PEX1_HUMAN
ID PEX1_HUMAN Reviewed; 1283 AA.
AC O43933; A4D1G3; A8KA90; B4DIM7; E9PE75; Q96S71; Q96S72; Q96S73; Q99994;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Peroxisome biogenesis factor 1;
DE AltName: Full=Peroxin-1;
DE AltName: Full=Peroxisome biogenesis disorder protein 1;
GN Name=PEX1;
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 PBD1A/PBD1B ASP-843.
RX PubMed=9398848; DOI=10.1038/ng1297-449;
RA Portsteffen H., Beyer A., Becker E., Epplen C., Pawlak A., Kunau W.-H.,
RA Dodt G.;
RT "Human PEX1 is mutated in complementation group 1 of the peroxisome
RT biogenesis disorders.";
RL Nat. Genet. 17:449-452(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PBD1A
RP ASP-843, AND VARIANT PBD1B ASP-843.
RX PubMed=9398847; DOI=10.1038/ng1297-445;
RA Reuber B.E., Germain-Lee E., Collins C.S., Morrell J.C., Ameritunga R.,
RA Moser H.W., Valle D., Gould S.J.;
RT "Mutations in PEX1 are the most common cause of peroxisome biogenesis
RT disorders.";
RL Nat. Genet. 17:445-448(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PBD1A 634-GLY--HIS-690
RP DEL; PRO-664 AND ASP-843, AND VARIANTS PBD1B 634-GLY--HIS-690 DEL; PRO-664
RP AND ASP-843.
RX PubMed=9539740; DOI=10.1073/pnas.95.8.4350;
RA Tamura S., Okumoto K., Toyama R., Shimozawa N., Tsukamoto T., Suzuki Y.,
RA Osumi T., Kondo N., Fujiki Y.;
RT "Human PEX1 cloned by functional complementation on a CHO cell mutant is
RT responsible for peroxisome-deficient Zellweger syndrome of complementation
RT group I.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4350-4355(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PBD1B ASP-843.
RX PubMed=11439091; DOI=10.1042/0264-6021:3570417;
RA Tamura S., Matsumoto N., Imamura A., Shimozawa N., Suzuki Y., Kondo N.,
RA Fujiki Y.;
RT "Phenotype-genotype relationships in peroxisome biogenesis disorders of
RT PEX1-defective complementation group 1 are defined by Pex1p-Pex6p
RT interaction.";
RL Biochem. J. 357:417-426(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-696.
RC TISSUE=Hippocampus, and Trachea;
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=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [10]
RP INTERACTION WITH PEX26 AND PEX6.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INVOLVEMENT IN PBD-CG1, VARIANTS PBD-CG1 ARG-590; ARG-593; GLY-798;
RP ASP-843; PRO-1008 DEL AND GLU-1237, AND VARIANTS MET-696 AND GLN-948.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354; SER-1181 AND SER-1211,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP INVOLVEMENT IN HMLR1, VARIANTS HMLR1 PRO-581 AND TRP-705, AND
RP CHARACTERIZATION OF VARIANTS HMLR1 PRO-581 AND TRP-705.
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 [20]
RP VARIANTS PBD1B THR-989 AND GLN-998.
RX PubMed=16088892; DOI=10.1002/humu.9356;
RA Maxwell M.A., Leane P.B., Paton B.C., Crane D.I.;
RT "Novel PEX1 coding mutations and 5' UTR regulatory polymorphisms.";
RL Hum. Mutat. 26:279-279(2005).
RN [21]
RP VARIANT HMLR1 THR-989.
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: Required for stability of PEX5 and protein import into the
CC peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly
CC to form heteromeric AAA ATPase complexes required for the import of
CC proteins into peroxisomes.
CC -!- SUBUNIT: Interacts directly with PEX6. Interacts indirectly with PEX26,
CC via its interaction with PEX6. {ECO:0000269|PubMed:12717447}.
