位置:首页 > 蛋白库 > PEX5_HUMAN
PEX5_HUMAN
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   03-AUG-2022, entry version 217.
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; P63010: AP2B1; NbExp=2; IntAct=EBI-597835, EBI-432924;
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
CC       intellectual disability with spasticity. {ECO:0000269|PubMed:26220973}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this 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   AlphaFoldDB; P50542; -.
DR   SMR; P50542; -.
DR   BioGRID; 111788; 215.
DR   DIP; DIP-34654N; -.
DR   ELM; P50542; -.
DR   IntAct; P50542; 65.
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; 289 antibodies from 32 providers.
DR   DNASU; 5830; -.
DR   Ensembl; ENST00000266563.9; ENSP00000266563.5; ENSG00000139197.11. [P50542-2]
DR   Ensembl; ENST00000266564.7; ENSP00000266564.3; ENSG00000139197.11. [P50542-3]
DR   Ensembl; ENST00000420616.6; ENSP00000410159.2; ENSG00000139197.11. [P50542-1]
DR   Ensembl; ENST00000434354.6; ENSP00000407401.2; ENSG00000139197.11. [P50542-4]
DR   Ensembl; ENST00000455147.6; ENSP00000400647.2; ENSG00000139197.11. [P50542-1]
DR   Ensembl; ENST00000671993.1; ENSP00000500509.1; ENSG00000288217.3. [P50542-1]
DR   Ensembl; ENST00000672242.1; ENSP00000500696.1; ENSG00000288217.3. [P50542-2]
DR   Ensembl; ENST00000672541.1; ENSP00000500043.1; ENSG00000288217.3. [P50542-4]
DR   Ensembl; ENST00000672694.1; ENSP00000499823.1; ENSG00000288217.3. [P50542-1]
DR   Ensembl; ENST00000672776.1; ENSP00000500230.1; ENSG00000288217.3. [P50542-3]
DR   Ensembl; ENST00000675855.1; ENSP00000502374.1; ENSG00000139197.11. [P50542-1]
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; NYRMKGP; -.
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; 63 hits in 1086 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 gastrocnemius and 100 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024