ID PEX7_HUMAN Reviewed; 323 AA. AC O00628; C0H5X6; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Peroxisomal targeting signal 2 receptor {ECO:0000305}; DE Short=PTS2 receptor {ECO:0000303|PubMed:9090381}; DE AltName: Full=Peroxin-7 {ECO:0000305}; GN Name=PEX7 {ECO:0000303|PubMed:9090383, ECO:0000312|HGNC:HGNC:8860}; GN Synonyms=PTS2R; 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 INVOLVEMENT IN RCDP1. RX PubMed=9090383; DOI=10.1038/ng0497-381; RA Purdue P.E., Zhang J.W., Skoneczny M., Lazarow P.B.; RT "Rhizomelic chondrodysplasia punctata is caused by deficiency of human RT PEX7, a homologue of the yeast PTS2 receptor."; RL Nat. Genet. 15:381-384(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP VARIANTS RCDP1 ARG-217 AND VAL-218. RC TISSUE=Retina; RX PubMed=9090381; DOI=10.1038/ng0497-369; RA Braverman N., Steel G., Obie C., Moser A., Moser H., Gould S.J., Valle D.; RT "Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for RT rhizomelic chondrodysplasia punctata."; RL Nat. Genet. 15:369-376(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10673331; DOI=10.1006/geno.1999.6080; RA Braverman N., Steel G., Lin P., Moser A., Moser H., Valle D.; RT "PEX7 gene structure, alternative transcripts, and evidence for a founder RT haplotype for the frequent RCDP allele, L292ter."; RL Genomics 63:181-192(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PEX5. RX PubMed=11546814; DOI=10.1074/jbc.m106932200; RA Dodt G., Warren D., Becker E., Rehling P., Gould S.J.; RT "Domain mapping of human PEX5 reveals functional and structural RT similarities to Saccharomyces cerevisiae Pex18p and Pex21p."; RL J. Biol. Chem. 276:41769-41781(2001). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11931631; DOI=10.1042/bj20011432; RA Ghys K., Fransen M., Mannaerts G.P., Van Veldhoven P.P.; RT "Functional studies on human Pex7p: subcellular localization and RT interaction with proteins containing a peroxisome-targeting signal type 2 RT and other peroxins."; RL Biochem. J. 365:41-50(2002). RN [9] RP FUNCTION, AND MUTAGENESIS OF GLU-113; GLU-200 AND GLU-287. RX PubMed=22057399; DOI=10.1074/jbc.m111.301853; RA Kunze M., Neuberger G., Maurer-Stroh S., Ma J., Eck T., Braverman N., RA Schmid J.A., Eisenhaber F., Berger J.; RT "Structural requirements for interaction of peroxisomal targeting signal 2 RT and its receptor PEX7."; RL J. Biol. Chem. 286:45048-45062(2011). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5, AND MUTAGENESIS OF RP GLU-113; GLU-200 AND GLU-287. RX PubMed=25538232; DOI=10.1074/jbc.m114.601575; RA Kunze M., Malkani N., Maurer-Stroh S., Wiesinger C., Schmid J.A., RA Berger J.; RT "Mechanistic insights into PTS2-mediated peroxisomal protein import: the RT co-receptor PEX5L drastically increases the interaction strength between RT the cargo protein and the receptor PEX7."; RL J. Biol. Chem. 290:4928-4940(2015). RN [11] RP INTERACTION WITH VWA8. RX PubMed=30204880; DOI=10.1093/jb/mvy073; RA Niwa H., Miyauchi-Nanri Y., Okumoto K., Mukai S., Noi K., Ogura T., RA Fujiki Y.; RT "A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel RT dynein-type AAA+ protein."; RL J. Biochem. 164:437-447(2018). RN [12] RP INTERACTION WITH PEX5. 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). RN [13] RP VARIANT PBD9B PRO-14. RX PubMed=12522768; DOI=10.1086/346093; RA van den Brink D.M., Brites P., Haasjes J., Wierzbicki A.S., Mitchell J., RA Lambert-Hamill M., de Belleroche J., Jansen G.A., Waterham H.R., RA Wanders R.J.A.; RT "Identification of PEX7 as the second gene involved in Refsum disease."; RL Am. J. Hum. Genet. 72:471-477(2003). CC -!- FUNCTION: Receptor required for the peroxisomal import of proteins CC containing a C-terminal PTS2-type peroxisomal targeting signal CC (PubMed:9090381, PubMed:11931631, PubMed:22057399, PubMed:25538232). CC Specifically binds to cargo proteins containing a PTS2 peroxisomal CC targeting signal in the cytosol (PubMed:11931631, PubMed:22057399, CC PubMed:25538232). Cargo protein-binding triggers interaction with PEX5 CC and formation of a ternary complex composed of PEX5 and PEX7 along with CC PTS2-containing cargo proteins, which is tranlocated into peroxisomes CC by passing through the PEX13-PEX14 docking complex (PubMed:11546814, CC PubMed:25538232). {ECO:0000269|PubMed:11546814, CC ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:22057399, CC ECO:0000269|PubMed:25538232, ECO:0000269|PubMed:9090381}. CC -!