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Peroxisome assembly factor 2 (PAF-2) (Peroxin-6) (Peroxisomal biogenesis factor 6) (Peroxisomal-type ATPase 1)

 PEX6_HUMAN              Reviewed;         980 AA.
Q13608; Q5T8W1; Q8WYQ0; Q8WYQ1; Q8WYQ2; Q99476;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
08-DEC-2000, sequence version 2.
27-SEP-2017, entry version 160.
RecName: Full=Peroxisome assembly factor 2;
Short=PAF-2;
AltName: Full=Peroxin-6;
AltName: Full=Peroxisomal biogenesis factor 6;
AltName: Full=Peroxisomal-type ATPase 1;
Name=PEX6; Synonyms=PXAAA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN PBD4A.
PubMed=8670792;
Yahraus T., Braverman N., Dodt G., Kalish J.E., Morrell J.C.,
Moser H.W., Valle D., Gould S.J.;
"The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a
cytoplasmic ATPase required for stability of the PTS1 receptor.";
EMBO J. 15:2914-2923(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8940266;
Fukuda S., Shimozawa N., Suzuki Y., Zhang Z., Tomatsu S.,
Tsukamoto T., Hashiguchi N., Osumi T., Masuno M., Imaizumi K.,
Kuroki Y., Fujiki Y., Orii T., Kondo N.;
"Human peroxisome assembly factor-2 (PAF-2): a gene responsible for
group C peroxisome biogenesis disorder in humans.";
Am. J. Hum. Genet. 59:1210-1220(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PBD4A GLN-812 AND
TRP-812.
PubMed=10408779;
DOI=10.1002/(SICI)1098-1004(1999)13:6<487::AID-HUMU9>3.0.CO;2-T;
Zhang Z., Suzuki Y., Shimozawa N., Fukuda S., Imamura A.,
Tsukamoto T., Osumi T., Fujiki Y., Orii T., Wanders R.J.A.,
Barth P.G., Moser H.W., Paton B.C., Besley G.T., Kondo N.;
"Genomic structure and identification of 11 novel mutations of the
PEX6 'peroxisome assembly factor-2' gene in patients with peroxisome
biogenesis disorders.";
Hum. Mutat. 13:487-496(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR
LOCATION, VARIANT GLN-939, INVOLVEMENT IN PBD4B, AND ALTERNATIVE
SPLICING.
PubMed=11355018; DOI=10.1007/s100380170078;
Matsumoto N., Tamura S., Moser A., Moser H.W., Braverman N.,
Suzuki Y., Shimozawa N., Kondo N., Fujiki Y.;
"The peroxin Pex6p gene is impaired in peroxisomal biogenesis
disorders of complementation group 6.";
J. Hum. Genet. 46:273-277(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PEX26 AND PEX1.
PubMed=12717447; DOI=10.1038/ncb982;
Matsumoto N., Tamura S., Fujiki Y.;
"The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase
complexes to peroxisomes.";
Nat. Cell Biol. 5:454-460(2003).
[10]
INVOLVEMENT IN PBD-CG4, INVOLVEMENT IN HMLR2, VARIANTS PBD-CG4
THR-849; GLN-860 AND TRP-860, VARIANTS HMLR2 LEU-274 AND GLN-601, AND
VARIANTS PRO-79; VAL-809; ILE-882; SER-924 AND GLN-939.
PubMed=19105186; DOI=10.1002/humu.20932;
Yik W.Y., Steinberg S.J., Moser A.B., Moser H.W., Hacia J.G.;
"Identification of novel mutations and sequence variation in the
Zellweger syndrome spectrum of peroxisome biogenesis disorders.";
Hum. Mutat. 30:E467-E480(2009).
[11]
INVOLVEMENT IN PBD-CG4, AND VARIANT PBD-CG4 PRO-534.
