ID PEX5_MOUSE Reviewed; 639 AA. AC O09012; Q3UM58; Q8K2V5; Q91YC7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Peroxisomal targeting signal 1 receptor {ECO:0000305}; DE Short=PTS1 receptor; DE Short=PTS1R; DE AltName: Full=PTS1-BP; DE AltName: Full=PXR1P; DE AltName: Full=Peroxin-5 {ECO:0000305}; DE AltName: Full=Peroxisomal C-terminal targeting signal import receptor; DE AltName: Full=Peroxisome receptor 1; GN Name=Pex5 {ECO:0000303|PubMed:15732085, ECO:0000312|MGI:MGI:1098808}; GN Synonyms=Pxr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9288097; DOI=10.1038/ng0997-49; RA Baes M.I., Gressens P., Baumgart E., Carmeliet P., Casteels M., Fransen M., RA Evrard P., Fahimi D., Declercq P., Collen D., Vanveldhoven P., RA Mannaerts G.P.; RT "A mouse model for Zellweger syndrome."; RL Nat. Genet. 17:49-57(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Van Veldhoven P.P.; RT "Studies on mammalian peroxines."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Mammary gland; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=15732085; DOI=10.1002/hep.20628; RA Dirkx R., Vanhorebeek I., Martens K., Schad A., Grabenbauer M., Fahimi D., RA Declercq P., Van Veldhoven P.P., Baes M.; RT "Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER RT abnormalities."; RL Hepatology 41:868-878(2005). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=17442273; DOI=10.1016/j.bbrc.2007.03.198; RA Dirkx R., Meyhi E., Asselberghs S., Reddy J., Baes M., Van Veldhoven P.P.; RT "Beta-oxidation in hepatocyte cultures from mice with peroxisomal gene RT knockouts."; RL Biochem. Biophys. Res. Commun. 357:718-723(2007). RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=33389129; DOI=10.1007/s00439-020-02238-z; RA Ali M., Khan S.Y., Rodrigues T.A., Francisco T., Jiao X., Qi H., Kabir F., RA Irum B., Rauf B., Khan A.A., Mehmood A., Naeem M.A., Assir M.Z., Ali M.H., RA Shahzad M., Abu-Amero K.K., Akram S.J., Akram J., Riazuddin S., RA Riazuddin S., Robinson M.L., Baes M., Azevedo J.E., Hejtmancik J.F., RA Riazuddin S.A.; RT "A missense allele of PEX5 is responsible for the defective import of PTS2 RT cargo proteins into peroxisomes."; RL Hum. Genet. 140:649-666(2021). CC -!- FUNCTION: Receptor that mediates peroxisomal import of proteins CC containing a C-terminal PTS1-type tripeptide peroxisomal targeting CC signal (SKL-type). Binds to cargo proteins containing a PTS1 CC peroxisomal targeting signal in the cytosol, and translocates them into CC the peroxisome matrix by passing through the PEX13-PEX14 docking CC complex along with cargo proteins. PEX5 receptor is then CC retrotranslocated into the cytosol, leading to release of bound cargo CC in the peroxisome matrix, and reset for a subsequent peroxisome import CC cycle. {ECO:0000250|UniProtKB:P50542}. CC -!- FUNCTION: [Isoform 1]: In addition to promoting peroxisomal CC translocation of proteins containing a PTS1 peroxisomal targeting CC signal, mediates peroxisomal import of proteins containing a C-terminal CC PTS2-type peroxisomal targeting signal via its interaction with PEX7. CC Interaction with PEX7 only takes place when PEX7 is associated with CC cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 CC along with PTS2-containing cargo proteins are then translocated through CC the PEX13-PEX14 docking complex together with PEX5. CC {ECO:0000250|UniProtKB:P50542}. CC -!- FUNCTION: [Isoform 2]: Does not mediate translocation of peroxisomal CC import of proteins containing a C-terminal PTS2-type peroxisomal CC targeting signal. {ECO:0000250|UniProtKB:P50542}. CC -!- ACTIVITY REGULATION: Cys-11 acts as a sensor of redox state. In CC response to oxidative stress, monoubiquitination at Cys-11 is CC prevented. {ECO:0000250|UniProtKB:P50542}. CC -!- SUBUNIT: Interacts (via WxxxF/Y and LVxEF motifs) with PEX14; promoting CC translocation through the PEX13-PEX14 docking complex. Interacts with CC PEX12. Interacts (Cys-linked ubiquitinated) with ZFAND6. Interacts CC (when ubiquitinated at Lys-210) with p62/SQSTM1. Interacts with DDO; CC the interaction is direct and required for localization of DDO to the CC peroxisome. {ECO:0000250|UniProtKB:P50542}. CC -!