- SUBUNIT: Interacts with PEX5; interaction only takes place when PEX7 is CC associated with cargo proteins (PubMed:11546814, PubMed:33389129, CC PubMed:25538232). Interacts with VWA8 (PubMed:30204880). CC {ECO:0000269|PubMed:11546814, ECO:0000269|PubMed:25538232, CC ECO:0000269|PubMed:30204880, ECO:0000269|PubMed:33389129}. CC -!- INTERACTION: CC O00628; O75925: PIAS1; NbExp=3; IntAct=EBI-5238811, EBI-629434; CC O00628-2; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-25882083, EBI-2410266; CC O00628-2; Q96EL1: INKA1; NbExp=3; IntAct=EBI-25882083, EBI-10285157; CC O00628-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-25882083, EBI-11959123; CC O00628-2; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-25882083, EBI-357085; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11931631, CC ECO:0000269|PubMed:25538232}. Peroxisome matrix CC {ECO:0000269|PubMed:11546814, ECO:0000269|PubMed:11931631, CC ECO:0000269|PubMed:25538232}. Note=Translocated into the peroxisome CC matrix together with PTS2-containing cargo proteins and PEX5. CC {ECO:0000269|PubMed:25538232}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00628-1; Sequence=Displayed; CC Name=2; CC IsoId=O00628-2; Sequence=VSP_056393; CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:9090381). Highest expression in CC pancreas, skeletal muscle and heart (PubMed:9090381). CC {ECO:0000269|PubMed:9090381}. CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 11 (PBD- CC CG11) [MIM:614879]: 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 Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Rhizomelic chondrodysplasia punctata 1 (RCDP1) [MIM:215100]: A CC peroxisome biogenesis disorder. It is characterized by severely CC disturbed endochondral bone formation, rhizomelic shortening of femur CC and humerus, vertebral disorders, dwarfism, cataract, cutaneous CC lesions, facial dysmorphism, and severe intellectual disability with CC spasticity. {ECO:0000269|PubMed:9090381, ECO:0000269|PubMed:9090383}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 9B (PBD9B) [MIM:614879]: A CC peroxisome biogenesis disorder with unusually mild clinical and CC biochemical manifestations. Affected individuals manifest a variable CC phenotype similar to, and in some cases indistinguishable from, classic CC Refsum disease. Variable features include ocular abnormalities, CC sensorimotor neuropathy, ichthyosis, deafness, chondrodysplasia CC punctata without rhizomelia or growth failure. CC {ECO:0000269|PubMed:12522768}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the WD repeat peroxin-7 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; U88871; AAC51238.1; -; mRNA. DR EMBL; U76560; AAB50556.1; -; mRNA. DR EMBL; AF180814; AAF37350.1; -; Genomic_DNA. DR EMBL; AF180806; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180807; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180808; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180809; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180810; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180811; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180812; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AF180813; AAF37350.1; JOINED; Genomic_DNA. DR EMBL; AL121933; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL357082; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47941.1; -; Genomic_DNA. DR EMBL; BC006268; AAH06268.1; -; mRNA. DR EMBL; BC031606; AAH31606.1; -; mRNA. DR CCDS; CCDS5180.1; -. [O00628-1] DR RefSeq; NP_000279.1; NM_000288.3. [O00628-1] DR AlphaFoldDB; O00628; -. DR SMR; O00628; -. DR BioGRID; 111214; 39. DR IntAct; O00628; 27. DR MINT; O00628; -. DR STRING; 9606.ENSP00000315680; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR iPTMnet; O00628; -. DR PhosphoSitePlus; O00628; -. DR BioMuta; PEX7; -. DR EPD; O00628; -. DR jPOST; O00628; -. DR MassIVE; O00628; -. DR MaxQB; O00628; -. DR PaxDb; 9606-ENSP00000315680; -. DR PeptideAtlas; O00628; -. DR ProteomicsDB; 48001; -. [O00628-1] DR ProteomicsDB; 7570; -. DR Pumba; O00628; -. DR ABCD; O00628; 1 sequenced antibody. DR Antibodypedia; 33017; 188 antibodies from 34 providers. DR DNASU; 5191; -. DR Ensembl; ENST00000318471.5; ENSP00000315680.3; ENSG00000112357.14. [O00628-1] DR Ensembl; ENST00000541292.6; ENSP00000441004.1; ENSG00000112357.14. [O00628-2] DR