CC -!- INTERACTION:
CC O43933; Q9NYG5: ANAPC11; NbExp=3; IntAct=EBI-988601, EBI-2130187;
CC O43933; P13928: ANXA8; NbExp=3; IntAct=EBI-988601, EBI-2556915;
CC O43933; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-988601, EBI-2875816;
CC O43933; Q16520: BATF; NbExp=3; IntAct=EBI-988601, EBI-749503;
CC O43933; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-988601, EBI-350590;
CC O43933; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-988601, EBI-25842815;
CC O43933; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-988601, EBI-724653;
CC O43933; O60841: EIF5B; NbExp=3; IntAct=EBI-988601, EBI-928530;
CC O43933; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-988601, EBI-21574901;
CC O43933; Q8NCL4: GALNT6; NbExp=3; IntAct=EBI-988601, EBI-3907241;
CC O43933; P68431: H3C12; NbExp=3; IntAct=EBI-988601, EBI-79722;
CC O43933; A0A024R1L7: hCG_41307; NbExp=3; IntAct=EBI-988601, EBI-25849938;
CC O43933; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-988601, EBI-9091197;
CC O43933; Q9UNL4: ING4; NbExp=3; IntAct=EBI-988601, EBI-2866661;
CC O43933; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-988601, EBI-25871195;
CC O43933; P57682: KLF3; NbExp=3; IntAct=EBI-988601, EBI-8472267;
CC O43933; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-988601, EBI-8473062;
CC O43933; Q68G74: LHX8; NbExp=3; IntAct=EBI-988601, EBI-8474075;
CC O43933; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-988601, EBI-10182361;
CC O43933; P41218: MNDA; NbExp=3; IntAct=EBI-988601, EBI-2829677;
CC O43933; O43196-4: MSH5; NbExp=3; IntAct=EBI-988601, EBI-25860238;
CC O43933; Q96A32: MYLPF; NbExp=3; IntAct=EBI-988601, EBI-1390771;
CC O43933; Q13608: PEX6; NbExp=2; IntAct=EBI-988601, EBI-988581;
CC O43933; O75925: PIAS1; NbExp=3; IntAct=EBI-988601, EBI-629434;
CC O43933; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-988601, EBI-18063495;
CC O43933; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-988601, EBI-746325;
CC O43933; Q8N488: RYBP; NbExp=3; IntAct=EBI-988601, EBI-752324;
CC O43933; Q9C0C4: SEMA4C; NbExp=3; IntAct=EBI-988601, EBI-10303490;
CC O43933; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-988601, EBI-9089805;
CC O43933; Q13530: SERINC3; NbExp=3; IntAct=EBI-988601, EBI-1045571;
CC O43933; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-988601, EBI-8635958;
CC O43933; Q9UJZ1: STOML2; NbExp=3; IntAct=EBI-988601, EBI-1044428;
CC O43933; Q8WUA7-2: TBC1D22A; NbExp=3; IntAct=EBI-988601, EBI-21575846;
CC O43933; Q96EI5: TCEAL4; NbExp=3; IntAct=EBI-988601, EBI-2511291;
CC O43933; P19429: TNNI3; NbExp=3; IntAct=EBI-988601, EBI-704146;
CC O43933; P45880: VDAC2; NbExp=3; IntAct=EBI-988601, EBI-354022;
CC O43933; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-988601, EBI-358545;
CC O43933; O00308: WWP2; NbExp=3; IntAct=EBI-988601, EBI-743923;
CC O43933; Q8TBF4: ZCRB1; NbExp=3; IntAct=EBI-988601, EBI-11124401;
CC O43933; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-988601, EBI-12055755;
CC O43933; Q8N895: ZNF366; NbExp=3; IntAct=EBI-988601, EBI-2813661;
CC O43933; Q86V28; NbExp=3; IntAct=EBI-988601, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane. Note=Associated
CC with peroxisomal membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43933-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43933-2; Sequence=VSP_057136;
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 1 (PBD-
CC CG1) [MIM:214100]: 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 1A (PBD1A) [MIM:214100]: A
CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease
CC spectrum. PBD1A is an autosomal recessive systemic disorder
CC characterized clinically by severe neurologic dysfunction with profound
CC psychomotor retardation, severe hypotonia and neonatal seizures,
CC craniofacial abnormalities, liver dysfunction, and biochemically by the
CC absence of peroxisomes. Additional features include cardiovascular and
CC skeletal defects, renal cysts, ocular abnormalities, and hearing
CC impairment. Most severely affected individuals with the classic form of
CC the disease (classic Zellweger syndrome) die within the first year of
CC life. {ECO:0000269|PubMed:9398847, ECO:0000269|PubMed:9398848,
CC ECO:0000269|PubMed:9539740}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 1B (PBD1B) [MIM:601539]: 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:11439091, ECO:0000269|PubMed:16088892,
CC ECO:0000269|PubMed:9398847, ECO:0000269|PubMed:9539740}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Heimler syndrome 1 (HMLR1) [MIM:234580]: 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:26387595, ECO:0000269|PubMed:27302843}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB46346.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbPEX, PEX Gene Database;
CC URL="https://databases.lovd.nl/shared/genes/PEX1";
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DR EMBL; AF030356; AAB99758.1; -; mRNA.
