PEX6_HUMAN
ID PEX6_HUMAN Reviewed; 980 AA.
AC Q13608; Q5T8W1; Q8WYQ0; Q8WYQ1; Q8WYQ2; Q99476;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peroxisome assembly factor 2;
DE Short=PAF-2;
DE AltName: Full=Peroxin-6;
DE AltName: Full=Peroxisomal biogenesis factor 6;
DE AltName: Full=Peroxisomal-type ATPase 1;
GN Name=PEX6; Synonyms=PXAAA1;
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 [GENOMIC DNA], AND INVOLVEMENT IN PBD4A.
RX PubMed=8670792; DOI=10.1002/j.1460-2075.1996.tb00654.x;
RA Yahraus T., Braverman N., Dodt G., Kalish J.E., Morrell J.C., Moser H.W.,
RA Valle D., Gould S.J.;
RT "The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a
RT cytoplasmic ATPase required for stability of the PTS1 receptor.";
RL EMBO J. 15:2914-2923(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8940266;
RA Fukuda S., Shimozawa N., Suzuki Y., Zhang Z., Tomatsu S., Tsukamoto T.,
RA Hashiguchi N., Osumi T., Masuno M., Imaizumi K., Kuroki Y., Fujiki Y.,
RA Orii T., Kondo N.;
RT "Human peroxisome assembly factor-2 (PAF-2): a gene responsible for group C
RT peroxisome biogenesis disorder in humans.";
RL Am. J. Hum. Genet. 59:1210-1220(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PBD4A GLN-812 AND TRP-812.
RX PubMed=10408779;
RX DOI=10.1002/(sici)1098-1004(1999)13:6<487::aid-humu9>3.0.co;2-t;
RA Zhang Z., Suzuki Y., Shimozawa N., Fukuda S., Imamura A., Tsukamoto T.,
RA Osumi T., Fujiki Y., Orii T., Wanders R.J.A., Barth P.G., Moser H.W.,
RA Paton B.C., Besley G.T., Kondo N.;
RT "Genomic structure and identification of 11 novel mutations of the PEX6
RT 'peroxisome assembly factor-2' gene in patients with peroxisome biogenesis
RT disorders.";
RL Hum. Mutat. 13:487-496(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION,
RP VARIANT GLN-939, INVOLVEMENT IN PBD4B, AND ALTERNATIVE SPLICING.
RX PubMed=11355018; DOI=10.1007/s100380170078;
RA Matsumoto N., Tamura S., Moser A., Moser H.W., Braverman N., Suzuki Y.,
RA Shimozawa N., Kondo N., Fujiki Y.;
RT "The peroxin Pex6p gene is impaired in peroxisomal biogenesis disorders of
RT complementation group 6.";
RL J. Hum. Genet. 46:273-277(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [9]
RP INTERACTION WITH PEX26 AND PEX1.
RX PubMed=12717447; DOI=10.1038/ncb982;
RA Matsumoto N., Tamura S., Fujiki Y.;
RT "The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase
RT complexes to peroxisomes.";
RL Nat. Cell Biol. 5:454-460(2003).
RN [10]
RP INVOLVEMENT IN PBD-CG4, INVOLVEMENT IN HMLR2, VARIANTS PBD-CG4 THR-849;
RP GLN-860 AND TRP-860, VARIANTS HMLR2 LEU-274 AND GLN-601, AND VARIANTS
RP PRO-79; VAL-809; ILE-882; SER-924 AND GLN-939.
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 [11]
RP INVOLVEMENT IN PBD-CG4, AND VARIANT PBD-CG4 PRO-534.
RX PubMed=21937992; DOI=10.1038/nature10423;
RA Najmabadi H., Hu H., Garshasbi M., Zemojtel T., Abedini S.S., Chen W.,
RA Hosseini M., Behjati F., Haas S., Jamali P., Zecha A., Mohseni M.,
RA Puettmann L., Vahid L.N., Jensen C., Moheb L.A., Bienek M., Larti F.,
RA Mueller I., Weissmann R., Darvish H., Wrogemann K., Hadavi V.,
RA Lipkowitz B., Esmaeeli-Nieh S., Wieczorek D., Kariminejad R.,
RA Firouzabadi S.G., Cohen M., Fattahi Z., Rost I., Mojahedi F., Hertzberg C.,
RA Dehghan A., Rajab A., Banavandi M.J., Hoffer J., Falah M., Musante L.,
RA Kalscheuer V., Ullmann R., Kuss A.W., Tzschach A., Kahrizi K., Ropers H.H.;
RT "Deep sequencing reveals 50 novel genes for recessive cognitive
RT disorders.";
RL Nature 478:57-63(2011).