- SUBUNIT: [Isoform 1]: Interacts with PEX7, promoting peroxisomal import CC of proteins containing a C-terminal PTS2-type peroxisomal targeting CC signal. {ECO:0000250|UniProtKB:P50542}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P50542}. Peroxisome matrix CC {ECO:0000250|UniProtKB:P50542}. Note=Cycles between the cytosol and the CC peroxisome matrix (By similarity). Following binding to cargo proteins CC containing a PTS1 peroxisomal targeting signal in the cytosol, CC recruited to the docking complex, composed of PEX13 and PEX14, leading CC to translocation into the peroxisome matrix along with cargo proteins. CC Export and recycling to the cytosol is initiated by binding to the CC PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that CC inserts into the ligase pore and emerges in the cytosol (By CC similarity). Cys-11 of PEX5 is then monoubiquitinated, promoting its CC extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase CC complex (By similarity). Extraction is accompanied by unfolding of the CC TPR repeats and release of bound cargo in the peroxisome matrix. The CC TPR repeats refold in the cytosol and ubiquitination is removed by CC deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle CC (By similarity). {ECO:0000250|UniProtKB:A0A1L8FDW4, CC ECO:0000250|UniProtKB:P50542}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long, PEX5L {ECO:0000250|UniProtKB:P50542}; CC IsoId=O09012-1; Sequence=Displayed; CC Name=2; Synonyms=PEX5S {ECO:0000250|UniProtKB:P50542}; CC IsoId=O09012-2; Sequence=VSP_024107; CC -!- DOMAIN: The TPR repeats mediate interaction with proteins containing a CC C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL- CC type). {ECO:0000250|UniProtKB:P50542}. CC -!- DOMAIN: The WxxxF/Y motifs mediate interaction with PEX14, promoting CC association with the PEX13-PEX14 docking complex. CC {ECO:0000250|UniProtKB:P50542}. CC -!- DOMAIN: The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are CC required for PEX5 retrotranslocation and recycling. AH2 mediates CC interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, CC while AH1 is required for extraction from peroxisomal membrane by the CC PEX1-PEX6 AAA ATPase complex. {ECO:0000250|UniProtKB:A0A1L8FDW4}. CC -!- PTM: Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through CC the retrotranslocation channel (By similarity). Cys-11 CC monoubiquitination acts as a recognition signal for the PEX1-PEX6 CC complex and is required for PEX5 extraction and export from CC peroxisomes. Monoubiquitination at Cys-11 is removed by USP9X in the CC cytosol, resetting PEX5 for a subsequent import cycle (By similarity). CC When PEX5 recycling is compromised, polyubiquitinated by PEX10 during CC its passage through the retrotranslocation channel, leading to its CC degradation (By similarity). Monoubiquitination at Lys-472 by TRIM37 CC promotes its stability by preventing its polyubiquitination and CC degradation by the proteasome. Ubiquitination at Lys-527 is not CC mediated by the PEX2-PEX10-PEX12 ligase complex and is not related to CC PEX5 recycling. Monoubiquitinated at Lys-210 by PEX2 following CC phosphorylation by ATM in response to starvation or reactive oxygen CC species (ROS), leading to PEX5 recognition by p62/SQSTM1 and induction CC of pexophagy (By similarity). {ECO:0000250|UniProtKB:P35056, CC ECO:0000250|UniProtKB:P50542}. CC -!- PTM: Phosphorylated at Ser-141 by ATM in response to reactive oxygen CC species (ROS), promoting monoubiquitination at Lys-210 and induction of CC pexophagy. {ECO:0000250|UniProtKB:P50542}. CC -!- DISRUPTION PHENOTYPE: Liver-specific knockout mice display a growth CC retardation from the third postnatal week resulting in a 30% to 40% CC lower body weight than control mice at the age of 7 weeks CC (PubMed:15732085). Thereafter, mice tend to catch up in growth, and by CC 3 months their weight is not different from control mice CC (PubMed:15732085). Throughout this period, the mice look healthy, are CC fertile and liver function is unaffected (PubMed:15732085). However, CC 10-week-old mutant mice display a severe hepatomegaly due to CC hypertrophic and hyperplastic hepatocytes (PubMed:15732085). Mutant CC mice survive but develope extensive liver tumors from 12 months on CC (PubMed:15732085). Peroxisomes are absent in mutant hepatocytes and CC multiple ultrastructural alterations are noticed, smooth endoplasmic CC reticulum proliferation, and accumulation of lipid droplets and CC lysosomes (PubMed:15732085). Most prominent is the abnormal structure CC of the inner mitochondrial membrane (PubMed:15732085). This is CC accompanied