DR EMBL; AF026086; AAB87880.1; -; mRNA.
DR EMBL; AB008112; BAA85162.1; -; mRNA.
DR EMBL; AB052090; BAB59061.1; -; mRNA.
DR EMBL; AB052091; BAB59062.1; -; mRNA.
DR EMBL; AB052092; BAB59063.1; -; mRNA.
DR EMBL; AK292955; BAF85644.1; -; mRNA.
DR EMBL; AK295686; BAG58539.1; -; mRNA.
DR EMBL; AC007566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000064; AAB46346.1; ALT_SEQ; Genomic_DNA.
DR EMBL; KF458517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236949; EAL24149.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76840.1; -; Genomic_DNA.
DR EMBL; BC035575; AAH35575.1; -; mRNA.
DR CCDS; CCDS5627.1; -. [O43933-1]
DR RefSeq; NP_000457.1; NM_000466.2. [O43933-1]
DR RefSeq; NP_001269606.1; NM_001282677.1.
DR RefSeq; NP_001269607.1; NM_001282678.1.
DR AlphaFoldDB; O43933; -.
DR SMR; O43933; -.
DR BioGRID; 111212; 94.
DR CORUM; O43933; -.
DR IntAct; O43933; 55.
DR MINT; O43933; -.
DR STRING; 9606.ENSP00000248633; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; O43933; -.
DR PhosphoSitePlus; O43933; -.
DR BioMuta; PEX1; -.
DR EPD; O43933; -.
DR jPOST; O43933; -.
DR MassIVE; O43933; -.
DR MaxQB; O43933; -.
DR PaxDb; O43933; -.
DR PeptideAtlas; O43933; -.
DR PRIDE; O43933; -.
DR ProteomicsDB; 19827; -.
DR ProteomicsDB; 49243; -. [O43933-1]
DR Antibodypedia; 15612; 194 antibodies from 32 providers.
DR DNASU; 5189; -.
DR Ensembl; ENST00000248633.9; ENSP00000248633.4; ENSG00000127980.16. [O43933-1]
DR Ensembl; ENST00000438045.5; ENSP00000410438.1; ENSG00000127980.16. [O43933-2]
DR GeneID; 5189; -.
DR KEGG; hsa:5189; -.
DR MANE-Select; ENST00000248633.9; ENSP00000248633.4; NM_000466.3; NP_000457.1.
DR UCSC; uc003uly.4; human. [O43933-1]
DR CTD; 5189; -.
DR DisGeNET; 5189; -.
DR GeneCards; PEX1; -.
DR GeneReviews; PEX1; -.
DR HGNC; HGNC:8850; PEX1.
DR HPA; ENSG00000127980; Low tissue specificity.
DR MalaCards; PEX1; -.
DR MIM; 214100; phenotype.
DR MIM; 234580; phenotype.
DR MIM; 601539; phenotype.
DR MIM; 602136; gene.
DR neXtProt; NX_O43933; -.
DR OpenTargets; ENSG00000127980; -.
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; PA33192; -.
