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 23-FEB-2022, entry version 215. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN PBD2A, VARIANT PBD2B RP LYS-526, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=7719337; DOI=10.1038/ng0295-115; RA Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P., Valle D., RA Gould S.J.; RT "Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 RT of the peroxisome biogenesis disorders."; RL Nat. Genet. 9:115-125(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX 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 protein RT import in cells from patients with fatal peroxisomal disorders."; RL J. Cell Biol. 130:51-65(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC TISSUE=Liver; RX 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 C- RT 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., 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 [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., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., 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., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., 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., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA 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., 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 [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 project: RT 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 peroxisomal RT membrane protein PEX14."; RL J. Biol. Chem. 276:34524-34529(2001). RN [10] RP INTERACTION WITH ZFAND6. RX PubMed=21980954; DOI=10.1111/j.1600-0854.2011.01298.x; RA Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.; RT "AWP1/ZFAND6 functions in Pex5 export by interacting with cys- RT monoubiquitinated Pex5 and Pex6 AAA ATPase."; RL Traffic 13:168-183(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-153; SER-155; RP SER-167 AND SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP INVOLVEMENT IN RCDP5. RX PubMed=26220973; DOI=10.1093/hmg/ddv305; RA Baroey T., Koster J., Stroemme P., Ebberink M.S., Misceo D., RA Ferdinandusse S., Holmgren A., Hughes T., Merckoll E., Westvik J., RA Woldseth B., Walter J., Wood N., Tvedt B., Stadskleiv K., Wanders R.J., RA Waterham H.R., Frengen E.; RT "A novel type of rhizomelic chondrodysplasia punctata, RCDP5, is caused by RT loss of the PEX5 long isoform."; RL Hum. Mol. Genet. 24:5845-5854(2015). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639 IN COMPLEX WITH TARGETING RP 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 human RT PEX5."; RL Nat. Struct. Biol. 7:1091-1095(2000). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 321-639 IN COMPLEX WITH TARGETING RP 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 import RT receptor Pex5p."; RL Mol. Cell 24:653-663(2006). RN [16] 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 suggests RT roles for intrinsic flexibility and rigid domain motions in ligand RT binding."; RL BMC Struct. Biol. 7:24-24(2007). RN [17] 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., Sattler M.; RT "Structural basis for competitive interactions of Pex14 with the import RT receptors Pex5 and Pex19."; RL EMBO J. 28:745-754(2009). RN [18] RP VARIANTS PBD2B LYS-526 AND TRP-600, AND CHARACTERIZATION OF VARIANTS PBD2B RP LYS-526 AND 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 in RT 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 peroxisomal CC protein import. {ECO:0000269|PubMed:7706321, CC ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}. CC -!- SUBUNIT: Interacts with PEX7 and PEX13 (By similarity). Interacts with CC PEX12 and PEX14. Interacts (Cys-linked ubiquitinated) with ZFAND6. CC Interacts with VWA8 in a PEX7-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:Q920N5, ECO:0000269|PubMed:10562279, CC ECO:0000269|PubMed:11101887, ECO:0000269|PubMed:11438541, CC ECO:0000269|PubMed:17157249, ECO:0000269|PubMed:19197237, CC ECO:0000269|PubMed:21980954}. CC -!