PubMed=21937992; DOI=10.1038/nature10423;
Najmabadi H., Hu H., Garshasbi M., Zemojtel T., Abedini S.S., Chen W.,
Hosseini M., Behjati F., Haas S., Jamali P., Zecha A., Mohseni M.,
Puettmann L., Vahid L.N., Jensen C., Moheb L.A., Bienek M., Larti F.,
Mueller I., Weissmann R., Darvish H., Wrogemann K., Hadavi V.,
Lipkowitz B., Esmaeeli-Nieh S., Wieczorek D., Kariminejad R.,
Firouzabadi S.G., Cohen M., Fattahi Z., Rost I., Mojahedi F.,
Hertzberg C., Dehghan A., Rajab A., Banavandi M.J., Hoffer J.,
Falah M., Musante L., Kalscheuer V., Ullmann R., Kuss A.W.,
Tzschach A., Kahrizi K., Ropers H.H.;
"Deep sequencing reveals 50 novel genes for recessive cognitive
disorders.";
Nature 478:57-63(2011).
[12]
INTERACTION WITH ZFAND6.
PubMed=21980954; DOI=10.1111/j.1600-0854.2011.01298.x;
Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.;
"AWP1/ZFAND6 functions in Pex5 export by interacting with cys-
monoubiquitinated Pex5 and Pex6 AAA ATPase.";
Traffic 13:168-183(2012).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-119, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[14]
INVOLVEMENT IN HMLR2, VARIANTS HMLR2 LEU-274; GLN-601 AND TRP-644, AND
CHARACTERIZATION OF VARIANTS HMLR2 LEU-274; GLN-601 AND TRP-644.
PubMed=26387595; DOI=10.1016/j.ajhg.2015.08.011;
Ratbi I., Falkenberg K.D., Sommen M., Al-Sheqaih N., Guaoua S.,
Vandeweyer G., Urquhart J.E., Chandler K.E., Williams S.G.,
Roberts N.A., El Alloussi M., Black G.C., Ferdinandusse S., Ramdi H.,
Heimler A., Fryer A., Lynch S.A., Cooper N., Ong K.R., Smith C.E.,
Inglehearn C.F., Mighell A.J., Elcock C., Poulter J.A.,
Tischkowitz M., Davies S.J., Sefiani A., Mironov A.A., Newman W.G.,
Waterham H.R., Van Camp G.;
"Heimler syndrome is caused by hypomorphic mutations in the
peroxisome-biogenesis genes PEX1 and PEX6.";
Am. J. Hum. Genet. 97:535-545(2015).
[15]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT PBD-CG4 VAL-413.
PubMed=26593283; DOI=10.1002/humu.22934;
Zaki M.S., Heller R., Thoenes M., Nuernberg G., Stern-Schneider G.,
Nuernberg P., Karnati S., Swan D., Fateen E., Nagel-Wolfrum K.,
Mostafa M.I., Thiele H., Wolfrum U., Baumgart-Vogt E., Bolz H.J.;
"PEX6 is expressed in photoreceptor cilia and mutated in deafblindness
with enamel dysplasia and microcephaly.";
Hum. Mutat. 37:170-174(2016).
[16]
VARIANTS HMLR2 GLY-92; LEU-99; LEU-218; ILE-572; GLN-601 AND PHE-905.
PubMed=27302843; DOI=10.1038/ejhg.2016.62;
Smith C.E., Poulter J.A., Levin A.V., Capasso J.E., Price S.,
Ben-Yosef T., Sharony R., Newman W.G., Shore R.C., Brookes S.J.,
Mighell A.J., Inglehearn C.F.;
"Spectrum of PEX1 and PEX6 variants in Heimler syndrome.";
Eur. J. Hum. Genet. 24:1565-1571(2016).
-!- FUNCTION: Involved in peroxisome biosynthesis. Required for
stability of the PTS1 receptor. Anchored by PEX26 to peroxisome
membranes, possibly to form heteromeric AAA ATPase complexes
required for the import of proteins into peroxisomes.
-!- SUBUNIT: Interacts directly with PEX26 and PEX1. Mediates the
indirect interaction between PEX1 and PEX26. Interacts with
ZFAND6. {ECO:0000269|PubMed:12717447,
ECO:0000269|PubMed:21980954}.
