PEX26_HUMAN
ID PEX26_HUMAN Reviewed; 305 AA.
AC Q7Z412; F6UBB5; Q7Z413; Q7Z414; Q7Z415; Q7Z416; Q96B12; Q9NWQ0; Q9NXU0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peroxisome assembly protein 26;
DE AltName: Full=Peroxin-26;
GN Name=PEX26;
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), FUNCTION, SUBCELLULAR LOCATION,
RP INVOLVEMENT IN PBD-CG8, INTERACTION WITH PEX1 AND PEX6, AND VARIANT PBD7B
RP TRP-98.
RC TISSUE=Fibroblast;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INVOLVEMENT IN PBD-CG8, VARIANT PBD7A ARG-89, AND VARIANTS PBD7B PRO-45 AND
RP TRP-98.
RX PubMed=12851857; DOI=10.1086/377004;
RA Matsumoto N., Tamura S., Furuki S., Miyata N., Moser A., Shimozawa N.,
RA Moser H.W., Suzuki Y., Kondo N., Fujiki Y.;
RT "Mutations in novel peroxin gene PEX26 that cause peroxisome-biogenesis
RT disorders of complementation group 8 provide a genotype-phenotype
RT correlation.";
RL Am. J. Hum. Genet. 73:233-246(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Ileal mucosa;
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 MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-305 (ISOFORM 2).
RX PubMed=10737800; DOI=10.1073/pnas.97.7.3491;
RA Dias Neto E., Correa R.G., Verjovski-Almeida S., Briones M.R.S.,
RA Nagai M.A., da Silva W. Jr., Zago M.A., Bordin S., Costa F.F.,
RA Goldman G.H., Carvalho A.F., Matsukuma A., Baia G.S., Simpson D.H.,
RA Brunstein A., de Oliveira P.S.L., Bucher P., Jongeneel C.V., O'Hare M.J.,
RA Soares F., Brentani R.R., Reis L.F.L., de Souza S.J., Simpson A.J.G.;
RT "Shotgun sequencing of the human transcriptome with ORF expressed sequence
RT tags.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3491-3496(2000).
RN [8]
RP INVOLVEMENT IN PBD-CG8, VARIANT PBD-CG8 TRP-98, AND VARIANT VAL-153.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Probably required for protein import into peroxisomes.
CC Anchors PEX1 and PEX6 to peroxisome membranes, possibly to form
CC heteromeric AAA ATPase complexes required for the import of proteins
CC into peroxisomes. Involved in the import of catalase and proteins
CC containing a PTS2 target sequence, but not in import of proteins with a
CC PTS1 target sequence. {ECO:0000269|PubMed:12717447,
CC ECO:0000269|PubMed:12851857}.
CC -!- SUBUNIT: Interacts directly with PEX6 via its cytoplasmic domain.
CC Interacts indirectly with PEX1, via its interaction with PEX6.
CC {ECO:0000269|PubMed:12717447}.
CC -!- INTERACTION:
CC Q7Z412; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-752057, EBI-22011868;
CC Q7Z412; P63010-2: AP2B1; NbExp=3; IntAct=EBI-752057, EBI-11529439;
CC Q7Z412; Q0P5N6: ARL16; NbExp=3; IntAct=EBI-752057, EBI-10186132;
CC Q7Z412; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-752057, EBI-10254793;
CC Q7Z412; Q9UQB8-3: BAIAP2; NbExp=3; IntAct=EBI-752057, EBI-9091996;
CC Q7Z412; Q9BUW7: BBLN; NbExp=3; IntAct=EBI-752057, EBI-752084;
CC Q7Z412; O15392: BIRC5; NbExp=3; IntAct=EBI-752057, EBI-518823;
CC Q7Z412; Q96LC9: BMF; NbExp=3; IntAct=EBI-752057, EBI-3919268;
CC Q7Z412; Q5JTY5: CBWD3; NbExp=3; IntAct=EBI-752057, EBI-723434;
CC Q7Z412; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-752057, EBI-350590;
CC Q7Z412; Q9UER7: DAXX; NbExp=3; IntAct=EBI-752057, EBI-77321;
CC Q7Z412; A0AVK6: E2F8; NbExp=3; IntAct=EBI-752057, EBI-7779316;
CC Q7Z412; Q5JUQ0: FAM78A; NbExp=3; IntAct=EBI-752057, EBI-21900888;
CC Q7Z412; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-752057, EBI-10253815;
CC Q7Z412; Q969S8: HDAC10; NbExp=3; IntAct=EBI-752057, EBI-301762;
CC Q7Z412; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-752057, EBI-21911304;
CC Q7Z412; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-752057, EBI-12382297;
CC Q7Z412; Q6P597: KLC3; NbExp=3; IntAct=EBI-752057, EBI-1643885;
CC Q7Z412; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-752057, EBI-12811111;