- INTERACTION: CC P50542; O14734: ACOT8; NbExp=3; IntAct=EBI-597835, EBI-1237371; CC P50542; Q6IMN6: CAPRIN2; NbExp=3; IntAct=EBI-597835, EBI-6918449; CC P50542; Q49A88: CCDC14; NbExp=3; IntAct=EBI-597835, EBI-751035; CC P50542; Q8WTR4: GDPD5; NbExp=3; IntAct=EBI-597835, EBI-2833203; CC P50542; P07195: LDHB; NbExp=3; IntAct=EBI-597835, EBI-358748; CC P50542; Q6NSB6: MKRN3; NbExp=3; IntAct=EBI-597835, EBI-10195599; CC P50542; O00623: PEX12; NbExp=4; IntAct=EBI-597835, EBI-594836; CC P50542; O75381: PEX14; NbExp=13; IntAct=EBI-597835, EBI-594898; CC P50542; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-597835, EBI-740924; CC P50542; Q6IPH7: RPL14; NbExp=3; IntAct=EBI-597835, EBI-7813901; CC P50542; P06703: S100A6; NbExp=3; IntAct=EBI-597835, EBI-352877; CC P50542; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-597835, EBI-717399; CC P50542; Q8N5N8: TM6SF1; NbExp=3; IntAct=EBI-597835, EBI-10266890; CC P50542; Q75MR5: TOM7; NbExp=3; IntAct=EBI-597835, EBI-10255903; CC P50542; Q68DY9: ZNF772; NbExp=3; IntAct=EBI-597835, EBI-10249148; CC P50542; A8K3Q9; NbExp=3; IntAct=EBI-597835, EBI-10174314; CC P50542-1; P21549: AGXT; NbExp=4; IntAct=EBI-15982193, EBI-727098; CC P50542-3; A0A0S2Z6F4: ANKRD50; NbExp=3; IntAct=EBI-12181987, EBI-16433393; CC P50542-3; Q92990: GLMN; NbExp=3; IntAct=EBI-12181987, EBI-726150; CC P50542-3; P31943: HNRNPH1; NbExp=3; IntAct=EBI-12181987, EBI-351590; CC P50542-3; P07602: PSAP; NbExp=3; IntAct=EBI-12181987, EBI-716699; CC P50542-3; Q96FV2: SCRN2; NbExp=3; IntAct=EBI-12181987, EBI-11306862; CC P50542-3; Q13501: SQSTM1; NbExp=2; IntAct=EBI-12181987, EBI-307104; CC P50542-3; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-12181987, EBI-6268651; CC P50542-3; Q9H8U3: ZFAND3; NbExp=3; IntAct=EBI-12181987, EBI-725171; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7719337}. CC Peroxisome membrane {ECO:0000269|PubMed:7706321, CC ECO:0000269|PubMed:7719337}; Peripheral membrane protein. Note=Its CC distribution appears to be dynamic. It is probably a cycling receptor CC found mainly in the cytoplasm and as well associated to the peroxisomal CC membrane through a docking 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 -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver, CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:7706321, CC ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}. CC -!- PTM: Monoubiquitination at Cys-11 is required for proper export from CC peroxisomes and recycling. {ECO:0000250|UniProtKB:Q920N5}. CC -!- DISEASE: Peroxisome biogenesis disorder 2A (PBD2A) [MIM:214110]: A CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease CC spectrum and characterized clinically by severe neurologic dysfunction CC with profound psychomotor retardation, severe hypotonia and neonatal CC seizures, craniofacial abnormalities, liver dysfunction, and CC biochemically by the absence of peroxisomes. Additional features CC include cardiovascular and skeletal defects, renal cysts, ocular CC abnormalities, and hearing impairment. Most severely affected CC individuals with the classic form of the disease (classic Zellweger CC syndrome) die within the first year of life. CC {ECO:0000269|PubMed:7719337}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 2B (PBD2B) [MIM:202370]: 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:10462504, ECO:0000269|PubMed:7719337}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Rhizomelic chondrodysplasia punctata 5 (RCDP5) [MIM:616716]: A CC form of rhizomelic chondrodysplasia punctata, a disease characterized CC by severely disturbed endochondral bone formation, rhizomelic CC shortening of femur and humerus, vertebral disorders, dwarfism, CC cataract, cutaneous lesions, facial dysmorphism, and severe mental CC retardation with spasticity. {ECO:0000269|PubMed:26220973}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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; 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 CCDS; CCDS44822.1; -. [P50542-4] DR CCDS; CCDS44823.1; -. [P50542-1] DR CCDS; CCDS44824.1; -. [P50542-2] DR CCDS; CCDS73433.1; -. [P50542-1] DR CCDS; CCDS8576.1; -. [P50542-3] DR PIR; A56126; A56126. DR RefSeq; NP_000310.2; NM_000319.4. [P50542-3] DR RefSeq; NP_001124495.1; NM_001131023.1. [P50542-4] DR RefSeq; NP_001124496.1; NM_001131024.1. [P50542-2] DR