-!- INTERACTION:
O43933:PEX1; NbExp=2; IntAct=EBI-988581, EBI-988601;
-!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane
{ECO:0000269|PubMed:11355018}. Cell projection, cilium,
photoreceptor outer segment {ECO:0000269|PubMed:26593283}.
Note=Associated with peroxisomal membranes. Localized at the base
of the outer segment of photoreceptor cells (PubMed:26593283).
{ECO:0000269|PubMed:26593283}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13608-1; Sequence=Displayed;
Name=2;
IsoId=Q13608-2; Sequence=VSP_057138, VSP_057139;
Name=3;
IsoId=Q13608-3; Sequence=VSP_057137;
-!- TISSUE SPECIFICITY: Expressed in the retina, at higher levels in
the photoreceptor layer at the joint between the outer and inner
segments. {ECO:0000269|PubMed:26593283}.
-!- DISEASE: Peroxisome biogenesis disorder complementation group 4
(PBD-CG4) [MIM:614862]: A peroxisomal disorder arising from a
failure of protein import into the peroxisomal membrane or matrix.
The peroxisome biogenesis disorders (PBD group) are genetically
heterogeneous with at least 14 distinct genetic groups as
concluded from complementation studies. Include disorders are:
Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD),
infantile Refsum disease (IRD), and classical rhizomelic
chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct
from RCDP and constitute a clinical continuum of overlapping
phenotypes known as the Zellweger spectrum (PBD-ZSS).
{ECO:0000269|PubMed:19105186, ECO:0000269|PubMed:21937992,
ECO:0000269|PubMed:26593283}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 4A (PBD4A) [MIM:614862]: A
fatal peroxisome biogenesis disorder belonging to the Zellweger
disease spectrum and clinically characterized by severe neurologic
dysfunction with profound psychomotor retardation, severe
hypotonia and neonatal seizures, craniofacial abnormalities, liver
dysfunction, and biochemically by the absence of peroxisomes.
Additional features include cardiovascular and skeletal defects,
renal cysts, ocular abnormalities, and hearing impairment. Most
severely affected individuals with the classic form of the disease
(classic Zellweger syndrome) die within the first year of life.
{ECO:0000269|PubMed:10408779, ECO:0000269|PubMed:8670792}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 4B (PBD4B) [MIM:614863]: A
peroxisome biogenesis disorder that includes neonatal
adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD),
two milder manifestations of the Zellweger disease spectrum. The
clinical course of patients with the NALD and IRD presentation is
variable and may include developmental delay, hypotonia, liver
dysfunction, sensorineural hearing loss, retinal dystrophy and
vision impairment. Children with the NALD presentation may reach
their teens, while patients with the IRD presentation may reach
adulthood. The clinical conditions are often slowly progressive in
particular with respect to loss of hearing and vision. The
biochemical abnormalities include accumulation of phytanic acid,
very long chain fatty acids (VLCFA), di- and
trihydroxycholestanoic acid and pipecolic acid.
{ECO:0000269|PubMed:11355018}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Heimler syndrome 2 (HMLR2) [MIM:616617]: A form of
Heimler syndrome, a very mild peroxisome biogenesis disorder
characterized by sensorineural hearing loss, amelogenesis
imperfecta resulting in enamel hyoplasia of the secondary
dentition, nail defects, and occasional or late-onset retinal
pigmentation abnormalities. {ECO:0000269|PubMed:19105186,
ECO:0000269|PubMed:26387595, ECO:0000269|PubMed:27302843}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=dbPEX, PEX Gene Database;
URL="http://www.dbpex.org/home.php?select_db=PEX6";
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EMBL; U56602; AAC50655.1; -; Genomic_DNA.
EMBL; D83703; BAA12069.1; -; mRNA.
EMBL; AF108098; AAF62564.1; -; Genomic_DNA.
EMBL; AF108095; AAF62564.1; JOINED; Genomic_DNA.
EMBL; AF108096; AAF62564.1; JOINED; Genomic_DNA.
EMBL; AF108097; AAF62564.1; JOINED; Genomic_DNA.
EMBL; AB051076; BAB83046.1; -; mRNA.
EMBL; AB051077; BAB83047.1; -; mRNA.