CC Q7Z412; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-752057, EBI-10261141;
CC Q7Z412; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-752057, EBI-25835523;
CC Q7Z412; Q6ZP95: LOC642947; NbExp=3; IntAct=EBI-752057, EBI-25831954;
CC Q7Z412; P50221: MEOX1; NbExp=3; IntAct=EBI-752057, EBI-2864512;
CC Q7Z412; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-752057, EBI-21250407;
CC Q7Z412; Q13064: MKRN3; NbExp=3; IntAct=EBI-752057, EBI-2340269;
CC Q7Z412; Q9Y3D2: MSRB2; NbExp=3; IntAct=EBI-752057, EBI-9092052;
CC Q7Z412; O76041: NEBL; NbExp=3; IntAct=EBI-752057, EBI-2880203;
CC Q7Z412; P40855: PEX19; NbExp=9; IntAct=EBI-752057, EBI-594747;
CC Q7Z412; Q99471: PFDN5; NbExp=3; IntAct=EBI-752057, EBI-357275;
CC Q7Z412; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-752057, EBI-25829984;
CC Q7Z412; Q6UVJ0: SASS6; NbExp=3; IntAct=EBI-752057, EBI-1570153;
CC Q7Z412; Q9UMX1: SUFU; NbExp=2; IntAct=EBI-752057, EBI-740595;
CC Q7Z412; P04637: TP53; NbExp=3; IntAct=EBI-752057, EBI-366083;
CC Q7Z412; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-752057, EBI-358545;
CC Q7Z412; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-752057, EBI-2682299;
CC Q7Z412; Q7Z783; NbExp=3; IntAct=EBI-752057, EBI-9088990;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:12717447}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12717447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z412-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z412-2; Sequence=VSP_053499;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney,
CC liver, brain and skeletal muscles. Expressed at intermediate level in
CC pancreas, placenta and heart. Weakly expressed in lung.
CC {ECO:0000269|PubMed:12851857}.
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 8 (PBD-
CC CG8) [MIM:614872]: 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:12717447, ECO:0000269|PubMed:12851857,
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 7A (PBD7A) [MIM:614872]: 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:12851857}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 7B (PBD7B) [MIM:614873]: 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:12717447, ECO:0000269|PubMed:12851857}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peroxin-26 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90920.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbPEX, PEX Gene Database;
CC URL="https://databases.lovd.nl/shared/genes/PEX26";
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DR EMBL; AB089678; BAC66616.1; -; mRNA.
DR EMBL; AB103106; BAC78804.1; -; mRNA.
DR EMBL; AB103107; BAC78805.1; -; mRNA.
DR EMBL; AB103108; BAC78806.1; -; mRNA.
DR EMBL; AB103109; BAC78807.1; -; mRNA.
DR EMBL; AB103110; BAC78808.1; -; mRNA.
DR EMBL; AK000065; BAA90920.1; ALT_SEQ; mRNA.
DR EMBL; AK000702; BAA91329.1; -; mRNA.
DR EMBL; CR456362; CAG30248.1; -; mRNA.
DR EMBL; AC008079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016280; AAH16280.1; -; mRNA.
DR EMBL; BC047320; AAH47320.1; -; mRNA.
DR EMBL; BF930319; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13750.1; -. [Q7Z412-1]
DR CCDS; CCDS56221.1; -. [Q7Z412-2]
DR RefSeq; NP_001121121.1; NM_001127649.2. [Q7Z412-1]
DR RefSeq; NP_001186248.1; NM_001199319.1. [Q7Z412-2]
DR RefSeq; NP_060399.1; NM_017929.5. [Q7Z412-1]
DR AlphaFoldDB; Q7Z412; -.
DR SMR; Q7Z412; -.
DR BioGRID; 120802; 10.
DR CORUM; Q7Z412; -.
DR IntAct; Q7Z412; 40.
DR MINT; Q7Z412; -.
DR STRING; 9606.ENSP00000331106; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q7Z412; -.
DR PhosphoSitePlus; Q7Z412; -.
DR BioMuta; PEX26; -.
DR DMDM; 47606028; -.
DR EPD; Q7Z412; -.
DR jPOST; Q7Z412; -.
DR MassIVE; Q7Z412; -.
DR MaxQB; Q7Z412; -.
DR PaxDb; Q7Z412; -.
DR PeptideAtlas; Q7Z412; -.
DR PRIDE; Q7Z412; -.
DR ProteomicsDB; 28013; -.
DR ProteomicsDB; 69127; -. [Q7Z412-1]
DR Antibodypedia; 22750; 134 antibodies from 28 providers.
DR DNASU; 55670; -.
