PEX5_BOVIN
ID PEX5_BOVIN Reviewed; 640 AA.
AC Q1RMV0; A1L572;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {ECO:0000250}.
CC -!- PTM: Monoubiquitination at Cys-11 is required for proper export from
CC peroxisomes and recycling. {ECO:0000250|UniProtKB:Q920N5}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; BT029859; ABM06112.1; -; mRNA.
DR EMBL; BC114692; AAI14693.1; -; mRNA.
DR RefSeq; NP_001039648.1; NM_001046183.1.
DR RefSeq; XP_005207194.1; XM_005207137.3.
DR AlphaFoldDB; Q1RMV0; -.
DR SMR; Q1RMV0; -.
DR STRING; 9913.ENSBTAP00000052543; -.
DR PaxDb; Q1RMV0; -.
DR PRIDE; Q1RMV0; -.
DR Ensembl; ENSBTAT00000013864; ENSBTAP00000013864; ENSBTAG00000010490.
DR Ensembl; ENSBTAT00000052144; ENSBTAP00000052543; ENSBTAG00000010490.
DR Ensembl; ENSBTAT00000074239; ENSBTAP00000070766; ENSBTAG00000010490.
DR GeneID; 514832; -.
DR KEGG; bta:514832; -.
DR CTD; 5830; -.
DR VEuPathDB; HostDB:ENSBTAG00000010490; -.
DR VGNC; VGNC:32761; PEX5.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000156605; -.
DR HOGENOM; CLU_013516_4_0_1; -.
DR InParanoid; Q1RMV0; -.
DR OMA; NYRMKGP; -.
DR OrthoDB; 588648at2759; -.
DR TreeFam; TF315044; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000010490; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; Q1RMV0; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISS:UniProtKB.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0140311; F:protein sequestering activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
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; IEA:Ensembl.
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:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISS:UniProtKB.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IEA:Ensembl.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Peroxisome; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Thioester bond; TPR repeat; Transport;
KW Ubl conjugation.
FT CHAIN 1..640
FT /note="Peroxisomal targeting signal 1 receptor"
FT /id="PRO_0000263625"
FT REPEAT 336..369
FT /note="TPR 1"
FT REPEAT 371..403
FT /note="TPR 2"
FT REPEAT 404..437
FT /note="TPR 3"
FT REPEAT 454..486
FT /note="TPR 4"
FT REPEAT 489..522
FT /note="TPR 5"
FT REPEAT 524..556
FT /note="TPR 6"
FT REPEAT 558..590
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 280
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"
SQ SEQUENCE 640 AA; 70878 MW; BD4BF1ADE929CE70 CRC64;
MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAV SKPLGVASED
ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQEIEQSNFR QAPQRAPGVA DLALSENWAQ
EFLAAGDAVD VTQEYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA
AADRWYDEYQ PEEDLQHTAS DFVAKVDDPK LANSEFLKFV RQIGEGQVSL ESGAGSGRAQ
AEQWAAEFIQ QQGTSEAWVD QFTRPVNTSA LDMEFERAKS AIESDVDFWD KLQAELEEMA
KRDAEAHPWL SDHDDLTSAS YDKGYHFEEE NPLRDHPQPF EEGLRRLQEG DLPNAVLLFE
AAVQQDPKHM EAWQYLGTTQ AENEQELLAI SALRKCLELK PDNRTALMAL AVSFTNESLQ
RQACETLRDW LRYTPAYAHL VAPGEEGAGG VGLGSSKRIL GSLLSDSLFL EVKELFLAAV
RLDPTSIDPD VQCGLGVLFN LSGEYDKAVD CFTAALSVRP DDYLLWNKLG ATLANGNQSE
EAVAAYRRAL ELQPGYIRSR YNLGISCINL GAHREAVEHF LEALNMQRKS RGPRGEGGAM
SENIWSTLRL ALSMLGQSDA YGAADARDLP TLLAMFGLPQ