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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
 
 
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