DR VEuPathDB; HostDB:ENSG00000127980; -.
DR eggNOG; KOG0735; Eukaryota.
DR GeneTree; ENSGT00550000075032; -.
DR HOGENOM; CLU_000688_1_1_1; -.
DR InParanoid; O43933; -.
DR OMA; VVECHAL; -.
DR OrthoDB; 1171861at2759; -.
DR PhylomeDB; O43933; -.
DR TreeFam; TF106447; -.
DR BRENDA; 3.6.4.7; 2681.
DR PathwayCommons; O43933; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; O43933; -.
DR SIGNOR; O43933; -.
DR BioGRID-ORCS; 5189; 102 hits in 1087 CRISPR screens.
DR ChiTaRS; PEX1; human.
DR GeneWiki; PEX1; -.
DR GenomeRNAi; 5189; -.
DR Pharos; O43933; Tbio.
DR PRO; PR:O43933; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43933; protein.
DR Bgee; ENSG00000127980; Expressed in calcaneal tendon and 185 other tissues.
DR ExpressionAtlas; O43933; baseline and differential.
DR Genevisible; O43933; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
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:0060152; P:microtubule-based peroxisome localization; IMP:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; 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; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015343; PEX-N_a/b.
DR InterPro; IPR015342; PEX-N_psi_beta-barrel.
DR InterPro; IPR025653; Pex1.
DR PANTHER; PTHR23077:SF12; PTHR23077:SF12; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09262; PEX-1N; 1.
DR Pfam; PF09263; PEX-2N; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amelogenesis imperfecta; ATP-binding; Cytoplasm;
KW Deafness; Disease variant; Membrane; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Peroxisome biogenesis disorder; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport;
KW Zellweger syndrome.
FT CHAIN 1..1283
FT /note="Peroxisome biogenesis factor 1"
FT /id="PRO_0000084604"
FT REGION 346..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 881..888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 92..413
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057136"
FT VARIANT 581
FT /note="R -> P (in HMLR1; results in mild functional
FT decrease in peroxisome biogenesis; dbSNP:rs370483961)"
FT /evidence="ECO:0000269|PubMed:26387595"
FT /id="VAR_074108"
FT VARIANT 590
FT /note="L -> R (in PBD-CG1)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058376"
FT VARIANT 593
FT /note="G -> R (in PBD-CG1; dbSNP:rs61750407)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058377"
FT VARIANT 634..690
FT /note="Missing (in PBD1A and PBD1B)"
FT /evidence="ECO:0000269|PubMed:9539740"
FT /id="VAR_014358"
FT VARIANT 640
FT /note="I -> R (in dbSNP:rs4559173)"
FT /id="VAR_048113"
FT VARIANT 664
FT /note="L -> P (in PBD1A and PBD1B; dbSNP:rs121434455)"
FT /evidence="ECO:0000269|PubMed:9539740"
FT /id="VAR_008876"
FT VARIANT 696
FT /note="I -> M (in dbSNP:rs35996821)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:19105186"
