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Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1)

 PEX5_HUMAN              Reviewed;         639 AA.
P50542; A8K891; B4DZ45; B7ZAD5; D3DUT8; Q15115; Q15266; Q96FN7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 3.
22-NOV-2017, entry version 187.
RecName: Full=Peroxisomal targeting signal 1 receptor;
Short=PTS1 receptor;
Short=PTS1R;
AltName: Full=PTS1-BP;
AltName: Full=Peroxin-5;
AltName: Full=Peroxisomal C-terminal targeting signal import receptor;
AltName: Full=Peroxisome receptor 1;
Name=PEX5; Synonyms=PXR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN PBD2A, VARIANT
PBD2B LYS-526, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=7719337; DOI=10.1038/ng0295-115;
Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P.,
Valle D., Gould S.J.;
"Mutations in the PTS1 receptor gene, PXR1, define complementation
group 2 of the peroxisome biogenesis disorders.";
Nat. Genet. 9:115-125(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Liver;
PubMed=7790377; DOI=10.1083/jcb.130.1.51;
Wiemer E.A.C., Nuttley W.M., Bertolaet B.L., Li X., Francke U.,
Wheelock M.J., Anne U.K., Johnson K.R., Subramani S.;
"Human peroxisomal targeting signal-1 receptor restores peroxisomal
protein import in cells from patients with fatal peroxisomal
disorders.";
J. Cell Biol. 130:51-65(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=7706321; DOI=10.1074/jbc.270.13.7731;
Fransen M., Brees C., Baumgart E., Vanhooren J.C.T., Baes M.,
Mannaerts G.P., van Veldhoven P.P.;
"Identification and characterization of the putative human peroxisomal
C-terminal targeting signal import receptor.";
J. Biol. Chem. 270:7731-7736(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH PEX12.
PubMed=10562279; DOI=10.1083/jcb.147.4.761;
Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J.;
"PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor
docking in peroxisomal matrix protein import.";
J. Cell Biol. 147:761-774(1999).
[9]
INTERACTION WITH PEX14, AND MUTAGENESIS OF TRP-118 AND PHE-122.
PubMed=11438541; DOI=10.1074/jbc.M104647200;
Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W.,
Kunau W.-H., Schliebs W.;
"The di-aromatic pentapeptide repeats of the human peroxisome import
receptor PEX5 are separate high affinity binding sites for the
peroxisomal membrane protein PEX14.";
J. Biol. Chem. 276:34524-34529(2001).
[10]
INTERACTION WITH ZFAND6.
PubMed=21980954; DOI=10.1111/j.1600-0854.2011.01298.x;
Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.;
"AWP1/ZFAND6 functions in Pex5 export by interacting with cys-
monoubiquitinated Pex5 and Pex6 AAA ATPase.";
Traffic 13:168-183(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-153; SER-155;
SER-167 AND SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
INVOLVEMENT IN RCDP5.
PubMed=26220973; DOI=10.1093/hmg/ddv305;
Baroey T., Koster J., Stroemme P., Ebberink M.S., Misceo D.,
Ferdinandusse S., Holmgren A., Hughes T., Merckoll E., Westvik J.,
Woldseth B., Walter J., Wood N., Tvedt B., Stadskleiv K.,
Wanders R.J., Waterham H.R., Frengen E.;
"A novel type of rhizomelic chondrodysplasia punctata, RCDP5, is
caused by loss of the PEX5 long isoform.";
Hum. Mol. Genet. 24:5845-5854(2015).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639 IN COMPLEX WITH
TARGETING PEPTIDE.
PubMed=11101887; DOI=10.1038/81930;
Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M.;
"Peroxisomal targeting signal-1 recognition by the TPR domains of
human PEX5.";
Nat. Struct. Biol. 7:1091-1095(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 321-639 IN COMPLEX WITH
TARGETING PEPTIDE.
PubMed=17157249; DOI=10.1016/j.molcel.2006.10.024;
Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R.,
Schliebs W., Sattler M., Wilmanns M.;
"Recognition of a functional peroxisome type 1 target by the dynamic
import receptor Pex5p.";
Mol. Cell 24:653-663(2006).
[16]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 315-639, AND BINDING TO
C-TERMINAL TARGETING PEPTIDES.
