Q752X0

PR
Gene name
PEX5 (AFR453W)
Protein name
Peroxisomal targeting signal receptor
Names
PTS1 receptor, PTS1R, Peroxin-5
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_AFR453W
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

86-174 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q752X0

Entry ID Method Resolution Chain Position Source
AF-Q752X0-F1 Predicted AlphaFoldDB

No variants for Q752X0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q752X0

No associated diseases with Q752X0

4 regional properties for Q752X0

Type Name Position InterPro Accession
repeat Tetratricopeptide repeat 316 - 349 IPR019734-1
repeat Tetratricopeptide repeat 417 - 450 IPR019734-2
repeat Tetratricopeptide repeat 451 - 484 IPR019734-3
repeat Tetratricopeptide repeat 485 - 518 IPR019734-4

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Peroxisome matrix
  • Cycles between the cytosol and the peroxisome matrix
  • Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins
  • Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol
  • Cys-5 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity)
  • Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity)
  • The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
peroxisomal importomer complex A protein complex responsible for transporting proteins into the peroxisomal matrix. An example of this complex is Pex14 found in S. cerevisae which has 9 core components and 12 transient interaction partners.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.

2 GO annotations of molecular function

Name Definition
peroxisome matrix targeting signal-1 binding Binding to a type 1 peroxisome targeting signal, a tripeptide with the consensus sequence (S/A/C)-(K/R/H)-L.
protein-macromolecule adaptor activity The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.

1 GO annotations of biological process

Name Definition
protein import into peroxisome matrix, docking The process in which a complex formed of a peroxisome targeting sequence (PTS) receptor bound to a PTS-bearing protein docks with translocation machinery in the peroxisomal membrane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSADCSVGAN PLAQLNKRVQ QDRTLQHGSH VNIHQGAEAQ AFKSGPQVSE SNKFQMEQFM
70 80 90 100 110 120
AGKASSGGNM FMGAGMSSGP LALGGSSGLR MSPGPAKELG ARLGGAPMTG SWSQEFNQQV
130 140 150 160 170 180
GSPVQSSSAV SSVSMSSASS SVARAGAYRP MNMMRPVMGL QGARAVGVER HAGPAINDAA
190 200 210 220 230 240
WEQQFQELEK QVEKTLNISD PVEQQQVLEE LSAEAREADY AGGDYEKRFQ QIWNDIHDQT
250 260 270 280 290 300
DDLDSRTELG GGSGDYQRVF STRPAQTAQY AFETDNQYLH NTDAYKIGCI LMENGAKLSE
310 320 330 340 350 360
AALAFEAAVQ QDPGHVDAWL RLGLVQTQNE KELSGINALE QCLKADPHNL MALMTVAISY
370 380 390 400 410 420
INEGYDVSAF TMLGRWLETK YPAFVEEPLD RVDRYNLSRL IIEQYLRVAN ALPEVDPDVQ
430 440 450 460 470 480
LGLGILFYAN EDFDKTIDCF RAALAVRPDD ECMWNRLGAS LANSNRSEEA IQAYHRAIQL
490 500 510 520 530 540
KPTFVRARYN LAVSSMNIGC YREAAEHLLT ALSMHEVEGV AMAPGSGNVP SSNILETLKR
550 560
AFIAMDRRDL LERVVPNMDL QQFRGEFNF