RefSeq; NP_001124497.1; NM_001131025.1. [P50542-1] DR RefSeq; NP_001124498.1; NM_001131026.1. [P50542-1] DR RefSeq; NP_001287718.1; NM_001300789.1. [P50542-1] DR RefSeq; XP_011519097.1; XM_011520795.1. [P50542-4] DR RefSeq; XP_011519099.1; XM_011520797.1. DR RefSeq; XP_011519100.1; XM_011520798.1. DR RefSeq; XP_011519101.1; XM_011520799.2. DR RefSeq; XP_011519102.1; XM_011520800.1. DR RefSeq; XP_016875237.1; XM_017019748.1. [P50542-4] DR RefSeq; XP_016875238.1; XM_017019749.1. [P50542-1] DR RefSeq; XP_016875239.1; XM_017019750.1. DR RefSeq; XP_016875241.1; XM_017019752.1. DR RefSeq; XP_016875242.1; XM_017019753.1. DR RefSeq; XP_016875243.1; XM_017019754.1. DR RefSeq; XP_016875244.1; XM_017019755.1. 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 PDB; 4BXU; NMR; -; B=57-71. DR PDB; 4KXK; X-ray; 2.90 A; B/D=315-639. DR PDB; 4KYO; X-ray; 2.20 A; B/D=315-639. DR PDBsum; 1FCH; -. DR PDBsum; 2C0L; -. DR PDBsum; 2C0M; -. DR PDBsum; 2J9Q; -. DR PDBsum; 2W84; -. DR PDBsum; 3R9A; -. DR PDBsum; 4BXU; -. DR PDBsum; 4KXK; -. DR PDBsum; 4KYO; -. DR SMR; P50542; -. DR BioGRID; 111788; 185. DR DIP; DIP-34654N; -. DR ELM; P50542; -. DR IntAct; P50542; 63. DR MINT; P50542; -. DR STRING; 9606.ENSP00000391601; -. DR iPTMnet; P50542; -. DR MetOSite; P50542; -. DR PhosphoSitePlus; P50542; -. DR BioMuta; PEX5; -. DR DMDM; 119364633; -. DR EPD; P50542; -. DR jPOST; P50542; -. DR MassIVE; P50542; -. DR MaxQB; P50542; -. DR PaxDb; P50542; -. DR PeptideAtlas; P50542; -. DR PRIDE; P50542; -. DR ProteomicsDB; 56239; -. [P50542-1] DR ProteomicsDB; 56240; -. [P50542-2] DR ProteomicsDB; 56241; -. [P50542-3] DR ProteomicsDB; 56242; -. [P50542-4] DR Antibodypedia; 22900; 275 antibodies from 32 providers. DR DNASU; 5830; -. DR Ensembl; ENST00000266563; ENSP00000266563; ENSG00000139197. [P50542-2] DR Ensembl; ENST00000266564; ENSP00000266564; ENSG00000139197. [P50542-3] DR Ensembl; ENST00000420616; ENSP00000410159; ENSG00000139197. DR Ensembl; ENST00000434354; ENSP00000407401; ENSG00000139197. [P50542-4] DR Ensembl; ENST00000455147; ENSP00000400647; ENSG00000139197. DR Ensembl; ENST00000671993; ENSP00000500509; ENSG00000288217. DR Ensembl; ENST00000672242; ENSP00000500696; ENSG00000288217. [P50542-2] DR Ensembl; ENST00000672541; ENSP00000500043; ENSG00000288217. [P50542-4] DR Ensembl; ENST00000672694; ENSP00000499823; ENSG00000288217. DR Ensembl; ENST00000672776; ENSP00000500230; ENSG00000288217. [P50542-3] DR Ensembl; ENST00000675855; ENSP00000502374; ENSG00000139197. DR GeneID; 5830; -. DR KEGG; hsa:5830; -. DR MANE-Select; ENST00000675855.1; ENSP00000502374.1; NM_001351132.2; NP_001338061.1. DR UCSC; uc001qsu.4; human. [P50542-1] DR CTD; 5830; -. DR DisGeNET; 5830; -. DR GeneCards; PEX5; -. DR GeneReviews; PEX5; -. DR HGNC; HGNC:9719; PEX5. DR HPA; ENSG00000139197; Low tissue specificity. DR MalaCards; PEX5; -. DR MIM; 202370; phenotype. DR MIM; 214110; phenotype. DR MIM; 600414; gene. DR MIM; 616716; phenotype. DR neXtProt; NX_P50542; -. DR OpenTargets; ENSG00000139197; -. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 468717; Rhizomelic chondrodysplasia punctata type 5. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA34063; -. DR VEuPathDB; HostDB:ENSG00000139197; -. DR eggNOG; KOG1125; Eukaryota. DR GeneTree; ENSGT00940000156605; -. DR HOGENOM; CLU_013516_4_0_1; -. DR InParanoid; P50542; -. DR OMA; QQHEMEQ; -. DR OrthoDB; 588648at2759; -. DR PhylomeDB; P50542; -. DR TreeFam; TF315044; -. DR PathwayCommons; P50542; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR Reactome; R-HSA-9664873; Pexophagy. DR SignaLink; P50542; -. DR SIGNOR; P50542; -. DR BioGRID-ORCS; 5830; 55 hits in 1053 CRISPR screens. DR ChiTaRS; PEX5; human. DR EvolutionaryTrace; P50542; -. DR GeneWiki; PEX5; -. DR GenomeRNAi; 5830; -. DR Pharos; P50542; Tbio. DR PRO; PR:P50542; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P50542; protein. DR Bgee; ENSG00000139197; Expressed in medial globus pallidus and 243 other tissues. DR ExpressionAtlas; P50542; baseline and differential. DR Genevisible; P50542; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; IDA:UniProtKB. DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IPI:UniProtKB. DR GO; GO:0000268; F:peroxisome targeting sequence 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:0140311; F:protein sequestering activity; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0048468; P:cell development; IEA:Ensembl. DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl. DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl. DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl. DR GO; GO:0007006; P:mitochondrial membrane organization; IEA:Ensembl. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProtKB. DR GO; GO:0045046; P:protein import into peroxisome membrane; IMP:UniProtKB. DR GO; GO:0006625; P:protein targeting to peroxisome; IDA:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl. DR DisProt; DP00472; -. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR024111; PEX5/PEX5L. DR InterPro; IPR024113; PEX5_animals. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR10130; PTHR10130; 1. DR PANTHER; PTHR10130:SF2; PTHR10130:SF2; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Membrane; KW Peroxisome; Peroxisome biogenesis disorder; Phosphoprotein; KW Protein transport; Reference proteome; Repeat; KW Rhizomelic chondrodysplasia punctata; Thioester bond; TPR repeat; KW Transport; Ubl conjugation; Zellweger syndrome. FT CHAIN 1..639 FT /note="Peroxisomal targeting signal 1 receptor" FT /id="PRO_0000106305" FT REPEAT 335..368 FT /note="TPR 1" FT REPEAT 369..402 FT /note="TPR 2" FT REPEAT 403..436 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 33..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 11 FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q920N5" FT VAR_SEQ 45 FT /note="P -> PASEAVSVLEVESPGA (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043639" FT VAR_SEQ 215..251 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:7719337, ECO:0000303|PubMed:7790377" FT /id="VSP_021880" FT VAR_SEQ 283..290 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024106" FT VARIANT 526 FT /note="N -> K (in PBD2B; neonatal adrenoleukodystrophy; FT strongly affects peroxisomal protein import; FT dbSNP:rs61752138)" FT /evidence="ECO:0000269|PubMed:10462504, FT ECO:0000269|PubMed:7719337" FT /id="VAR_007543" FT VARIANT 600 FT /note="S -> W (in PBD2B; infantile Refsum disease; mildly FT affects peroxisomal protein import)" FT /evidence="ECO:0000269|PubMed:10462504" FT /id="VAR_031328" FT MUTAGEN 118 FT /note="W->A: Strongly reduced interaction with PEX14." FT /evidence="ECO:0000269|PubMed:11438541" FT MUTAGEN 122 FT /note="F->A: Strongly reduced interaction with PEX14." FT /evidence="ECO:0000269|PubMed:11438541" FT CONFLICT 425 FT /note="T -> I (in Ref. 1; AAC50103)" FT /evidence="ECO:0000305" FT HELIX 60..69 FT /evidence="ECO:0007829|PDB:4BXU" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:2W84" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:1FCH" FT TURN 331..334 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 338..347 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 351..363 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 369..381 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 385..398 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 403..415 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 419..431 FT /evidence="ECO:0007829|PDB:1FCH" FT TURN 434..436 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 437..439 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 460..481 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 488..500 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 504..517 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 522..534 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 538..551 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 556..569 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 572..587 FT /evidence="ECO:0007829|PDB:1FCH" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:2C0L" FT HELIX 601..614 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 617..619 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 620..624 FT /evidence="ECO:0007829|PDB:1FCH" FT HELIX 628..634 FT /evidence="ECO:0007829|PDB:1FCH" 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 //