ID PEX5_HUMAN Reviewed; 639 AA. AC P50542; A8K891; B4DZ45; B7ZAD5; D3DUT8; Q15115; Q15266; Q96FN7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 3. DT 13-JUN-2012, entry version 133. DE RecName: Full=Peroxisomal targeting signal 1 receptor; DE Short=PTS1 receptor; DE Short=PTS1R; DE AltName: Full=PTS1-BP; DE AltName: Full=Peroxin-5; DE AltName: Full=Peroxisomal C-terminal targeting signal import receptor; DE AltName: Full=Peroxisome receptor 1; GN Name=PEX5; Synonyms=PXR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN ZWS, VARIANT RP NALD LYS-526, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX MEDLINE=95235555; PubMed=7719337; DOI=10.1038/ng0295-115; RA Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P., RA Valle D., Gould S.J.; RT "Mutations in the PTS1 receptor gene, PXR1, define complementation RT group 2 of the peroxisome biogenesis disorders."; RL Nat. Genet. 9:115-125(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX MEDLINE=95310365; PubMed=7790377; DOI=10.1083/jcb.130.1.51; RA Wiemer E.A.C., Nuttley W.M., Bertolaet B.L., Li X., Francke U., RA Wheelock M.J., Anne U.K., Johnson K.R., Subramani S.; RT "Human peroxisomal targeting signal-1 receptor restores peroxisomal RT protein import in cells from patients with fatal peroxisomal RT disorders."; RL J. Cell Biol. 130:51-65(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP AND SUBCELLULAR LOCATION. RC TISSUE=Liver; RX MEDLINE=95221441; PubMed=7706321; DOI=10.1074/jbc.270.13.7731; RA Fransen M., Brees C., Baumgart E., Vanhooren J.C.T., Baes M., RA Mannaerts G.P., van Veldhoven P.P.; RT "Identification and characterization of the putative human peroxisomal RT C-terminal targeting signal import receptor."; RL J. Biol. Chem. 270:7731-7736(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Eye; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH PEX12. RX PubMed=10562279; DOI=10.1083/jcb.147.4.761; RA Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J.; RT "PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor RT docking in peroxisomal matrix protein import."; RL J. Cell Biol. 147:761-774(1999). RN [9] RP INTERACTION WITH PEX14, AND MUTAGENESIS OF TRP-118 AND PHE-122. RX PubMed=11438541; DOI=10.1074/jbc.M104647200; RA Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W., RA Kunau W.-H., Schliebs W.; RT "The di-aromatic pentapeptide repeats of the human peroxisome import RT receptor PEX5 are separate high affinity binding sites for the RT peroxisomal membrane protein PEX14."; RL J. Biol. Chem. 276:34524-34529(2001). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639 IN COMPLEX WITH RP TARGETING PEPTIDE. RX PubMed=11101887; DOI=10.1038/81930; RA Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M.; RT "Peroxisomal targeting signal-1 recognition by the TPR domains of RT human PEX5."; RL Nat. Struct. Biol. 7:1091-1095(2000). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 321-639 IN COMPLEX WITH RP TARGETING PEPTIDE. RX PubMed=17157249; DOI=10.1016/j.molcel.2006.10.024; RA Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., RA Schliebs W., Sattler M., Wilmanns M.; RT "Recognition of a functional peroxisome type 1 target by the dynamic RT import receptor Pex5p."; RL Mol. Cell 24:653-663(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 315-639, AND BINDING TO RP C-TERMINAL TARGETING PEPTIDES. RX PubMed=17428317; DOI=10.1186/1472-6807-7-24; RA Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M., RA Kursula P.; RT "A previously unobserved conformation for the human Pex5p receptor RT suggests roles for intrinsic flexibility and rigid domain motions in RT ligand binding."; RL BMC Struct. Biol. 7:24-24(2007). RN [13] RP STRUCTURE BY NMR OF 108-127 IN COMPLEX WITH PEX14. RX PubMed=19197237; DOI=10.1038/emboj.2009.7; RA Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., RA Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., RA Sattler M.; RT "Structural basis for competitive interactions of Pex14 with the RT import receptors Pex5 and Pex19."; RL EMBO J. 28:745-754(2009). RN [14] RP VARIANT NALD LYS-526, VARIANT IRD TRP-600, CHARACTERIZATION OF VARIANT RP NALD LYS-526, AND CHARACTERIZATION OF VARIANT IRD TRP-600. RX PubMed=10462504; DOI=10.1006/bbrc.1999.1232; RA Shimozawa N., Zhang Z., Suzuki Y., Imamura A., Tsukamoto T., Osumi T., RA Fujiki Y., Orii T., Barth P.G., Wanders R.J., Kondo N.; RT "Functional heterogeneity of C-terminal peroxisome targeting signal 1 RT in PEX5-defective patients."; RL Biochem. Biophys. Res. Commun. 