GeneID; 5191; -. DR KEGG; hsa:5191; -. DR MANE-Select; ENST00000318471.5; ENSP00000315680.3; NM_000288.4; NP_000279.1. DR UCSC; uc063rtk.1; human. [O00628-1] DR AGR; HGNC:8860; -. DR CTD; 5191; -. DR DisGeNET; 5191; -. DR GeneCards; PEX7; -. DR GeneReviews; PEX7; -. DR HGNC; HGNC:8860; PEX7. DR HPA; ENSG00000112357; Low tissue specificity. DR MalaCards; PEX7; -. DR MIM; 215100; phenotype. DR MIM; 601757; gene. DR MIM; 614879; phenotype. DR neXtProt; NX_O00628; -. DR OpenTargets; ENSG00000112357; -. DR Orphanet; 773; Refsum disease. DR Orphanet; 309789; Rhizomelic chondrodysplasia punctata type 1. DR PharmGKB; PA33202; -. DR VEuPathDB; HostDB:ENSG00000112357; -. DR eggNOG; KOG0277; Eukaryota. DR GeneTree; ENSGT00940000157264; -. DR HOGENOM; CLU_046581_0_1_1; -. DR InParanoid; O00628; -. DR OMA; FAVHWNL; -. DR OrthoDB; 5474268at2759; -. DR PhylomeDB; O00628; -. DR TreeFam; TF323220; -. DR PathwayCommons; O00628; -. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; O00628; -. DR SIGNOR; O00628; -. DR BioGRID-ORCS; 5191; 32 hits in 1163 CRISPR screens. DR ChiTaRS; PEX7; human. DR GenomeRNAi; 5191; -. DR Pharos; O00628; Tbio. DR PRO; PR:O00628; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O00628; Protein. DR Bgee; ENSG00000112357; Expressed in pigmented layer of retina and 189 other cell types or tissues. DR ExpressionAtlas; O00628; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0005053; F:peroxisome matrix targeting signal-2 binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl. DR GO; GO:0008611; P:ether lipid biosynthetic process; IMP:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB. DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:UniProtKB. DR GO; GO:0006625; P:protein targeting to peroxisome; IEA:Ensembl. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR044536; PEX7. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR46027; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; 1. DR PANTHER; PTHR46027:SF1; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; 1. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; O00628; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cataract; Cytoplasm; Deafness; Disease variant; KW Ichthyosis; Peroxisome; Peroxisome biogenesis disorder; Protein transport; KW Reference proteome; Repeat; Retinitis pigmentosa; KW Rhizomelic chondrodysplasia punctata; Transport; WD repeat. FT CHAIN 1..323 FT /note="Peroxisomal targeting signal 2 receptor" FT /id="PRO_0000051116" FT REPEAT 65..96 FT /note="WD 1" FT REPEAT 109..141 FT /note="WD 2" FT REPEAT 153..184 FT /note="WD 3" FT REPEAT 196..227 FT /note="WD 4" FT REPEAT 240..271 FT /note="WD 5" FT REPEAT 284..315 FT /note="WD 6" FT VAR_SEQ 250..323 FT /note="FSPFHASVLASCSYDFTVRFWNFSKPDSLLETVEHHTEFTCGLDFSLQSPTQ FT VADCSWDETIKIYDPACLTIPA -> MESCPVTQTRSQLTATSAFWVQAVLLPQPTE FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056393" FT VARIANT 14 FT /note="T -> P (in PBD9B; dbSNP:rs61753233)" FT /evidence="ECO:0000269|PubMed:12522768" FT /id="VAR_016810" FT VARIANT 217 FT /note="G -> R (in RCDP1; uncertain significance; FT dbSNP:rs121909152)" FT /evidence="ECO:0000269|PubMed:9090381" FT /id="VAR_007725" FT VARIANT 218 FT /note="A -> V (in RCDP1; dbSNP:rs121909151)" FT /evidence="ECO:0000269|PubMed:9090381" FT /id="VAR_007726" FT MUTAGEN 113 FT /note="E->R: Impaired binding to cargo proteins containing FT a PTS2 peroxisomal targeting signal." FT /evidence="ECO:0000269|PubMed:22057399, FT ECO:0000269|PubMed:25538232" FT MUTAGEN 200 FT /note="E->R: Impaired binding to cargo proteins containing FT a PTS2 peroxisomal targeting signal." FT /evidence="ECO:0000269|PubMed:22057399, FT ECO:0000269|PubMed:25538232" FT MUTAGEN 287 FT /note="E->R: Impaired interaction with PEX5, leading to FT decreased peroxisomal import of proteins containing a PTS2 FT peroxisomal targeting signal." FT /evidence="ECO:0000269|PubMed:22057399, FT ECO:0000269|PubMed:25538232" SQ SEQUENCE 323 AA; 35892 MW; D405387F7F14B432 CRC64; MSAVCGGAAR MLRTPGRHGY AAEFSPYLPG RLACATAQHY GIAGCGTLLI LDPDEAGLRL FRSFDWNDGL FDVTWSENNE HVLITCSGDG SLQLWDTAKA AGPLQVYKEH AQEVYSVDWS QTRGEQLVVS GSWDQTVKLW DPTVGKSLCT FRGHESIIYS TIWSPHIPGC FASASGDQTL RIWDVKAAGV RIVIPAHQAE ILSCDWCKYN ENLLVTGAVD CSLRGWDLRN VRQPVFELLG HTYAIRRVKF SPFHASVLAS CSYDFTVRFW NFSKPDSLLE TVEHHTEFTC GLDFSLQSPT QVADCSWDET IKIYDPACLT IPA //