ID   PEX5_PICAN              Reviewed;         569 AA.
AC   Q01495; Q01496;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Peroxisomal targeting signal receptor;
DE            Short=PTS1 receptor;
DE            Short=PTS1R;
DE   AltName: Full=Peroxin-5;
DE   AltName: Full=Peroxisomal protein PAH2;
GN   Name=PEX5; Synonyms=PAH2, PER3;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=7628714; DOI=10.1016/0378-1119(95)00230-4;
RA   Nuttley W.M., Szilard R.K., Smith J.J., Veenhuis M., Rachubinski R.A.;
RT   "The PAH2 gene is required for peroxisome assembly in the methylotrophic
RT   yeast Hansenula polymorpha and encodes a member of the tetratricopeptide
RT   repeat family of proteins.";
RL   Gene 160:33-39(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=7615522; DOI=10.1074/jbc.270.29.17229;
RA   Klei I.J., der Hilbrands R.E., Swaving J., Waterham H.R., Vrieling E.G.,
RA   Titorenko I., Cregg J.M., Harder W., Veenhuis M.;
RT   "The Hansenula polymorpha PER3 gene is essential for the import of PTS1
RT   proteins into the peroxisomal matrix.";
RL   J. Biol. Chem. 270:17229-17236(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.
CC   -!- INTERACTION:
CC       Q01495; Q3ZJZ2: PEX20; NbExp=3; IntAct=EBI-7372203, EBI-7372223;
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-9 is UBC4-independent but requires the
CC       presence of PEX4. Ubiquitination at Lys-21 is UBC4-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U22930; AAC49059.1; -; Genomic_DNA.
DR   EMBL; U26678; AAC49040.1; -; Genomic_DNA.
DR   PIR; JC4177; JC4177.
DR   AlphaFoldDB; Q01495; -.
DR   SMR; Q01495; -.
DR   ELM; Q01495; -.
DR   IntAct; Q01495; 1.
DR   MINT; Q01495; -.
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   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Membrane; Peroxisome; Protein transport;
KW   Repeat; Thioester bond; TPR repeat; Transport; Ubl conjugation.
FT   CHAIN           1..569
FT                   /note="Peroxisomal targeting signal receptor"
FT                   /id="PRO_0000106312"
FT   REPEAT          272..305
FT                   /note="TPR 1"
FT   REPEAT          306..339
FT                   /note="TPR 2"
FT   REPEAT          340..377
FT                   /note="TPR 3"
FT   REPEAT          378..415
FT                   /note="TPR 4"
FT   REPEAT          416..449
FT                   /note="TPR 5"
FT   REPEAT          450..483
FT                   /note="TPR 6"
FT   REPEAT          484..517
FT                   /note="TPR 7"
FT   REGION          23..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        9
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        202
FT                   /note="A -> E (in Ref. 2; AAC49040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="T -> A (in Ref. 2; AAC49040)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   569 AA;  63910 MW;  A407FC5808C8885A CRC64;
     MSFLGGSECA ANANPLAQFF KQSQHDTSLE QSLRNSAHDT HQNAQIRAPV AMNEAERAHM
     EQFMNQSTPF NFQPMANELR MIQPDLQTQT TPALRGPRAQ NPVPLQIPGQ AQPQVSGWSS
     EFQNTATSQV THSPSPVSQV RMRSMGMAPR LHLRPFSSAN GPIQASSMTN SVMQEDTSQQ
     VDWEQQFKEM EEMEEMEEAT AAMQQPAEET VSAQESAFDQ VWDNIQETYA DNMLSNDEFQ
     AQWEKDFEKY AQTRLNYGEY TFEENNQFRN NLDAYEIGIK LMESGAKLSE AALAFEAAVE
     QNPGHVDAWL RLGQVQTQNE KELAGIAALE KCLELSPQNL VALMTLAISY INEGYDNAAF
     ATLERWIETK YPEVAERARN ANPDIQADDR FSLNKRVTQL FIKAAQLSPE GANMDSEVQT
     GLGVLFYSME EYSKTLDCFQ AAIEHNPNDA LAWNRLGASL ANSNKPEQAI EAYSRTLQLN
     PNFVRARYNL GVSFINMGMY RDAVDHLLTG LSMHEVESLD GSSSVARSNQ STSLIETLKR
     AFLAMDRRDL IDKVKPGLNV ESFRKTYDI