RN [12]
RP INTERACTION WITH ZFAND6.
RX PubMed=21980954; DOI=10.1111/j.1600-0854.2011.01298.x;
RA Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.;
RT "AWP1/ZFAND6 functions in Pex5 export by interacting with cys-
RT monoubiquitinated Pex5 and Pex6 AAA ATPase.";
RL Traffic 13:168-183(2012).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-119, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP INVOLVEMENT IN HMLR2, VARIANTS HMLR2 LEU-274; GLN-601 AND TRP-644, AND
RP CHARACTERIZATION OF VARIANTS HMLR2 LEU-274; GLN-601 AND TRP-644.
RX PubMed=26387595; DOI=10.1016/j.ajhg.2015.08.011;
RA Ratbi I., Falkenberg K.D., Sommen M., Al-Sheqaih N., Guaoua S.,
RA Vandeweyer G., Urquhart J.E., Chandler K.E., Williams S.G., Roberts N.A.,
RA El Alloussi M., Black G.C., Ferdinandusse S., Ramdi H., Heimler A.,
RA Fryer A., Lynch S.A., Cooper N., Ong K.R., Smith C.E., Inglehearn C.F.,
RA Mighell A.J., Elcock C., Poulter J.A., Tischkowitz M., Davies S.J.,
RA Sefiani A., Mironov A.A., Newman W.G., Waterham H.R., Van Camp G.;
RT "Heimler syndrome is caused by hypomorphic mutations in the peroxisome-
RT biogenesis genes PEX1 and PEX6.";
RL Am. J. Hum. Genet. 97:535-545(2015).
RN [15]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT PBD-CG4 VAL-413.
RX PubMed=26593283; DOI=10.1002/humu.22934;
RA Zaki M.S., Heller R., Thoenes M., Nuernberg G., Stern-Schneider G.,
RA Nuernberg P., Karnati S., Swan D., Fateen E., Nagel-Wolfrum K.,
RA Mostafa M.I., Thiele H., Wolfrum U., Baumgart-Vogt E., Bolz H.J.;
RT "PEX6 is expressed in photoreceptor cilia and mutated in deafblindness with
RT enamel dysplasia and microcephaly.";
RL Hum. Mutat. 37:170-174(2016).
RN [16]
RP VARIANTS HMLR2 GLY-92; LEU-99; LEU-218; ILE-572; GLN-601 AND PHE-905.
RX PubMed=27302843; DOI=10.1038/ejhg.2016.62;
RA Smith C.E., Poulter J.A., Levin A.V., Capasso J.E., Price S., Ben-Yosef T.,
RA Sharony R., Newman W.G., Shore R.C., Brookes S.J., Mighell A.J.,
RA Inglehearn C.F.;
RT "Spectrum of PEX1 and PEX6 variants in Heimler syndrome.";
RL Eur. J. Hum. Genet. 24:1565-1571(2016).
CC -!- FUNCTION: Involved in peroxisome biosynthesis. Required for stability
CC of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes,
CC possibly to form heteromeric AAA ATPase complexes required for the
CC import of proteins into peroxisomes.
CC -!- SUBUNIT: Interacts directly with PEX26 and PEX1. Mediates the indirect
CC interaction between PEX1 and PEX26. Interacts with ZFAND6.
CC {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:21980954}.
CC -!- INTERACTION:
CC Q13608; O43933: PEX1; NbExp=2; IntAct=EBI-988581, EBI-988601;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane
CC {ECO:0000269|PubMed:11355018}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:26593283}. Note=Associated with
CC peroxisomal membranes. Localized at the base of the outer segment of
CC photoreceptor cells (PubMed:26593283). {ECO:0000269|PubMed:26593283}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13608-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13608-2; Sequence=VSP_057138, VSP_057139;
CC Name=3;
CC IsoId=Q13608-3; Sequence=VSP_057137;
CC -!- TISSUE SPECIFICITY: Expressed in the retina, at higher levels in the
CC photoreceptor layer at the joint between the outer and inner segments.