EMBL; AB051078; BAB83048.1; -; mRNA.
EMBL; AK314237; BAG36906.1; -; mRNA.
EMBL; AL158815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04125.1; -; Genomic_DNA.
EMBL; CH471081; EAX04128.1; -; Genomic_DNA.
EMBL; CH471081; EAX04129.1; -; Genomic_DNA.
EMBL; BC048331; AAH48331.1; -; mRNA.
CCDS; CCDS4877.1; -. [Q13608-1]
PIR; S71090; S71090.
RefSeq; NP_000278.3; NM_000287.3. [Q13608-1]
RefSeq; NP_001303242.1; NM_001316313.1. [Q13608-3]
UniGene; Hs.656425; -.
ProteinModelPortal; Q13608; -.
SMR; Q13608; -.
BioGrid; 111213; 18.
CORUM; Q13608; -.
IntAct; Q13608; 6.
MINT; MINT-1183928; -.
STRING; 9606.ENSP00000303511; -.
TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
iPTMnet; Q13608; -.
PhosphoSitePlus; Q13608; -.
BioMuta; PEX6; -.
DMDM; 12644408; -.
EPD; Q13608; -.
PaxDb; Q13608; -.
PeptideAtlas; Q13608; -.
PRIDE; Q13608; -.
Ensembl; ENST00000244546; ENSP00000244546; ENSG00000124587. [Q13608-2]
Ensembl; ENST00000304611; ENSP00000303511; ENSG00000124587. [Q13608-1]
GeneID; 5190; -.
KEGG; hsa:5190; -.
UCSC; uc003otf.4; human. [Q13608-1]
CTD; 5190; -.
DisGeNET; 5190; -.
EuPathDB; HostDB:ENSG00000124587.13; -.
GeneCards; PEX6; -.
GeneReviews; PEX6; -.
HGNC; HGNC:8859; PEX6.
HPA; HPA025924; -.
HPA; HPA074179; -.
MalaCards; PEX6; -.
MIM; 601498; gene.
MIM; 614862; phenotype.
MIM; 614863; phenotype.
MIM; 616617; phenotype.
neXtProt; NX_Q13608; -.
OpenTargets; ENSG00000124587; -.
Orphanet; 772; Infantile Refsum disease.
Orphanet; 44; Neonatal adrenoleukodystrophy.
Orphanet; 912; Zellweger syndrome.
PharmGKB; PA33201; -.
eggNOG; KOG0736; Eukaryota.
eggNOG; ENOG410XNT9; LUCA.
GeneTree; ENSGT00550000074953; -.
HOGENOM; HOG000241031; -.
HOVERGEN; HBG002311; -.
InParanoid; Q13608; -.
KO; K13339; -.
OMA; PSVSWHD; -.
OrthoDB; EOG091G048C; -.
PhylomeDB; Q13608; -.
TreeFam; TF106428; -.
SIGNOR; Q13608; -.
ChiTaRS; PEX6; human.
GeneWiki; PEX6; -.
GenomeRNAi; 5190; -.
PRO; PR:Q13608; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124587; -.
CleanEx; HS_PEX6; -.
ExpressionAtlas; Q13608; baseline and differential.
Genevisible; Q13608; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0097733; C:photoreceptor cell cilium; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
GO; GO:0016887; F:ATPase activity; IMP:UniProtKB.
GO; GO:0042623; F:ATPase activity, coupled; IMP:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; IMP:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
Alternative splicing; Amelogenesis imperfecta; ATP-binding;
Cell projection; Complete proteome; Cytoplasm; Deafness;
Disease mutation; Membrane; Methylation; Nucleotide-binding;
Peroxisome; Peroxisome biogenesis; Peroxisome biogenesis disorder;
Polymorphism; Reference proteome; Repeat; Zellweger syndrome.
CHAIN 1 980 Peroxisome assembly factor 2.
/FTId=PRO_0000084607.
NP_BIND 470 477 ATP. {ECO:0000255}.
NP_BIND 744 751 ATP. {ECO:0000255}.
MOD_RES 119 119 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 207 294 Missing (in isoform 3).