PubMed=17428317; DOI=10.1186/1472-6807-7-24;
Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M.,
Kursula P.;
"A previously unobserved conformation for the human Pex5p receptor
suggests roles for intrinsic flexibility and rigid domain motions in
ligand binding.";
BMC Struct. Biol. 7:24-24(2007).
[17]
STRUCTURE BY NMR OF 108-127 IN COMPLEX WITH PEX14.
PubMed=19197237; DOI=10.1038/emboj.2009.7;
Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C.,
Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M.,
Sattler M.;
"Structural basis for competitive interactions of Pex14 with the
import receptors Pex5 and Pex19.";
EMBO J. 28:745-754(2009).
[18]
VARIANTS PBD2B LYS-526 AND TRP-600, AND CHARACTERIZATION OF VARIANTS
PBD2B LYS-526 AND TRP-600.
PubMed=10462504; DOI=10.1006/bbrc.1999.1232;
Shimozawa N., Zhang Z., Suzuki Y., Imamura A., Tsukamoto T., Osumi T.,
Fujiki Y., Orii T., Barth P.G., Wanders R.J., Kondo N.;
"Functional heterogeneity of C-terminal peroxisome targeting signal 1
in PEX5-defective patients.";
Biochem. Biophys. Res. Commun. 262:504-508(1999).
-!- FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal
targeting signal (SKL-type) and plays an essential role in
peroxisomal protein import. {ECO:0000269|PubMed:7706321,
ECO:0000269|PubMed:7719337, ECO:0000269|PubMed:7790377}.
-!- SUBUNIT: Interacts with PEX7 and PEX13 (By similarity). Interacts
with PEX12 and PEX14. Interacts (Cys-linked ubiquitinated) with
ZFAND6. {ECO:0000250, ECO:0000269|PubMed:10562279,
ECO:0000269|PubMed:11101887, ECO:0000269|PubMed:11438541,
ECO:0000269|PubMed:17157249, ECO:0000269|PubMed:19197237,
ECO:0000269|PubMed:21980954}.
-!- INTERACTION:
A8K3Q9:-; NbExp=3; IntAct=EBI-597835, EBI-10174314;
O14734:ACOT8; NbExp=3; IntAct=EBI-597835, EBI-1237371;
P21549:AGXT; NbExp=4; IntAct=EBI-15982193, EBI-727098;
Q6IMN6:CAPRIN2; NbExp=3; IntAct=EBI-597835, EBI-6918449;
Q49A88:CCDC14; NbExp=3; IntAct=EBI-597835, EBI-751035;
H9KV84:EP400NL; NbExp=3; IntAct=EBI-597835, EBI-10178184;
Q8WTR4:GDPD5; NbExp=3; IntAct=EBI-597835, EBI-2833203;
P07195:LDHB; NbExp=3; IntAct=EBI-597835, EBI-358748;
Q6NSB6:MKRN3; NbExp=3; IntAct=EBI-597835, EBI-10195599;
O00623:PEX12; NbExp=4; IntAct=EBI-597835, EBI-594836;
O75381:PEX14; NbExp=13; IntAct=EBI-597835, EBI-594898;
Q9NZ81:PRR13; NbExp=3; IntAct=EBI-597835, EBI-740924;
Q6IPH7:RPL14; NbExp=3; IntAct=EBI-597835, EBI-7813901;
P06703:S100A6; NbExp=3; IntAct=EBI-597835, EBI-352877;
Q13501:SQSTM1; NbExp=2; IntAct=EBI-12181987, EBI-307104;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-597835, EBI-717399;
Q8N5N8:TM6SF1; NbExp=3; IntAct=EBI-597835, EBI-10266890;
Q75MR5:TOM7; NbExp=3; IntAct=EBI-597835, EBI-10255903;
Q68DY9:ZNF772; NbExp=3; IntAct=EBI-597835, EBI-10249148;
-!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Peripheral
membrane protein. Note=Its distribution appears to be dynamic. It
is probably a cycling receptor found mainly in the cytoplasm and
as well associated to the peroxisomal membrane through a docking
factor (PEX13).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P50542-1; Sequence=Displayed;
Name=2;
IsoId=P50542-2; Sequence=VSP_021880;
Name=3;
IsoId=P50542-3; Sequence=VSP_024106;
Name=4;
IsoId=P50542-4; Sequence=VSP_043639;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung,
liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:7706321, ECO:0000269|PubMed:7719337,
ECO:0000269|PubMed:7790377}.