by severely reduced activities of complex I, III, and V and CC a collapse of the mitochondrial inner membrane potential CC (PubMed:15732085). Liver-specific knockout mice display severely CC impaired oxidation of 2-methylhexadecanoic acid, the bile acid CC intermediate trihydroxycholestanoic acid (THCA), and tetradecanedioic CC acid (PubMed:17442273). In contrast, mitochondrial beta-oxidation rates CC of palmitate are doubled (PubMed:17442273). Lens-specific knockout mice CC develop cataracts (PubMed:33389129). {ECO:0000269|PubMed:15732085, CC ECO:0000269|PubMed:17442273, ECO:0000269|PubMed:33389129}. CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor CC family. {ECO:0000305}. 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; Z97018; CAB09694.1; -; mRNA. DR EMBL; AJ416473; CAC94925.1; -; mRNA. DR EMBL; AK088886; BAC40632.1; -; mRNA. DR EMBL; AK145111; BAE26240.1; -; mRNA. DR EMBL; AK145361; BAE26388.1; -; mRNA. DR EMBL; AK161470; BAE36414.1; -; mRNA. DR EMBL; BC029748; AAH29748.1; -; mRNA. DR CCDS; CCDS20517.1; -. [O09012-1] DR CCDS; CCDS20518.1; -. [O09012-2] DR RefSeq; NP_001264259.1; NM_001277330.1. [O09012-2] DR RefSeq; NP_001264734.1; NM_001277805.1. [O09012-1] DR RefSeq; NP_033021.2; NM_008995.2. [O09012-1] DR RefSeq; NP_787947.1; NM_175933.2. [O09012-2] DR RefSeq; XP_006505821.1; XM_006505758.3. DR RefSeq; XP_006505822.1; XM_006505759.3. DR RefSeq; XP_017176951.1; XM_017321462.1. DR AlphaFoldDB; O09012; -. DR SMR; O09012; -. DR BioGRID; 202526; 6. DR IntAct; O09012; 7. DR MINT; O09012; -. DR STRING; 10090.ENSMUSP00000108151; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR GlyGen; O09012; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O09012; -. DR PhosphoSitePlus; O09012; -. DR SwissPalm; O09012; -. DR EPD; O09012; -. DR jPOST; O09012; -. DR MaxQB; O09012; -. DR PaxDb; 10090-ENSMUSP00000079398; -. DR PeptideAtlas; O09012; -. DR ProteomicsDB; 288042; -. [O09012-1] DR ProteomicsDB; 288043; -. [O09012-2] DR Pumba; O09012; -. DR Antibodypedia; 22900; 330 antibodies from 32 providers. DR DNASU; 19305; -. DR Ensembl; ENSMUST00000035861.6; ENSMUSP00000049132.6; ENSMUSG00000005069.13. [O09012-1] DR Ensembl; ENSMUST00000080557.12; ENSMUSP00000079398.6; ENSMUSG00000005069.13. [O09012-2] DR Ensembl; ENSMUST00000112531.8; ENSMUSP00000108150.2; ENSMUSG00000005069.13. [O09012-2] DR Ensembl; ENSMUST00000112532.8; ENSMUSP00000108151.2; ENSMUSG00000005069.13. [O09012-1] DR GeneID; 19305; -. DR KEGG; mmu:19305; -. DR UCSC; uc009dqs.1; mouse. [O09012-1] DR UCSC; uc009dqt.1; mouse. [O09012-2] DR AGR; MGI:1098808; -. DR CTD; 5830; -. DR MGI; MGI:1098808; Pex5. DR VEuPathDB; HostDB:ENSMUSG00000005069; -. DR eggNOG; KOG1125; Eukaryota. DR GeneTree; ENSGT00940000156605; -. DR HOGENOM; CLU_013516_4_0_1; -. DR InParanoid; O09012; -. DR OMA; NYRMKGP; -. DR OrthoDB; 2020042at2759; -. DR PhylomeDB; O09012; -. DR TreeFam; TF315044; -. DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-MMU-9033241; Peroxisomal protein import. DR Reactome; R-MMU-9664873; Pexophagy. DR BioGRID-ORCS; 19305; 10 hits in 76 CRISPR screens. DR ChiTaRS; Pex5; mouse. DR PRO; PR:O09012; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; O09012; Protein. DR Bgee; ENSMUSG00000005069; Expressed in cortical plate and 262 other cell types or tissues. DR ExpressionAtlas; O09012; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI. DR GO; GO:0005777; C:peroxisome; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISS:UniProtKB. DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; ISO:MGI. DR GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:MGI. DR GO; GO:0140597; F:protein carrier chaperone; ISS:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; ISO:MGI. DR GO; GO:0048468; P:cell development; IMP:MGI. DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI. DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI. DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI. DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI. DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI. DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:MGI. DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI. DR GO; GO:0050905; P:neuromuscular process; IMP:MGI. DR GO; GO:0001764; P:neuron migration; IMP:MGI. DR GO; GO:0007031; P:peroxisome organization; IDA:MGI. DR GO; GO:0000425; P:pexophagy; ISS:UniProtKB. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; ISO:MGI. DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; ISS:UniProtKB. DR GO; GO:0044721; P:protein import into peroxisome matrix, substrate release; ISS:UniProtKB. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISO:MGI. DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:MGI. DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISO:MGI. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:MGI. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR024111; PEX5/PEX5L. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR10130:SF2; PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR; 1. DR PANTHER; PTHR10130; PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR PEX5; 1. DR Pfam; PF13432; TPR_16; 2. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. DR Genevisible; O09012; MM. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Isopeptide bond; Peroxisome; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Thioester bond; TPR repeat; Translocation; Transport; Ubl conjugation. FT CHAIN 1..639 FT /note="Peroxisomal targeting signal 1 receptor" FT /id="PRO_0000106306" FT REPEAT 337..370 FT /note="TPR 1" FT REPEAT 371..404 FT /note="TPR 2" FT REPEAT 405..438 FT /note="TPR 3" FT REPEAT 452..485 FT /note="TPR 4" FT REPEAT 488..521 FT /note="TPR 5" FT REPEAT 522..555 FT /note="TPR 6" FT REPEAT 556..589 FT /note="TPR 7" FT REGION 11..33 FT /note="Amphipathic helix 1 (AH1)" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT REGION 81..99 FT /note="Amphipathic helix 2 (AH2)" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT REGION 191..207 FT /note="Amphipathic helix 3 (AH3)" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT REGION 286..302 FT /note="Amphipathic helix 4 (AH4)" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 62..66 FT /note="LVxEF motif" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOTIF 118..122 FT /note="WxxxF/Y motif 1" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 140..144 FT /note="WxxxF/Y motif 2" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 159..163 FT /note="WxxxF/Y motif 3" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 185..189 FT /note="WxxxF/Y motif 4" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 244..248 FT /note="WxxxF/Y motif 5" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 258..262 FT /note="WxxxF/Y motif 6" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT MOTIF 310..314 FT /note="WxxxF/Y motif 7" FT /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4" FT SITE 11 FT /note="Sensor of redox state" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50542" FT CROSSLNK 11 FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q920N5" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P50542" FT CROSSLNK 472 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P50542" FT CROSSLNK 527 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P50542" FT VAR_SEQ 216..252 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2" FT /id="VSP_024107" FT CONFLICT 139 FT /note="D -> H (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="D -> G (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="S -> F (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="D -> N (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="Q -> R (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="H -> N (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="Y -> S (in Ref. 1; CAB09694)" FT /evidence="ECO:0000305" FT CONFLICT 473 FT /note="D -> E (in Ref. 2; BAE26240)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="M -> L (in Ref. 2; BAE26240)" FT /evidence="ECO:0000305" SQ SEQUENCE 639 AA; 70756 MW; A7013FF02926803C CRC64; MAMRELVEGE CGGANPLMKL ATHFTQDKAL RQEGLRPGPW PPGASAAETV SKPLGVGTED ELVSEFLQDQ NATLVSRAPQ TFKMDDLLAE MQEIEQSNFR QAPQRAPGVA DLALSENWAQ EFLAAGDAVD VAQDYNETDW SQEFIAEVTD PLSVSPARWA EEYLEQSEEK LWLGDQEGSS TADRWYDEYH PEEDLQHTAS DFVSKVDDPK LANSEFLKFV RQIGEGQVSL ESAAGSGGAQ AEQWAAEFIQ QQGTSEAWVD QFTRPGNKIA ALQVEFERAK SAIESDVDFW DKLQAELEEM AKRDAEAHPW LSDYDDLTSA SYDKGYQFEE ENPLRDHPQP FEEGLHRLEE GDLPNAVLLF EAAVQQDPKH MEAWQYLGTT QAENEQELLA ISALRRCLEL KPDNRTALMA LAVSFTNESL QRQACETLRD WLRYSPAYAH LVAPGEEGAT GAGPSKRILG SLLSDSLFLE VKDLFLAAVR LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLMWNKLGA TLANGNQSEE AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS ENIWSTLRLA LSMLGQSDAY GAADARDLSA LLAMFGLPQ //