PEX5_MOUSE
ID PEX5_MOUSE Reviewed; 639 AA.
AC O09012; Q3UM58; Q8K2V5; Q91YC7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Peroxisomal targeting signal 1 receptor {ECO:0000305};
DE Short=PTS1 receptor;
DE Short=PTS1R;
DE AltName: Full=PTS1-BP;
DE AltName: Full=PXR1P;
DE AltName: Full=Peroxin-5;
DE AltName: Full=Peroxisomal C-terminal targeting signal import receptor;
DE AltName: Full=Peroxisome receptor 1;
GN Name=Pex5 {ECO:0000312|MGI:MGI:1098808}; Synonyms=Pxr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9288097; DOI=10.1038/ng0997-49;
RA Baes M.I., Gressens P., Baumgart E., Carmeliet P., Casteels M., Fransen M.,
RA Evrard P., Fahimi D., Declercq P., Collen D., Vanveldhoven P.,
RA Mannaerts G.P.;
RT "A mouse model for Zellweger syndrome.";
RL Nat. Genet. 17:49-57(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Van Veldhoven P.P.;
RT "Studies on mammalian peroxines.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=15732085; DOI=10.1002/hep.20628;
RA Dirkx R., Vanhorebeek I., Martens K., Schad A., Grabenbauer M., Fahimi D.,
RA Declercq P., Van Veldhoven P.P., Baes M.;
RT "Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER
RT abnormalities.";
RL Hepatology 41:868-878(2005).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17442273; DOI=10.1016/j.bbrc.2007.03.198;
RA Dirkx R., Meyhi E., Asselberghs S., Reddy J., Baes M., Van Veldhoven P.P.;
RT "Beta-oxidation in hepatocyte cultures from mice with peroxisomal gene
RT knockouts.";
RL Biochem. Biophys. Res. Commun. 357:718-723(2007).
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:0000250|UniProtKB:Q920N5}.
CC -!- SUBUNIT: Interacts with PEX7, PEX12, PEX13 and PEX14. Interacts (Cys-
CC linked ubiquitinated) with ZFAND6 (By similarity). Interacts with VWA8
CC in a PEX7-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P50542, ECO:0000250|UniProtKB:Q920N5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q920N5}.
CC Peroxisome membrane {ECO:0000250|UniProtKB:Q920N5}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q920N5}. Note=Its distribution appears
CC to be dynamic. It is probably a cycling receptor found mainly in the
CC cytoplasm and as well associated to the peroxisomal membrane through a
CC docking factor (PEX13).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=O09012-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O09012-2; Sequence=VSP_024107;
CC -!- PTM: Monoubiquitination at Cys-11 is required for proper export from
CC peroxisomes and recycling. {ECO:0000250|UniProtKB:Q920N5}.
CC -!- DISRUPTION PHENOTYPE: Liver-specific knockout mice display a growth
CC retardation from the third postnatal week resulting in a 30% to 40%
CC lower body weight than control mice at the age of 7 weeks. Thereafter,
CC mice tend to catch up in growth, and by 3 months their weight is not
CC different from control mice. Throughout this period, the mice look
CC healthy, are fertile and liver function is unaffected. However, 10-
CC week-old mutant mice display a severe hepatomegaly due to hypertrophic
CC and hyperplastic hepatocytes. Mutant mice survive but develope
CC extensive liver tumors from 12 months on (PubMed:15732085). Peroxisomes
CC are absent in mutant hepatocytes and multiple ultrastructural
CC alterations are noticed, smooth endoplasmic reticulum proliferation,
CC and accumulation of lipid droplets and lysosomes. Most prominent is the
CC abnormal structure of the inner mitochondrial membrane. This is
CC accompanied by severely reduced activities of complex I, III, and V and
CC a collapse of the mitochondrial inner membrane potential
CC (PubMed:15732085). Liver-specific knockout mice display severely
CC impaired oxidation of 2-methylhexadecanoic acid, the bile acid
CC intermediate trihydroxycholestanoic acid (THCA), and tetradecanedioic
CC acid. In contrast, mitochondrial beta-oxidation rates of palmitate are
CC doubled (PubMed:17442273). {ECO:0000269|PubMed:15732085,
CC ECO:0000269|PubMed:17442273}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; Z97018; CAB09694.1; -; mRNA.
DR EMBL; AJ416473; CAC94925.1; -; mRNA.
DR EMBL; AK088886; BAC40632.1; -; mRNA.
DR EMBL; AK145111; BAE26240.1; -; mRNA.
DR EMBL; AK145361; BAE26388.1; -; mRNA.
DR EMBL; AK161470; BAE36414.1; -; mRNA.
DR EMBL; BC029748; AAH29748.1; -; mRNA.
DR CCDS; CCDS20517.1; -. [O09012-1]
DR CCDS; CCDS20518.1; -. [O09012-2]
DR RefSeq; NP_001264259.1; NM_001277330.1. [O09012-2]
DR RefSeq; NP_001264734.1; NM_001277805.1. [O09012-1]
DR RefSeq; NP_033021.2; NM_008995.2. [O09012-1]
DR RefSeq; NP_787947.1; NM_175933.2. [O09012-2]
DR RefSeq; XP_006505821.1; XM_006505758.3. [O09012-1]
DR RefSeq; XP_006505822.1; XM_006505759.3. [O09012-1]
DR RefSeq; XP_017176951.1; XM_017321462.1.
