000269|PubMed:27230853" FT /id="VAR_087146" FT VARIANT 274 FT /note="T -> A (in dbSNP:rs34154371)" FT /evidence="ECO:0000269|PubMed:19105186" FT /id="VAR_058388" FT VARIANT 276 FT /note="C -> F (in PBD6B)" FT /evidence="ECO:0000269|PubMed:27230853" FT /id="VAR_087147" FT VARIANT 290 FT /note="H -> Q (in PBD6B; neonatal adrenoleukodystrophy; FT abolished E3 ubiquitin-protein ligase activity; FT dbSNP:rs61752095)" FT /evidence="ECO:0000269|PubMed:24662292, FT ECO:0000269|PubMed:9683594" FT /id="VAR_007805" FT VARIANT 296 FT /note="C -> F (in PBD6A)" FT /evidence="ECO:0000269|PubMed:32069232" FT /id="VAR_087148" FT VARIANT 311 FT /note="R -> Q (in PBD6B)" FT /evidence="ECO:0000269|PubMed:20695019, FT ECO:0000269|PubMed:27230853" FT /id="VAR_087149" FT MUTAGEN 273 FT /note="C->A: Abolished E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:24662292" FT MUTAGEN 310 FT /note="C->G: Abolished E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:24662292" SQ SEQUENCE 326 AA; 37069 MW; 9CF2CE5E4C797799 CRC64; MAPAAASPPE VIRAAQKDEY YRGGLRSAAG GALHSLAGAR KWLEWRKEVE LLSDVAYFGL TTLAGYQTLG EEYVSIIQVD PSRIHVPSSL RRGVLVTLHA VLPYLLDKAL LPLEQELQAD PDSGRPLQGS LGPGGRGCSG ARRWMRHHTA TLTEQQRRAL LRAVFVLRQG LACLQRLHVA WFYIHGVFYH LAKRLTGITY LRVRSLPGED LRARVSYRLL GVISLLHLVL SMGLQLYGFR QRQRARKEWR LHRGLSHRRA SLEERAVSRN PLCTLCLEER RHPTATPCGH LFCWECITAW CSSKAECPLC REKFPPQKLI YLRHYR //