{ECO:0000303|PubMed:11355018}.
/FTId=VSP_057137.
VAR_SEQ 699 738 IPSVSWHDVGGLQEVKKEILETIQLPLEHPELLSLGLRRS
-> VETKSLECLPGPGLQLHALSSLMNWTLWPQAGGEVEIL
EE (in isoform 2).
{ECO:0000303|PubMed:11355018}.
/FTId=VSP_057138.
VAR_SEQ 739 980 Missing (in isoform 2).
{ECO:0000303|PubMed:11355018}.
/FTId=VSP_057139.
VARIANT 79 79 A -> P (in dbSNP:rs61752141).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058381.
VARIANT 92 92 V -> G (in HMLR2; unknown pathological
significance).
{ECO:0000269|PubMed:27302843}.
/FTId=VAR_077505.
VARIANT 99 99 R -> L (in HMLR2; unknown pathological
significance).
{ECO:0000269|PubMed:27302843}.
/FTId=VAR_077506.
VARIANT 218 218 F -> L (in HMLR2; unknown pathological
significance).
{ECO:0000269|PubMed:27302843}.
/FTId=VAR_077507.
VARIANT 274 274 P -> L (in HMLR2; results in severe
functional decrease in peroxisome
biogenesis; dbSNP:rs61753219).
{ECO:0000269|PubMed:19105186,
ECO:0000269|PubMed:26387595}.
/FTId=VAR_058382.
VARIANT 413 413 G -> V (in PBD-CG4; disease phenotype
includes hearing loss, visual impairment,
enamel dysplasia microcephaly with deep
white matter changes and developmental
delay). {ECO:0000269|PubMed:26593283}.
/FTId=VAR_077508.
VARIANT 534 534 L -> P (in PBD-CG4; dbSNP:rs387906809).
{ECO:0000269|PubMed:21937992}.
/FTId=VAR_075872.
VARIANT 572 572 T -> I (in HMLR2; dbSNP:rs61753224).
{ECO:0000269|PubMed:27302843}.
/FTId=VAR_077509.
VARIANT 601 601 R -> Q (in HMLR2; unknown pathological
significance; results in mild functional
decrease in peroxisome biogenesis;
dbSNP:rs34324426).
{ECO:0000269|PubMed:19105186,
ECO:0000269|PubMed:26387595,
ECO:0000269|PubMed:27302843}.
/FTId=VAR_058383.
VARIANT 644 644 R -> W (in HMLR2; results in mild
functional decrease in peroxisome
biogenesis; dbSNP:rs769896492).
{ECO:0000269|PubMed:26387595}.
/FTId=VAR_074110.
VARIANT 809 809 A -> V (in dbSNP:rs35830695).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_048114.
VARIANT 812 812 R -> Q (in PBD4A; dbSNP:rs61753229).
{ECO:0000269|PubMed:10408779}.
/FTId=VAR_007918.
VARIANT 812 812 R -> W (in PBD4A; atypical;
dbSNP:rs61753228).
{ECO:0000269|PubMed:10408779}.
/FTId=VAR_007919.
VARIANT 849 849 N -> T (in PBD-CG4; dbSNP:rs267608244).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058384.
VARIANT 860 860 R -> Q (in PBD-CG4; dbSNP:rs61753231).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058385.
VARIANT 860 860 R -> W (in PBD-CG4; dbSNP:rs61753230).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058386.
VARIANT 882 882 V -> I (in dbSNP:rs2274516).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_048115.
VARIANT 905 905 C -> F (in HMLR2).
{ECO:0000269|PubMed:27302843}.
/FTId=VAR_077510.
VARIANT 924 924 A -> S (in dbSNP:rs34551839).
{ECO:0000269|PubMed:19105186}.
/FTId=VAR_058387.
VARIANT 939 939 P -> Q (in dbSNP:rs1129187).
{ECO:0000269|PubMed:11355018,
ECO:0000269|PubMed:19105186}.
/FTId=VAR_048116.
CONFLICT 77 77 S -> N (in Ref. 1; AAC50655).
{ECO:0000305}.
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


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