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 27-MAR-2024, entry version 203. DE RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000305}; DE EC=3.6.4.- {ECO:0000269|PubMed:16854980}; DE AltName: Full=Peroxin-1 {ECO:0000305}; DE AltName: Full=Peroxisome biogenesis disorder protein 1; DE AltName: Full=Peroxisome biogenesis factor 1 {ECO:0000305}; GN Name=PEX1 {ECO:0000303|PubMed:9398848, ECO:0000312|HGNC:HGNC:8850}; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP 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 SUBCELLULAR LOCATION, AND 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 FUNCTION. RX PubMed=16314507; DOI=10.1128/mcb.25.24.10822-10832.2005; RA Miyata N., Fujiki Y.; RT "Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: RT ATP-independent import and ATP-dependent export."; RL Mol. Cell. Biol. 25:10822-10832(2005). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PEX6, RP MUTAGENESIS OF LYS-605; ASP-662; LYS-887 AND ASP-940, AND CHARACTERIZATION RP OF VARIANT PBD1A PRO-664. RX PubMed=16854980; DOI=10.1074/jbc.m605159200; RA Tamura S., Yasutake S., Matsumoto N., Fujiki Y.; RT "Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and RT their membrane receptor Pex26p."; RL J. Biol. Chem. 281:27693-27704(2006). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PEX6, AND MUTAGENESIS OF RP LYS-605; ASP-662; LYS-887 AND ASP-940. RX PubMed=21362118; DOI=10.1111/j.1600-0854.2011.01182.x; RA Nashiro C., Kashiwagi A., Matsuzaki T., Tamura S., Fujiki Y.; RT "Recruiting mechanism of the AAA peroxins, Pex1p and Pex6p, to Pex26p on RT the peroxisomal membrane."; RL Traffic 12:774-788(2011). RN [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] RP FUNCTION. RX PubMed=29884772; DOI=10.1074/jbc.ra118.003669; RA Pedrosa A.G., Francisco T., Bicho D., Dias A.F., Barros-Barbosa A., RA Hagmann V., Dodt G., Rodrigues T.A., Azevedo J.E.; RT "Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and RT PEX6 and is unfolded during its dislocation into the cytosol."; RL J. Biol. Chem. 293:11553-11563(2018). RN [23] 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 [24] 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 [25] 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). RN [26] RP VARIANT PBD1A PRO-597. RX PubMed=32069232; DOI=10.1515/jpem-2019-0194; RA Havali C., Dorum S., Akbas Y., Goeruekmez O., Hirfanoglu T.; RT "Two different missense mutations of PEX genes in two similar patients with RT severe Zellweger syndrome: an argument on the genotype-phenotype RT correlation."; RL J. Pediatr. Endocrinol. Metab. 33:437-441(2020). RN [27] RP VARIANTS PBD1A TRP-949 AND ALA-970, AND CHARACTERIZATION OF VARIANTS PBD1A RP TRP-949 AND ALA-970. RX PubMed=33955040; DOI=10.1002/jcb.29945; RA Alamatsaz M., Jalalypour F., Hashemi M.S., Shafeghati Y., RA Nasr-Esfahani M.H., Ghaedi K.; RT "Compound heterozygous p. Arg949Trp and p. Gly970Ala mutations deteriorated RT the function of PEX1p: A study on PEX1 in a patient with Zellweger RT syndrome."; RL J. Cell. Biochem. 0:0-0(2021). RN [28] RP VARIANT PBD1A 684-GLN--ALA-1283 DEL. RX PubMed=33708531; DOI=10.21037/tp-20-167; RA Lu P., Ma L., Sun J., Gong X., Cai C.; RT "A Chinese newborn with Zellweger syndrome and compound heterozygous RT mutations novel in the PEX1 gene: a case report and literature review."; RL Transl. Pediatr. 10:446-453(2021). CC -!- FUNCTION: Component of the PEX1-PEX6 AAA ATPase complex, a protein CC dislocase complex that mediates the ATP-dependent extraction of the CC PEX5 receptor from peroxisomal membranes, an essential step for PEX5 CC recycling (PubMed:11439091, PubMed:16314507, PubMed:16854980, CC PubMed:21362118, PubMed:29884772). Specifically recognizes PEX5 CC monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen CC through the PEX2-PEX10-PEX12 retrotranslocation channel CC (PubMed:29884772). Extraction by the PEX1-PEX6 AAA ATPase complex is CC accompanied by unfolding of the TPR repeats and release of bound cargo CC from PEX5 (PubMed:29884772). {ECO:0000269|PubMed:11439091, CC ECO:0000269|PubMed:16314507, ECO:0000269|PubMed:16854980, CC ECO:0000269|PubMed:21362118, ECO:0000269|PubMed:29884772}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:16854980}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:16854980}; CC -!- SUBUNIT: Homooligomer; homooligomerizes in the cytosol, interaction CC with PEX6 promotes dissociation of the homooligomer (PubMed:16854980). CC Interacts with PEX6; forming the PEX1-PEX6 AAA ATPase complex, which is CC composed of a heterohexamer formed by a trimer of PEX1-PEX6 dimers CC (PubMed:12717447, PubMed:16854980, PubMed:21362118). Interacts CC indirectly with PEX26, via its interaction with PEX6 (PubMed:12717447). CC {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980, CC ECO:0000269|PubMed:21362118}. 