CC {ECO:0000269|PubMed:26593283}.
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 4 (PBD-
CC CG4) [MIM:614862]: 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, ECO:0000269|PubMed:21937992,
CC ECO:0000269|PubMed:26593283}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 4A (PBD4A) [MIM:614862]: 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:10408779, ECO:0000269|PubMed:8670792}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 4B (PBD4B) [MIM:614863]: 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:11355018}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Heimler syndrome 2 (HMLR2) [MIM:616617]: A form of Heimler
CC syndrome, a very mild peroxisome biogenesis disorder characterized by
CC sensorineural hearing loss, amelogenesis imperfecta resulting in enamel
CC hyoplasia of the secondary dentition, nail defects, and occasional or
CC late-onset retinal pigmentation abnormalities.
CC {ECO:0000269|PubMed:19105186, ECO:0000269|PubMed:26387595,
CC ECO:0000269|PubMed:27302843}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbPEX, PEX Gene Database;
CC URL="https://databases.lovd.nl/shared/genes/PEX6";
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DR EMBL; U56602; AAC50655.1; -; Genomic_DNA.
DR EMBL; D83703; BAA12069.1; -; mRNA.
DR EMBL; AF108098; AAF62564.1; -; Genomic_DNA.
DR EMBL; AF108095; AAF62564.1; JOINED; Genomic_DNA.
DR EMBL; AF108096; AAF62564.1; JOINED; Genomic_DNA.
DR EMBL; AF108097; AAF62564.1; JOINED; Genomic_DNA.
DR EMBL; AB051076; BAB83046.1; -; mRNA.
DR EMBL; AB051077; BAB83047.1; -; mRNA.
DR EMBL; AB051078; BAB83048.1; -; mRNA.
DR EMBL; AK314237; BAG36906.1; -; mRNA.
DR EMBL; AL158815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04125.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04128.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04129.1; -; Genomic_DNA.
DR EMBL; BC048331; AAH48331.1; -; mRNA.
DR CCDS; CCDS4877.1; -. [Q13608-1]
DR PIR; S71090; S71090.
DR RefSeq; NP_000278.3; NM_000287.3. [Q13608-1]
DR RefSeq; NP_001303242.1; NM_001316313.1. [Q13608-3]
DR AlphaFoldDB; Q13608; -.
DR SMR; Q13608; -.
DR BioGRID; 111213; 124.
DR CORUM; Q13608; -.
DR IntAct; Q13608; 16.
DR MINT; Q13608; -.
DR STRING; 9606.ENSP00000303511; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q13608; -.
DR PhosphoSitePlus; Q13608; -.
DR BioMuta; PEX6; -.
DR DMDM; 12644408; -.
DR EPD; Q13608; -.
DR jPOST; Q13608; -.
DR MassIVE; Q13608; -.
DR PaxDb; Q13608; -.
DR PeptideAtlas; Q13608; -.
DR PRIDE; Q13608; -.
DR ProteomicsDB; 59595; -. [Q13608-1]
DR ProteomicsDB; 75184; -.
DR ABCD; Q13608; 1 sequenced antibody.
DR Antibodypedia; 16146; 232 antibodies from 33 providers.
DR DNASU; 5190; -.
DR Ensembl; ENST00000244546.4; ENSP00000244546.4; ENSG00000124587.14. [Q13608-2]
DR Ensembl; ENST00000304611.13; ENSP00000303511.8; ENSG00000124587.14. [Q13608-1]
DR GeneID; 5190; -.
DR KEGG; hsa:5190; -.
DR MANE-Select; ENST00000304611.13; ENSP00000303511.8; NM_000287.4; NP_000278.3.
DR UCSC; uc003otf.4; human. [Q13608-1]
DR CTD; 5190; -.
DR DisGeNET; 5190; -.
DR GeneCards; PEX6; -.
DR GeneReviews; PEX6; -.
DR HGNC; HGNC:8859; PEX6.
DR HPA; ENSG00000124587; Tissue enhanced (pancreas).
DR MalaCards; PEX6; -.
DR MIM; 601498; gene.
DR MIM; 614862; phenotype.
DR MIM; 614863; phenotype.
DR MIM; 616617; phenotype.
DR neXtProt; NX_Q13608; -.
DR OpenTargets; ENSG00000124587; -.
DR Orphanet; 95433; Autosomal recessive spinocerebellar ataxia-blindness-deafness syndrome.