FT /id="VAR_034376"
FT VARIANT 705
FT /note="L -> W (in HMLR1; results in mild functional
FT decrease in peroxisome biogenesis; dbSNP:rs863225084)"
FT /evidence="ECO:0000269|PubMed:26387595"
FT /id="VAR_074109"
FT VARIANT 798
FT /note="R -> G (in PBD-CG1; dbSNP:rs61750419)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058378"
FT VARIANT 843
FT /note="G -> D (in PBD1A, PBD1B and PBD-CG1;
FT dbSNP:rs61750420)"
FT /evidence="ECO:0000269|PubMed:11439091,
FT ECO:0000269|PubMed:19105186, ECO:0000269|PubMed:9398847,
FT ECO:0000269|PubMed:9398848, ECO:0000269|PubMed:9539740"
FT /id="VAR_008877"
FT VARIANT 948
FT /note="R -> Q (in dbSNP:rs535271603)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058379"
FT VARIANT 989
FT /note="I -> T (in PBD1B and HMLR1; dbSNP:rs61750427)"
FT /evidence="ECO:0000269|PubMed:16088892,
FT ECO:0000269|PubMed:27302843"
FT /id="VAR_077503"
FT VARIANT 998
FT /note="R -> Q (in PBD1B; dbSNP:rs61750429)"
FT /evidence="ECO:0000269|PubMed:16088892"
FT /id="VAR_077504"
FT VARIANT 1008
FT /note="Missing (in PBD-CG1; dbSNP:rs62653599)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_075871"
FT VARIANT 1237
FT /note="A -> E (in PBD-CG1; dbSNP:rs1473858573)"
FT /evidence="ECO:0000269|PubMed:19105186"
FT /id="VAR_058380"
FT CONFLICT 79
FT /note="Q -> R (in Ref. 5; BAG58539)"
FT CONFLICT 897
FT /note="E -> G (in Ref. 5; BAG58539)"
SQ SEQUENCE 1283 AA; 142867 MW; 333CE0B15D2E2017 CRC64;
MWGSDRLAGA GGGGAAVTVA FTNARDCFLH LPRRLVAQLH LLQNQAIEVV WSHQPAFLSW
VEGRHFSDQG ENVAEINRQV GQKLGLSNGG QVFLKPCSHV VSCQQVEVEP LSADDWEILE
LHAVSLEQHL LDQIRIVFPK AIFPVWVDQQ TYIFIQIVAL IPAASYGRLE TDTKLLIQPK
TRRAKENTFS KADAEYKKLH SYGRDQKGMM KELQTKQLQS NTVGITESNE NESEIPVDSS
SVASLWTMIG SIFSFQSEKK QETSWGLTEI NAFKNMQSKV VPLDNIFRVC KSQPPSIYNA
SATSVFHKHC AIHVFPWDQE YFDVEPSFTV TYGKLVKLLS PKQQQSKTKQ NVLSPEKEKQ
MSEPLDQKKI RSDHNEEDEK ACVLQVVWNG LEELNNAIKY TKNVEVLHLG KVWIPDDLRK
RLNIEMHAVV RITPVEVTPK IPRSLKLQPR ENLPKDISEE DIKTVFYSWL QQSTTTMLPL
VISEEEFIKL ETKDGLKEFS LSIVHSWEKE KDKNIFLLSP NLLQKTTIQV LLDPMVKEEN
SEEIDFILPF LKLSSLGGVN SLGVSSLEHI THSLLGRPLS RQLMSLVAGL RNGALLLTGG
KGSGKSTLAK AICKEAFDKL DAHVERVDCK ALRGKRLENI QKTLEVAFSE AVWMQPSVVL
LDDLDLIAGL PAVPEHEHSP DAVQSQRLAH ALNDMIKEFI SMGSLVALIA TSQSQQSLHP
LLVSAQGVHI FQCVQHIQPP NQEQRCEILC NVIKNKLDCD INKFTDLDLQ HVAKETGGFV
ARDFTVLVDR AIHSRLSRQS ISTREKLVLT TLDFQKALRG FLPASLRSVN LHKPRDLGWD
KIGGLHEVRQ ILMDTIQLPA KYPELFANLP IRQRTGILLY GPPGTGKTLL AGVIARESRM
NFISVKGPEL LSKYIGASEQ AVRDIFIRAQ AAKPCILFFD EFESIAPRRG HDNTGVTDRV
VNQLLTQLDG VEGLQGVYVL AATSRPDLID PALLRPGRLD KCVYCPPPDQ VSRLEILNVL
SDSLPLADDV DLQHVASVTD SFTGADLKAL LYNAQLEALH GMLLSSGLQD GSSSSDSDLS
LSSMVFLNHS SGSDDSAGDG ECGLDQSLVS LEMSEILPDE SKFNMYRLYF GSSYESELGN
GTSSDLSSQC LSAPSSMTQD LPGVPGKDQL FSQPPVLRTA SQEGCQELTQ EQRDQLRADI
SIIKGRYRSQ SGEDESMNQP GPIKTRLAIS QSHLMTALGH TRPSISEDDW KNFAELYESF
QNPKRRKNQS GTMFRPGQKV TLA