262:504-508(1999). CC -!- FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal CC targeting signal (SKL-type) and plays an essential role in CC peroxisomal protein import. CC -!- SUBUNIT: Interacts with PEX7 and PEX13 (By similarity). Interacts CC with PEX12 and PEX14. CC -!- INTERACTION: CC O00623:PEX12; NbExp=3; IntAct=EBI-597835, EBI-594836; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Peripheral CC membrane protein. Note=Its distribution appears to be dynamic. It CC is probably a cycling receptor found mainly in the cytoplasm and CC as well associated to the peroxisomal membrane through a docking CC factor (PEX13). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P50542-1; Sequence=Displayed; CC Name=2; CC IsoId=P50542-2; Sequence=VSP_021880; CC Name=3; CC IsoId=P50542-3; Sequence=VSP_024106; CC Name=4; CC IsoId=P50542-4; Sequence=VSP_043639; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, CC liver, skeletal muscle, kidney and pancreas. CC -!- DISEASE: Defects in PEX5 are a cause of adrenoleukodystrophy CC neonatal (NALD) [MIM:202370]. NALD is a peroxisome biogenesis CC disorder (PBD) characterized by the accumulation of very long- CC chain fatty acids, adrenal insufficiency and mental retardation. CC Inheritance is autosomal recessive. CC -!- DISEASE: Defects in PEX5 are a cause of Zellweger syndrome (ZWS) CC [MIM:214100]. ZWS is a fatal peroxisome biogenesis disorder CC characterized by dysmorphic facial features, hepatomegaly, ocular CC abnormalities, renal cysts, hearing impairment, profound CC psychomotor retardation, severe hypotonia and neonatal seizures. CC Death occurs within the first year of life. CC -!- DISEASE: Defects in PEX5 may be a cause of infantile Refsum CC disease (IRD) [MIM:266510]. IRD is a mild peroxisome biogenesis CC disorder (PBD). Clinical features include early onset, mental CC retardation, minor facial dysmorphism, retinopathy, sensorineural CC hearing deficit, hepatomegaly, osteoporosis, failure to thrive, CC and hypocholesterolemia. The biochemical abnormalities include CC accumulation of phytanic acid, very long chain fatty acids CC (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor CC family. CC -!- SIMILARITY: Contains 7 TPR repeats. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PEX5"; 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; U19721; AAC50103.1; -; mRNA. DR EMBL; Z48054; CAA88131.1; -; mRNA. DR EMBL; X84899; CAA59324.1; -; mRNA. DR EMBL; AK292256; BAF84945.1; -; mRNA. DR EMBL; AK302742; BAG63957.1; -; mRNA. DR EMBL; AK316250; BAH14621.1; -; mRNA. DR EMBL; AC018653; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471116; EAW88671.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88674.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88672.1; -; Genomic_DNA. DR EMBL; BC010621; AAH10621.1; -; mRNA. DR IPI; IPI00032931; -. DR IPI; IPI00165272; -. DR IPI; IPI00384805; -. DR IPI; IPI00940679; -. DR PIR; A56126; A56126. DR RefSeq; NP_000310.2; NM_000319.4. DR RefSeq; NP_001124495.1; NM_001131023.1. DR RefSeq; NP_001124496.1; NM_001131024.1. DR RefSeq; NP_001124497.1; NM_001131025.1. DR RefSeq; NP_001124498.1; NM_001131026.1. DR UniGene; Hs.567327; -. DR PDB; 1FCH; X-ray; 2.20 A; A/B=272-639. DR PDB; 2C0L; X-ray; 2.30 A; A=335-639. DR PDB; 2C0M; X-ray; 2.50 A; A/B/C/F=321-639. DR PDB; 2J9Q; X-ray; 2.65 A; A/B=315-639. DR PDB; 2W84; NMR; -; B=108-127. DR PDB; 3R9A; X-ray; 2.35 A; B/D=315-639. DR PDBsum; 1FCH; -. DR PDBsum; 2C0L; -. DR PDBsum; 2C0M; -. DR PDBsum; 2J9Q; -. DR PDBsum; 2W84; -. DR PDBsum; 3R9A; -. DR ProteinModelPortal; P50542; -. DR SMR; P50542; 