DR Orphanet; 3220; Deafness-enamel hypoplasia-nail defects syndrome.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA33201; -.
DR VEuPathDB; HostDB:ENSG00000124587; -.
DR eggNOG; KOG0736; Eukaryota.
DR GeneTree; ENSGT00550000074953; -.
DR HOGENOM; CLU_000688_0_8_1; -.
DR InParanoid; Q13608; -.
DR OMA; ALQPCIL; -.
DR PhylomeDB; Q13608; -.
DR TreeFam; TF106428; -.
DR BRENDA; 3.6.4.7; 2681.
DR PathwayCommons; Q13608; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q13608; -.
DR SIGNOR; Q13608; -.
DR BioGRID-ORCS; 5190; 76 hits in 1081 CRISPR screens.
DR ChiTaRS; PEX6; human.
DR GeneWiki; PEX6; -.
DR GenomeRNAi; 5190; -.
DR Pharos; Q13608; Tbio.
DR PRO; PR:Q13608; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13608; protein.
DR Bgee; ENSG00000124587; Expressed in right uterine tube and 142 other tissues.
DR ExpressionAtlas; Q13608; baseline and differential.
DR Genevisible; Q13608; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0006625; P:protein targeting to peroxisome; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amelogenesis imperfecta; ATP-binding;
KW Cell projection; Cytoplasm; Deafness; Disease variant; Membrane;
KW Methylation; Nucleotide-binding; Peroxisome; Peroxisome biogenesis;
KW Peroxisome biogenesis disorder; Reference proteome; Repeat;
KW Zellweger syndrome.
FT CHAIN 1..980
FT /note="Peroxisome assembly factor 2"
FT /id="PRO_0000084607"
FT BINDING 470..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 744..751
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 119
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 207..294
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11355018"
FT /id="VSP_057137"
FT VAR_SEQ 699..738
FT /note="IPSVSWHDVGGLQEVKKEILETIQLPLEHPELLSLGLRRS -> VETKSLEC
FT LPGPGLQLHALSSLMNWTLWPQAGGEVEILEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11355018"
FT /id="VSP_057138"
FT VAR_SEQ 739..980
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11355018"
FT /id="VSP_057139"
FT VARIANT 79
FT /note="A -> P (in dbSNP:rs61752141)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058381"
FT VARIANT 92
FT /note="V -> G (in HMLR2; unknown pathological significance;
FT dbSNP:rs886037780)"
FT /evidence="ECO:0000269|PubMed:27302843"
FT /id="VAR_077505"
FT VARIANT 99
FT /note="R -> L (in HMLR2; unknown pathological significance;
FT dbSNP:rs886037781)"
FT /evidence="ECO:0000269|PubMed:27302843"
FT /id="VAR_077506"
FT VARIANT 218
FT /note="F -> L (in HMLR2; unknown pathological significance;
FT dbSNP:rs886037779)"
FT /evidence="ECO:0000269|PubMed:27302843"
FT /id="VAR_077507"
FT VARIANT 274
FT /note="P -> L (in HMLR2; results in severe functional
FT decrease in peroxisome biogenesis; dbSNP:rs61753219)"
FT /evidence="ECO:0000269|PubMed:19105186,
FT ECO:0000269|PubMed:26387595"
FT /id="VAR_058382"
FT VARIANT 413
FT /note="G -> V (in PBD-CG4; disease phenotype includes
FT hearing loss, visual impairment, enamel dysplasia
FT microcephaly with deep white matter changes and
FT developmental delay; dbSNP:rs1554127531)"
FT /evidence="ECO:0000269|PubMed:26593283"
FT /id="VAR_077508"
FT VARIANT 534
FT /note="L -> P (in PBD-CG4; dbSNP:rs387906809)"
