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PEX5_PICPA
ID   PEX5_PICPA              Reviewed;         576 AA.
AC   P33292; Q01967;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Peroxisomal targeting signal receptor;
DE            Short=PTS1 receptor;
DE            Short=PTS1R;
DE   AltName: Full=Peroxin-5;
DE   AltName: Full=Peroxisomal protein PAS8;
GN   Name=PEX5; Synonyms=PAS8;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76273 / CBS 7435 / CECT 11407 / NRRL Y-11430;
RX   PubMed=8098333; DOI=10.1083/jcb.121.4.761;
RA   McCollum D., Monosov E., Subramani S.;
RT   "The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import
RT   deficiencies of Zellweger syndrome cells -- the PAS8 protein binds to the
RT   COOH-terminal tripeptide peroxisomal targeting signal, and is a member of
RT   the TPR protein family.";
RL   J. Cell Biol. 121:761-774(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gould S.J., Kalish J.E., Morrel J.C., Bjorkman J., Urquhart A.J.,
RA   Crane D.I.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=7641682; DOI=10.1002/j.1460-2075.1995.tb00032.x;
RA   Terlecky S.R., Nuttley W.M., McCollum D., Sock E., Subramani S.;
RT   "The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-
RT   terminal tripeptide peroxisomal targeting signal.";
RL   EMBO J. 14:3627-3634(1995).
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:7641682}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Peripheral
CC       membrane protein. Note=Its distribution appears to be dynamic. It is
CC       probably a cycling receptor found mainly in the cytoplasm and as well
CC       associated to the peroxisomal membrane through a docking factor
CC       (PEX13).
CC   -!- PTM: Ubiquitination at Cys-10 is UBC4-independent but requires the
CC       presence of PEX4. Ubiquitination at Lys-22 is UBC4-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC       family. {ECO:0000305}.
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DR   EMBL; Z19592; CAA79640.1; -; Genomic_DNA.
DR   EMBL; U59222; AAB40613.1; -; Genomic_DNA.
DR   PIR; A40688; A40688.
DR   AlphaFoldDB; P33292; -.
DR   SMR; P33292; -.
DR   PRIDE; P33292; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR024111; PEX5/PEX5L.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR10130; PTHR10130; 1.
DR   Pfam; PF00515; TPR_1; 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   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Membrane; Peroxisome; Protein transport;
KW   Repeat; Thioester bond; TPR repeat; Transport; Ubl conjugation.
FT   CHAIN           1..576
FT                   /note="Peroxisomal targeting signal receptor"
FT                   /id="PRO_0000106313"
FT   REPEAT          278..311
FT                   /note="TPR 1"
FT   REPEAT          312..345
FT                   /note="TPR 2"
FT   REPEAT          346..383
FT                   /note="TPR 3"
FT   REPEAT          384..421
FT                   /note="TPR 4"
FT   REPEAT          422..455
FT                   /note="TPR 5"
FT   REPEAT          456..489
FT                   /note="TPR 6"
FT   REPEAT          490..523
FT                   /note="TPR 7"
FT   REGION          176..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        10
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        243..259
FT                   /note="DQFQAQWEKDFAQYAEG -> RPVSGSMGERFCPIRRR (in Ref. 1;
FT                   CAA79640)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  65083 MW;  C249FBE50FDE5247 CRC64;
     MSLIGGGSDC AAGSNPLAQF TKHTQHDTSL QQSMRNGEFQ QGNQRMMRNE STMSPMERQQ
     MDQFMQQQNN PAFNFQPMQH ELNVMQQNMN APQQVANNSW NQEFRMKDPM VANAPSAQVQ
     TPVQSTNWAQ DFQQAGPEVQ HHAQQHQHPI LSVPGVRAGI YGGGRLMGGS MMNRAAQMQQ
     QNPAQAQTSE QSQTQWEDQF KDIESMLNSK TQEPKTKQQE QNTFEQVWDD IQVSYADVEL
     TNDQFQAQWE KDFAQYAEGR LNYGEYKYEE KNQFRNDPDA YEIGMRLMES GAKLSEAGLA
     FEAAVQQDPK HVDAWLKLGE VQTQNEKESD GIAALEKCLE LDPTNLAALM TLAISYINDG
     YDNAAYATLE RWIETKYPDI ASRARSSNPD LDGGDRIEQN KRVTELFMKA AQLSPDVASM
     DADVQTGLGV LFYSMEEFDK TIDCFKAAIE VEPDKALNWN RLGAALANYN KPEEAVEAYS
     RALQLNPNFV RARYNLGVSF INMGRYKEAV EHLLTGISLH EVEGVDASEM SSNQGLQNNA
     LVETLKRAFL GMNRRDLVDK VYPGMGLAQF RKMFDF
 
 
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