-!- PTM: Monoubiquitination at Cys-11 is required for proper export
from peroxisomes and recycling. {ECO:0000250}.
-!- DISEASE: Peroxisome biogenesis disorder 2A (PBD2A) [MIM:214110]: A
fatal peroxisome biogenesis disorder belonging to the Zellweger
disease spectrum and characterized clinically by severe neurologic
dysfunction with profound psychomotor retardation, severe
hypotonia and neonatal seizures, craniofacial abnormalities, liver
dysfunction, and biochemically by the absence of peroxisomes.
Additional features include cardiovascular and skeletal defects,
renal cysts, ocular abnormalities, and hearing impairment. Most
severely affected individuals with the classic form of the disease
(classic Zellweger syndrome) die within the first year of life.
{ECO:0000269|PubMed:7719337}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Peroxisome biogenesis disorder 2B (PBD2B) [MIM:202370]: A
peroxisome biogenesis disorder that includes neonatal
adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD),
two milder manifestations of the Zellweger disease spectrum. The
clinical course of patients with the NALD and IRD presentation is
variable and may include developmental delay, hypotonia, liver
dysfunction, sensorineural hearing loss, retinal dystrophy and
vision impairment. Children with the NALD presentation may reach
their teens, while patients with the IRD presentation may reach
adulthood. The clinical conditions are often slowly progressive in
particular with respect to loss of hearing and vision. The
biochemical abnormalities include accumulation of phytanic acid,
very long chain fatty acids (VLCFA), di- and
trihydroxycholestanoic acid and pipecolic acid.
{ECO:0000269|PubMed:10462504, ECO:0000269|PubMed:7719337}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Rhizomelic chondrodysplasia punctata 5 (RCDP5)
[MIM:616716]: A form of rhizomelic chondrodysplasia punctata, a
disease characterized by severely disturbed endochondral bone
formation, rhizomelic shortening of femur and humerus, vertebral
disorders, dwarfism, cataract, cutaneous lesions, facial
dysmorphism, and severe mental retardation with spasticity.
{ECO:0000269|PubMed:26220973}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
family. {ECO:0000305}.
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EMBL; U19721; AAC50103.1; -; mRNA.
EMBL; Z48054; CAA88131.1; -; mRNA.
EMBL; X84899; CAA59324.1; -; mRNA.
EMBL; AK292256; BAF84945.1; -; mRNA.
EMBL; AK302742; BAG63957.1; -; mRNA.
EMBL; AK316250; BAH14621.1; -; mRNA.
EMBL; AC018653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88671.1; -; Genomic_DNA.
EMBL; CH471116; EAW88674.1; -; Genomic_DNA.
EMBL; CH471116; EAW88672.1; -; Genomic_DNA.
EMBL; BC010621; AAH10621.1; -; mRNA.
CCDS; CCDS44822.1; -. [P50542-4]
CCDS; CCDS44823.1; -. [P50542-1]
CCDS; CCDS44824.1; -. [P50542-2]
CCDS; CCDS8576.1; -. [P50542-3]
PIR; A56126; A56126.
RefSeq; NP_000310.2; NM_000319.4. [P50542-3]
RefSeq; NP_001124495.1; NM_001131023.1. [P50542-4]
RefSeq; NP_001124496.1; NM_001131024.1. [P50542-2]
RefSeq; NP_001124497.1; NM_001131025.1. [P50542-1]
RefSeq; NP_001124498.1; NM_001131026.1. [P50542-1]
RefSeq; XP_011519097.1; XM_011520795.1. [P50542-4]
RefSeq; XP_011519099.1; XM_011520797.1.
RefSeq; XP_011519100.1; XM_011520798.1.
RefSeq; XP_011519101.1; XM_011520799.2.
RefSeq; XP_011519102.1; XM_011520800.1.