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: MYL11; 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; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-988601, EBI-358545; 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; 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, cytosol {ECO:0000269|PubMed:16854980}. CC Peroxisome membrane {ECO:0000269|PubMed:11439091, CC ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980, CC ECO:0000269|PubMed:21362118}. Note=Associated with peroxisomal CC membranes; anchored by PEX26 to peroxisome membranes. CC {ECO:0000269|PubMed:12717447, ECO:0000269|PubMed:16854980}. 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:16854980, ECO:0000269|PubMed:32069232, CC ECO:0000269|PubMed:33708531, ECO:0000269|PubMed:33955040, CC 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 101. 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; 9606-ENSP00000248633; -. DR PeptideAtlas; O43933; -. DR ProteomicsDB; 19827; -. DR ProteomicsDB; 49243; -. [O43933-1] DR Pumba; O43933; -. DR Antibodypedia; 15612; 205 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 AGR; HGNC:8850; -. 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; 544017at2759; -. 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; 104 hits in 1162 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 187 other cell types or tissues. DR ExpressionAtlas; O43933; baseline and differential. 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:HPA. DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB. DR GO; GO:0140318; F:protein transporter activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0140036; F:ubiquitin-dependent protein 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:0016562; P:protein import into peroxisome matrix, receptor recycling; IDA:UniProtKB. DR GO; GO:0006625; P:protein targeting to peroxisome; IMP:UniProtKB. DR GO; GO:0043335; P:protein unfolding; IDA:UniProtKB. DR CDD; cd19526; RecA-like_PEX1_r2; 1. DR Gene3D; 1.10.8.60; -; 2. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PEX1-N-lobe. DR InterPro; IPR015342; PEX1-N_C-lobe. DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1. DR PANTHER; PTHR23077:SF12; PEROXISOME BIOGENESIS FACTOR 1; 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; ADC-like; 1. DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00674; AAA; 1. DR Genevisible; O43933; HS. PE 1: Evidence at protein level; KW Alternative splicing; Amelogenesis imperfecta; ATP-binding; Cytoplasm; KW Deafness; Disease variant; Hydrolase; Membrane; Nucleotide-binding; KW Peroxisome; Peroxisome biogenesis; Peroxisome biogenesis disorder; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; KW Zellweger syndrome. FT CHAIN 1..1283 FT /note="Peroxisomal ATPase PEX1" 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 597 FT /note="L -> P (in PBD1A)" FT /evidence="ECO:0000269|PubMed:32069232" FT /id="VAR_087133" 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; decreased binding to FT PEX6; impaired protein import into peroxisomes; FT dbSNP:rs121434455)" FT /evidence="ECO:0000269|PubMed:16854980, FT ECO:0000269|PubMed:9539740" FT /id="VAR_008876" FT VARIANT 684..1283 FT /note="Missing (in PBD1A)" FT /evidence="ECO:0000269|PubMed:33708531" FT /id="VAR_087134" 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 949 FT /note="R -> W (in PBD1A; impaired protein import into FT peroxisomes; dbSNP:rs866184460)" FT /evidence="ECO:0000269|PubMed:33955040" FT /id="VAR_087135" FT VARIANT 970 FT /note="G -> A (in PBD1A; impaired protein import into FT peroxisomes)" FT /evidence="ECO:0000269|PubMed:33955040" FT /id="VAR_087136" 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 MUTAGEN 605 FT /note="K->E: In A1 mutant; abolished ATP-binding; decreased FT interaction with PEX6; decreased localization to FT peroxisomal membranes." FT /evidence="ECO:0000269|PubMed:16854980, FT ECO:0000269|PubMed:21362118" FT MUTAGEN 662 FT /note="D->N: In B1 mutant; abolished ATP hydrolysis; FT decreased interaction with PEX6; decreased localization to FT peroxisomal membranes." FT /evidence="ECO:0000269|PubMed:16854980, FT ECO:0000269|PubMed:21362118" FT MUTAGEN 887 FT /note="K->E: In A2 mutant; abolished ATP-binding; decreased FT interaction with PEX6; decreased localization to FT peroxisomal membranes." FT /evidence="ECO:0000269|PubMed:16854980, FT ECO:0000269|PubMed:21362118" FT MUTAGEN 940 FT /note="D->N: In B2 mutant; abolished ATP hydrolysis; does FT not affect interaction with PEX6; does not affect FT localization to peroxisomal membranes." FT /evidence="ECO:0000269|PubMed:16854980, FT ECO:0000269|PubMed:21362118" 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 //