Q54MD1

PR
Gene name
pex5 (DDB_G0286033)
Protein name
Peroxisomal targeting signal 1 receptor
Names
PTS1 receptor, PTS1R, Peroxin-5
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0286033
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

8-389 (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 Q54MD1

Entry ID Method Resolution Chain Position Source
AF-Q54MD1-F1 Predicted AlphaFoldDB

No variants for Q54MD1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54MD1

No associated diseases with Q54MD1

4 regional properties for Q54MD1

Type Name Position InterPro Accession
conserved_site Phosphoglucose isomerase, conserved site 269 - 282 IPR018189-1
conserved_site Phosphoglucose isomerase, conserved site 501 - 518 IPR018189-2
domain Phosphoglucose isomerase, SIS domain 1 127 - 288 IPR035476
domain Phosphoglucose isomerase, SIS domain 2 335 - 524 IPR035482

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-12 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex
  • Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix
  • The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle
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 membrane The lipid bilayer surrounding a peroxisome.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

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.
peroxisome targeting sequence binding Binding to a peroxisomal targeting sequence, a sequence of amino acids within a protein that acts as a signal for the localization of a protein into the peroxisome.

3 GO annotations of biological process

Name Definition
peroxisome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
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.
protein targeting to peroxisome The process of directing proteins towards the peroxisome, usually using signals contained within the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSVFRDLVEG ECSEPNALGN FVQHFTNERS YHDKFEDHGK NEFYDSLYRH EEEYNEQRHL
70 80 90 100 110 120
DSIFDGEGQE DDIHLMMDRH LNLRDGPREH KELPLSNVES DLQFLFQDFI NSTRAGQLFH
130 140 150 160 170 180
PSSLNHLPLT FEDKSKIKNR SSIMLKHFSN GESEQFEEDQ LNRMLDSLGI EVGDDFDQVW
190 200 210 220 230 240
DSQPHHTTTT TTTTTTTTTG QYDQYQKYVN DLPEEYEDYE QHQQELFDDG DLEDYELDEE
250 260 270 280 290 300
WDKGDDFHPY DSAWTESDRS VEAAWDETAR RTISDITRPI TQINDPKLKK SNFMKFMNQL
310 320 330 340 350 360
NSGEASIVGS DVVHNPDFKR QEEYQQQADQ WTEDYNDFHE HIPQHRIQEY QFSIQEARDS
370 380 390 400 410 420
DTLERGMGLF NEGHLSDSII ALESEVKRNP ENAMAWMYLG IAHAENDQDS QATTCLIKSL
430 440 450 460 470 480
QIDPTNSKAR LALAVSHTND YQKERALDTL EEWLQRTPEY TALYKQFKGS VDPNSFLDTW
490 500 510 520 530 540
SRHEFTTNLF IEAARSRPSN PDPEVQTALG LLYNMSYDYD KAVDCFKAAL QNSPTDYQLW
550 560 570 580 590 600
NKLGATLANS NRSQEALGAY FKALEHKPSY VRARSNLGIS YLSLNMFQES ATTFLGAIAI
610 620 630 640
HPAPNIWDNL KMVFRLMNRE DLVQKADLRD VNAFLDEFQF M