DR AlphaFoldDB; O09012; -.
DR SMR; O09012; -.
DR BioGRID; 202526; 4.
DR IntAct; O09012; 7.
DR MINT; O09012; -.
DR STRING; 10090.ENSMUSP00000079398; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; O09012; -.
DR PhosphoSitePlus; O09012; -.
DR EPD; O09012; -.
DR jPOST; O09012; -.
DR MaxQB; O09012; -.
DR PaxDb; O09012; -.
DR PeptideAtlas; O09012; -.
DR PRIDE; O09012; -.
DR ProteomicsDB; 288042; -. [O09012-1]
DR ProteomicsDB; 288043; -. [O09012-2]
DR Antibodypedia; 22900; 289 antibodies from 32 providers.
DR DNASU; 19305; -.
DR Ensembl; ENSMUST00000035861; ENSMUSP00000049132; ENSMUSG00000005069. [O09012-1]
DR Ensembl; ENSMUST00000080557; ENSMUSP00000079398; ENSMUSG00000005069. [O09012-2]
DR Ensembl; ENSMUST00000112531; ENSMUSP00000108150; ENSMUSG00000005069. [O09012-2]
DR Ensembl; ENSMUST00000112532; ENSMUSP00000108151; ENSMUSG00000005069. [O09012-1]
DR GeneID; 19305; -.
DR KEGG; mmu:19305; -.
DR UCSC; uc009dqs.1; mouse. [O09012-1]
DR UCSC; uc009dqt.1; mouse. [O09012-2]
DR CTD; 5830; -.
DR MGI; MGI:1098808; Pex5.
DR VEuPathDB; HostDB:ENSMUSG00000005069; -.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000156605; -.
DR HOGENOM; CLU_013516_4_0_1; -.
DR InParanoid; O09012; -.
DR OMA; NYRMKGP; -.
DR OrthoDB; 588648at2759; -.
DR PhylomeDB; O09012; -.
DR TreeFam; TF315044; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins. [O09012-1]
DR Reactome; R-MMU-9033241; Peroxisomal protein import. [O09012-1]
DR Reactome; R-MMU-9664873; Pexophagy. [O09012-1]
DR BioGRID-ORCS; 19305; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Pex5; mouse.
DR PRO; PR:O09012; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O09012; protein.
DR Bgee; ENSMUSG00000005069; Expressed in cortical plate and 259 other tissues.
DR ExpressionAtlas; O09012; baseline and differential.
DR Genevisible; O09012; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISS:UniProtKB.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; ISO:MGI.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0140311; F:protein sequestering activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0007031; P:peroxisome organization; IDA:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; ISO:MGI.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISO:MGI.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:MGI.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 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 Alternative splicing; Cytoplasm; Membrane; Peroxisome; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Thioester bond; TPR repeat;
KW Transport; Ubl conjugation.
FT CHAIN 1..639
FT /note="Peroxisomal targeting signal 1 receptor"
FT /id="PRO_0000106306"
FT REPEAT 337..370
FT /note="TPR 1"
FT REPEAT 371..404
FT /note="TPR 2"
FT REPEAT 405..438
FT /note="TPR 3"
FT REPEAT 452..485
FT /note="TPR 4"
FT REPEAT 488..521
FT /note="TPR 5"
FT REPEAT 522..555
FT /note="TPR 6"
FT REPEAT 556..589
FT /note="TPR 7"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT CROSSLNK 11
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q920N5"
FT VAR_SEQ 216..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_024107"
FT CONFLICT 139
FT /note="D -> H (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> G (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="S -> F (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="D -> N (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="Q -> R (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="H -> N (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="Y -> S (in Ref. 1; CAB09694)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="D -> E (in Ref. 2; BAE26240)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="M -> L (in Ref. 2; BAE26240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 70756 MW; A7013FF02926803C CRC64;
MAMRELVEGE CGGANPLMKL ATHFTQDKAL RQEGLRPGPW PPGASAAETV SKPLGVGTED
ELVSEFLQDQ NATLVSRAPQ TFKMDDLLAE MQEIEQSNFR QAPQRAPGVA DLALSENWAQ
EFLAAGDAVD VAQDYNETDW SQEFIAEVTD PLSVSPARWA EEYLEQSEEK LWLGDQEGSS
TADRWYDEYH PEEDLQHTAS DFVSKVDDPK LANSEFLKFV RQIGEGQVSL ESAAGSGGAQ
AEQWAAEFIQ QQGTSEAWVD QFTRPGNKIA ALQVEFERAK SAIESDVDFW DKLQAELEEM
AKRDAEAHPW LSDYDDLTSA SYDKGYQFEE ENPLRDHPQP FEEGLHRLEE GDLPNAVLLF
EAAVQQDPKH MEAWQYLGTT QAENEQELLA ISALRRCLEL KPDNRTALMA LAVSFTNESL
QRQACETLRD WLRYSPAYAH LVAPGEEGAT GAGPSKRILG SLLSDSLFLE VKDLFLAAVR
LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLMWNKLGA TLANGNQSEE
AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS
ENIWSTLRLA LSMLGQSDAY GAADARDLSA LLAMFGLPQ