DR Ensembl; ENST00000329627.11; ENSP00000331106.5; ENSG00000215193.14. [Q7Z412-1]
DR Ensembl; ENST00000399744.8; ENSP00000382648.4; ENSG00000215193.14. [Q7Z412-1]
DR Ensembl; ENST00000428061.2; ENSP00000412441.2; ENSG00000215193.14. [Q7Z412-2]
DR GeneID; 55670; -.
DR KEGG; hsa:55670; -.
DR MANE-Select; ENST00000399744.8; ENSP00000382648.4; NM_001127649.3; NP_001121121.1.
DR UCSC; uc002znp.5; human. [Q7Z412-1]
DR CTD; 55670; -.
DR DisGeNET; 55670; -.
DR GeneCards; PEX26; -.
DR GeneReviews; PEX26; -.
DR HGNC; HGNC:22965; PEX26.
DR HPA; ENSG00000215193; Low tissue specificity.
DR MalaCards; PEX26; -.
DR MIM; 608666; gene.
DR MIM; 614872; phenotype.
DR MIM; 614873; phenotype.
DR neXtProt; NX_Q7Z412; -.
DR OpenTargets; ENSG00000215193; -.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA134983458; -.
DR VEuPathDB; HostDB:ENSG00000215193; -.
DR eggNOG; ENOG502RXMN; Eukaryota.
DR GeneTree; ENSGT00510000049725; -.
DR HOGENOM; CLU_051194_0_0_1; -.
DR InParanoid; Q7Z412; -.
DR OMA; KCSLCIV; -.
DR PhylomeDB; Q7Z412; -.
DR TreeFam; TF332318; -.
DR PathwayCommons; Q7Z412; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; Q7Z412; -.
DR SIGNOR; Q7Z412; -.
DR BioGRID-ORCS; 55670; 80 hits in 1082 CRISPR screens.
DR ChiTaRS; PEX26; human.
DR GeneWiki; PEX26; -.
DR GenomeRNAi; 55670; -.
DR Pharos; Q7Z412; Tbio.
DR PRO; PR:Q7Z412; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q7Z412; protein.
DR Bgee; ENSG00000215193; Expressed in mucosa of transverse colon and 182 other tissues.
DR ExpressionAtlas; Q7Z412; baseline and differential.
DR Genevisible; Q7Z412; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IEA:InterPro.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI: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:0016558; P:protein import into peroxisome matrix; IDA:UniProtKB.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IEA:InterPro.
DR InterPro; IPR010797; Pex26.
DR PANTHER; PTHR16262; PTHR16262; 1.
DR Pfam; PF07163; Pex26; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Membrane; Peroxisome;
KW Peroxisome biogenesis disorder; Protein transport; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport;
KW Zellweger syndrome.
FT CHAIN 1..305
FT /note="Peroxisome assembly protein 26"
FT /id="PRO_0000058340"
FT TOPO_DOM 1..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..305
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 223..271
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10737800"
FT /id="VSP_053499"
FT VARIANT 45
FT /note="L -> P (in PBD7B; infantile Refsum disease;
FT dbSNP:rs61752132)"
FT /evidence="ECO:0000269|PubMed:12851857"
FT /id="VAR_018647"
FT VARIANT 89
FT /note="G -> R (in PBD7A; dbSNP:rs28940308)"
FT /evidence="ECO:0000269|PubMed:12851857"
FT /id="VAR_018648"
FT VARIANT 98
FT /note="R -> W (in PBD7B and PBD-CG8; neonatal
FT adrenoleukodystrophy; affects the interaction with PEX6;
FT dbSNP:rs62641228)"
FT /evidence="ECO:0000269|PubMed:12717447,
FT ECO:0000269|PubMed:12851857, ECO:0000269|PubMed:19105186"
FT /id="VAR_018649"
FT VARIANT 153
FT /note="L -> V (in dbSNP:rs12484657)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_034146"
FT CONFLICT 304
FT /note="R -> H (in Ref. 6; AAH16280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33898 MW; 0B9FCF8E2B3178E1 CRC64;
MKSDSSTSAA PLRGLGGPLR SSEPVRAVPA RAPAVDLLEE AADLLVVHLD FRAALETCER
AWQSLANHAV AEEPAGTSLE VKCSLCVVGI QALAEMDRWQ EVLSWVLQYY QVPEKLPPKV
LELCILLYSK MQEPGAVLDV VGAWLQDPAN QNLPEYGALA EFHVQRVLLP LGCLSEAEEL
VVGSAAFGEE RRLDVLQAIH TARQQQKQEH SGSEEAQKPN LEGSVSHKFL SLPMLVRQLW
DSAVSHFFSL PFKKSLLAAL ILCLLVVRFD PASPSSLHFL YKLAQLFRWI RKAAFSRLYQ
LRIRD
