PEX10_HUMAN
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 03-AUG-2022, entry version 184.
DE RecName: Full=Peroxisome biogenesis factor 10;
DE AltName: Full=Peroxin-10;
DE AltName: Full=Peroxisomal biogenesis factor 10;
DE AltName: Full=Peroxisome assembly protein 10;
DE AltName: Full=RING finger protein 69;
GN Name=PEX10; 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 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 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 [9]
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).
CC -!- FUNCTION: Somewhat implicated in the biogenesis of peroxisomes.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:11390669}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
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 -!- 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: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:9683594}. Note=The disease is caused by variants
CC affecting the gene represented in this 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";
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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 BioGRID; 111215; 31.
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 PeptideAtlas; O60683; -.
DR PRIDE; O60683; -.
DR ProteomicsDB; 49525; -. [O60683-1]
DR ProteomicsDB; 49526; -. [O60683-2]
DR Antibodypedia; 26727; 174 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 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; RNWIKYN; -.
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 BioGRID-ORCS; 5192; 64 hits in 1119 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 183 other tissues.
DR ExpressionAtlas; O60683; baseline and differential.
DR Genevisible; O60683; HS.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Membrane; Metal-binding; Peroxisome;
KW Peroxisome biogenesis; Peroxisome biogenesis disorder; Reference proteome;
KW Zellweger syndrome; Zinc; Zinc-finger.
FT CHAIN 1..326
FT /note="Peroxisome biogenesis factor 10"
FT /id="PRO_0000056376"
FT ZN_FING 273..311
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 200
FT /note="Y -> YQALRPDPLRVLMSVAPSALQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005771"
FT VARIANT 274
FT /note="T -> A (in dbSNP:rs34154371)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058388"
FT VARIANT 290
FT /note="H -> Q (in PBD6B; neonatal adrenoleukodystrophy;
FT dbSNP:rs61752095)"
FT /evidence="ECO:0000269|PubMed:9683594"
FT /id="VAR_007805"
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