RefSeq; XP_016875237.1; XM_017019748.1. [P50542-4]
RefSeq; XP_016875238.1; XM_017019749.1. [P50542-1]
RefSeq; XP_016875239.1; XM_017019750.1. [P50542-3]
RefSeq; XP_016875241.1; XM_017019752.1.
RefSeq; XP_016875242.1; XM_017019753.1.
RefSeq; XP_016875243.1; XM_017019754.1.
RefSeq; XP_016875244.1; XM_017019755.1.
UniGene; Hs.567327; -.
PDB; 1FCH; X-ray; 2.20 A; A/B=272-639.
PDB; 2C0L; X-ray; 2.30 A; A=335-639.
PDB; 2C0M; X-ray; 2.50 A; A/B/C/F=321-639.
PDB; 2J9Q; X-ray; 2.65 A; A/B=315-639.
PDB; 2W84; NMR; -; B=108-127.
PDB; 3R9A; X-ray; 2.35 A; B/D=315-639.
PDB; 4BXU; NMR; -; B=57-71.
PDB; 4KXK; X-ray; 2.90 A; B/D=315-639.
PDB; 4KYO; X-ray; 2.20 A; B/D=315-639.
PDBsum; 1FCH; -.
PDBsum; 2C0L; -.
PDBsum; 2C0M; -.
PDBsum; 2J9Q; -.
PDBsum; 2W84; -.
PDBsum; 3R9A; -.
PDBsum; 4BXU; -.
PDBsum; 4KXK; -.
PDBsum; 4KYO; -.
DisProt; DP00472; -.
ProteinModelPortal; P50542; -.
SMR; P50542; -.
BioGrid; 111788; 89.
DIP; DIP-34654N; -.
ELM; P50542; -.
IntAct; P50542; 48.
MINT; MINT-241634; -.
STRING; 9606.ENSP00000407401; -.
iPTMnet; P50542; -.
PhosphoSitePlus; P50542; -.
BioMuta; PEX5; -.
DMDM; 119364633; -.
EPD; P50542; -.
MaxQB; P50542; -.
PaxDb; P50542; -.
PeptideAtlas; P50542; -.
PRIDE; P50542; -.
DNASU; 5830; -.
Ensembl; ENST00000266563; ENSP00000266563; ENSG00000139197. [P50542-2]
Ensembl; ENST00000266564; ENSP00000266564; ENSG00000139197. [P50542-3]
Ensembl; ENST00000420616; ENSP00000410159; ENSG00000139197. [P50542-1]
Ensembl; ENST00000434354; ENSP00000407401; ENSG00000139197. [P50542-4]
Ensembl; ENST00000455147; ENSP00000400647; ENSG00000139197. [P50542-1]
GeneID; 5830; -.
KEGG; hsa:5830; -.
UCSC; uc001qsu.4; human. [P50542-1]
CTD; 5830; -.
DisGeNET; 5830; -.
EuPathDB; HostDB:ENSG00000139197.10; -.
GeneCards; PEX5; -.
GeneReviews; PEX5; -.
HGNC; HGNC:9719; PEX5.
HPA; HPA039259; -.
HPA; HPA039260; -.
MalaCards; PEX5; -.
MIM; 202370; phenotype.
MIM; 214110; phenotype.
MIM; 600414; gene.
MIM; 616716; phenotype.
neXtProt; NX_P50542; -.
OpenTargets; ENSG00000139197; -.
Orphanet; 772; Infantile Refsum disease.
Orphanet; 44; Neonatal adrenoleukodystrophy.
Orphanet; 912; Zellweger syndrome.
PharmGKB; PA34063; -.
eggNOG; KOG1125; Eukaryota.
eggNOG; ENOG410XQ6Q; LUCA.
GeneTree; ENSGT00390000013941; -.
HOGENOM; HOG000158146; -.
HOVERGEN; HBG053575; -.
InParanoid; P50542; -.
KO; K13342; -.
PhylomeDB; P50542; -.
TreeFam; TF315044; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SIGNOR; P50542; -.
ChiTaRS; PEX5; human.
EvolutionaryTrace; P50542; -.
GeneWiki; PEX5; -.
GenomeRNAi; 5830; -.
PRO; PR:P50542; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139197; -.
CleanEx; HS_PEX5; -.
ExpressionAtlas; P50542; baseline and differential.