FT /evidence="ECO:0000269|PubMed:21937992"
FT /id="VAR_075872"
FT VARIANT 572
FT /note="T -> I (in HMLR2; dbSNP:rs61753224)"
FT /evidence="ECO:0000269|PubMed:27302843"
FT /id="VAR_077509"
FT VARIANT 601
FT /note="R -> Q (in HMLR2; unknown pathological significance;
FT results in mild functional decrease in peroxisome
FT biogenesis; dbSNP:rs34324426)"
FT /evidence="ECO:0000269|PubMed:19105186,
FT ECO:0000269|PubMed:26387595, ECO:0000269|PubMed:27302843"
FT /id="VAR_058383"
FT VARIANT 644
FT /note="R -> W (in HMLR2; results in mild functional
FT decrease in peroxisome biogenesis; dbSNP:rs769896492)"
FT /evidence="ECO:0000269|PubMed:26387595"
FT /id="VAR_074110"
FT VARIANT 809
FT /note="A -> V (in dbSNP:rs35830695)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_048114"
FT VARIANT 812
FT /note="R -> Q (in PBD4A; dbSNP:rs61753229)"
FT /evidence="ECO:0000269|PubMed:10408779"
FT /id="VAR_007918"
FT VARIANT 812
FT /note="R -> W (in PBD4A; atypical; dbSNP:rs61753228)"
FT /evidence="ECO:0000269|PubMed:10408779"
FT /id="VAR_007919"
FT VARIANT 849
FT /note="N -> T (in PBD-CG4; dbSNP:rs267608244)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058384"
FT VARIANT 860
FT /note="R -> Q (in PBD-CG4; dbSNP:rs61753231)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058385"
FT VARIANT 860
FT /note="R -> W (in PBD-CG4; dbSNP:rs61753230)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058386"
FT VARIANT 882
FT /note="V -> I (in dbSNP:rs2274516)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_048115"
FT VARIANT 905
FT /note="C -> F (in HMLR2; dbSNP:rs886037782)"
FT /evidence="ECO:0000269|PubMed:27302843"
FT /id="VAR_077510"
FT VARIANT 924
FT /note="A -> S (in dbSNP:rs34551839)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058387"
FT VARIANT 939
FT /note="P -> Q (in dbSNP:rs1129187)"
FT /evidence="ECO:0000269|PubMed:11355018,
FT ECO:0000269|PubMed:19105186"
FT /id="VAR_048116"
FT CONFLICT 77
FT /note="S -> N (in Ref. 1; AAC50655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 104061 MW; 0EC1C2A75CE0038F CRC64;
MALAVLRVLE PFPTETPPLA VLLPPGGPWP AAELGLVLAL RPAGESPAGP ALLVAALEGP
DAGTEEQGPG PPQLLVSRAL LRLLALGSGA WVRARAVRRP PALGWALLGT SLGPGLGPRV
GPLLVRRGET LPVPGPRVLE TRPALQGLLG PGTRLAVTEL RGRARLCPES GDSSRPPPPP
VVSSFAVSGT VRRLQGVLGG TGDSLGVSRS CLRGLGLFQG EWVWVAQARE SSNTSQPHLA
RVQVLEPRWD LSDRLGPGSG PLGEPLADGL ALVPATLAFN LGCDPLEMGE LRIQRYLEGS
IAPEDKGSCS LLPGPPFARE LHIEIVSSPH YSTNGNYDGV LYRHFQIPRV VQEGDVLCVP
TIGQVEILEG SPEKLPRWRE MFFKVKKTVG EAPDGPASAY LADTTHTSLY MVGSTLSPVP
WLPSEESTLW SSLSPPGLEA LVSELCAVLK PRLQPGGALL TGTSSVLLRG PPGCGKTTVV
AAACSHLGLH LLKVPCSSLC AESSGAVETK LQAIFSRARR CRPAVLLLTA VDLLGRDRDG
LGEDARVMAV LRHLLLNEDP LNSCPPLMVV ATTSRAQDLP ADVQTAFPHE LEVPALSEGQ
RLSILRALTA HLPLGQEVNL AQLARRCAGF VVGDLYALLT HSSRAACTRI KNSGLAGGLT
EEDEGELCAA GFPLLAEDFG QALEQLQTAH SQAVGAPKIP SVSWHDVGGL QEVKKEILET
IQLPLEHPEL LSLGLRRSGL LLHGPPGTGK TLLAKAVATE CSLTFLSVKG PELINMYVGQ
SEENVREVFA RARAAAPCII FFDELDSLAP SRGRSGDSGG VMDRVVSQLL AELDGLHSTQ
DVFVIGATNR PDLLDPALLR PGRFDKLVFV GANEDRASQL RVLSAITRKF KLEPSVSLVN
VLDCCPPQLT GADLYSLCSD AMTAALKRRV HDLEEGLEPG SSALMLTMED LLQAAARLQP
SVSEQELLRY KRIQRKFAAC