335-639. DR IntAct; P50542; 16. DR MINT; MINT-241634; -. DR STRING; P50542; -. DR PhosphoSite; P50542; -. DR DMDM; 119364633; -. DR PRIDE; P50542; -. DR DNASU; 5830; -. DR Ensembl; ENST00000266563; ENSP00000266563; ENSG00000139197. DR Ensembl; ENST00000266564; ENSP00000266564; ENSG00000139197. DR Ensembl; ENST00000396637; ENSP00000379877; ENSG00000139197. DR Ensembl; ENST00000412720; ENSP00000391601; ENSG00000139197. DR Ensembl; ENST00000420616; ENSP00000410159; ENSG00000139197. DR Ensembl; ENST00000434354; ENSP00000407401; ENSG00000139197. DR Ensembl; ENST00000455147; ENSP00000400647; ENSG00000139197. DR GeneID; 5830; -. DR KEGG; hsa:5830; -. DR UCSC; uc001qsu.3; human. DR UCSC; uc001qsv.3; human. DR UCSC; uc001qsw.3; human. DR CTD; 5830; -. DR GeneCards; GC12P007341; -. DR HGNC; HGNC:9719; PEX5. DR HPA; HPA039259; -. DR MIM; 202370; phenotype. DR MIM; 214100; phenotype. DR MIM; 266510; phenotype. DR MIM; 600414; gene. DR neXtProt; NX_P50542; -. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA34063; -. DR eggNOG; COG0457; -. DR GeneTree; ENSGT00390000013941; -. DR HOGENOM; HOG000158146; -. DR HOVERGEN; HBG053575; -. DR InParanoid; P50542; -. DR KO; K13342; -. DR OrthoDB; EOG42V8FQ; -. DR EvolutionaryTrace; P50542; -. DR NextBio; 22716; -. DR ArrayExpress; P50542; -. DR Bgee; P50542; -. DR CleanEx; HS_PEX5; -. DR Genevestigator; P50542; -. DR GermOnline; ENSG00000139197; Homo sapiens. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IBA:RefGenome. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; IDA:UniProtKB. DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProtKB. DR GO; GO:0006625; P:protein targeting to peroxisome; IMP:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2. DR InterPro; IPR024111; PTS1R_family. DR InterPro; IPR001440; TPR-1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR10130; PTHR10130; 1. DR Pfam; PF00515; TPR_1; 3. DR SMART; SM00028; TPR; 4. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Disease mutation; Membrane; Peroxisome; KW Peroxisome biogenesis disorder; Protein transport; Reference proteome; KW Repeat; Thioester bond; TPR repeat; Transport; Ubl conjugation; KW Zellweger syndrome. FT CHAIN 1 639 Peroxisomal targeting signal 1 receptor. FT /FTId=PRO_0000106305. FT REPEAT 335 368 TPR 1. FT REPEAT 369 402 TPR 2. FT REPEAT 403 436 TPR 3. FT REPEAT 452 485 TPR 4. FT REPEAT 488 521 TPR 5. FT REPEAT 522 555 TPR 6. FT REPEAT 556 589 TPR 7. FT CROSSLNK 11 11 Glycyl cysteine thioester (Cys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VAR_SEQ 45 45 P -> PASEAVSVLEVESPGA (in isoform 4). FT /FTId=VSP_043639. FT VAR_SEQ 215 251 Missing (in isoform 2). FT /FTId=VSP_021880. FT VAR_SEQ 283 290 Missing (in isoform 3). FT /FTId=VSP_024106. FT VARIANT 526 526 N -> K (in NALD; strongly affects FT peroxisomal protein import). FT /FTId=VAR_007543. FT VARIANT 600 600 S -> W (in IRD; mildly affects FT peroxisomal protein import). FT /FTId=VAR_031328. FT MUTAGEN 118 118 W->A: Strongly reduced interaction with FT PEX14. FT MUTAGEN 122 122 F->A: Strongly reduced interaction with FT PEX14. FT CONFLICT 425 425 T -> I (in Ref. 1; AAC50103). FT HELIX 318 321 FT TURN 331 334 FT HELIX 338 347 FT HELIX 351 363 FT HELIX 369 381 FT HELIX 385 398 FT HELIX 403 415 FT HELIX 419 431 FT TURN 434 436 FT HELIX 437 439 FT HELIX 460 481 FT HELIX 488 500 FT HELIX 504 517 FT HELIX 522 534 FT HELIX 538 551 FT HELIX 556 569 FT HELIX 572 587 FT HELIX 601 614 FT HELIX 617 619 FT HELIX 620 624 FT HELIX 628 634 SQ SEQUENCE 639 AA; 70865 MW; 9D6951F58AED31AC CRC64; MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA EQWAAEFIQQ QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IESDVDFWDK LQAELEEMAK RDAEAHPWLS DYDDLTSATY DKGYQFEEEN PLRDHPQPFE EGLRRLQEGD LPNAVLLFEA AVQQDPKHME AWQYLGTTQA ENEQELLAIS ALRRCLELKP DNQTALMALA VSFTNESLQR QACETLRDWL RYTPAYAHLV TPAEEGAGGA GLGPSKRILG SLLSDSLFLE VKELFLAAVR LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLLWNKLGA TLANGNQSEE AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS ENIWSTLRLA LSMLGQSDAY GAADARDLST LLTMFGLPQ //