Genevisible; P50542; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; IDA:UniProtKB.
GO; GO:0000268; F:peroxisome targeting sequence binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
GO; GO:1901094; P:negative regulation of protein homotetramerization; IDA:UniProtKB.
GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB.
GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB.
GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProtKB.
GO; GO:0045046; P:protein import into peroxisome membrane; IMP:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR024113; PTS1R.
InterPro; IPR024111; PTS1R_family.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10130; PTHR10130; 1.
PANTHER; PTHR10130:SF2; PTHR10130:SF2; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 4.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50005; TPR; 5.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Membrane; Peroxisome;
Peroxisome biogenesis disorder; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Rhizomelic chondrodysplasia punctata;
Thioester bond; TPR repeat; Transport; Ubl conjugation;
Zellweger syndrome.
CHAIN 1 639 Peroxisomal targeting signal 1 receptor.
/FTId=PRO_0000106305.
REPEAT 335 368 TPR 1.
REPEAT 369 402 TPR 2.
REPEAT 403 436 TPR 3.
REPEAT 452 485 TPR 4.
REPEAT 488 521 TPR 5.
REPEAT 522 555 TPR 6.
REPEAT 556 589 TPR 7.
MOD_RES 115 115 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 11 11 Glycyl cysteine thioester (Cys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250}.
VAR_SEQ 45 45 P -> PASEAVSVLEVESPGA (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043639.
VAR_SEQ 215 251 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7719337,
ECO:0000303|PubMed:7790377}.
/FTId=VSP_021880.
VAR_SEQ 283 290 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024106.
VARIANT 526 526 N -> K (in PBD2B; neonatal
adrenoleukodystrophy; strongly affects
peroxisomal protein import;
dbSNP:rs61752138).
{ECO:0000269|PubMed:10462504,
ECO:0000269|PubMed:7719337}.
/FTId=VAR_007543.
VARIANT 600 600 S -> W (in PBD2B; infantile Refsum
disease; mildly affects peroxisomal
protein import).
{ECO:0000269|PubMed:10462504}.
/FTId=VAR_031328.
MUTAGEN 118 118 W->A: Strongly reduced interaction with
PEX14. {ECO:0000269|PubMed:11438541}.
MUTAGEN 122 122 F->A: Strongly reduced interaction with
PEX14. {ECO:0000269|PubMed:11438541}.
CONFLICT 425 425 T -> I (in Ref. 1; AAC50103).
{ECO:0000305}.
HELIX 60 69 {ECO:0000244|PDB:4BXU}.
HELIX 109 124 {ECO:0000244|PDB:2W84}.
HELIX 318 321 {ECO:0000244|PDB:1FCH}.
TURN 331 334 {ECO:0000244|PDB:1FCH}.
HELIX 338 347 {ECO:0000244|PDB:1FCH}.
HELIX 351 363 {ECO:0000244|PDB:1FCH}.
HELIX 369 381 {ECO:0000244|PDB:1FCH}.
HELIX 385 398 {ECO:0000244|PDB:1FCH}.
HELIX 403 415 {ECO:0000244|PDB:1FCH}.
HELIX 419 431 {ECO:0000244|PDB:1FCH}.
TURN 434 436 {ECO:0000244|PDB:1FCH}.
HELIX 437 439 {ECO:0000244|PDB:1FCH}.
HELIX 460 481 {ECO:0000244|PDB:1FCH}.
HELIX 488 500 {ECO:0000244|PDB:1FCH}.
HELIX 504 517 {ECO:0000244|PDB:1FCH}.
HELIX 522 534 {ECO:0000244|PDB:1FCH}.
HELIX 538 551 {ECO:0000244|PDB:1FCH}.
HELIX 556 569 {ECO:0000244|PDB:1FCH}.
HELIX 572 587 {ECO:0000244|PDB:1FCH}.
STRAND 593 595 {ECO:0000244|PDB:2C0L}.
HELIX 601 614 {ECO:0000244|PDB:1FCH}.
HELIX 617 619 {ECO:0000244|PDB:1FCH}.
HELIX 620 624 {ECO:0000244|PDB:1FCH}.
HELIX 628 634 {ECO:0000244|PDB:1FCH}.
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


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