Q9P4X1

PR
Gene name
SPAC959.05c
Protein name
Thioredoxin domain-containing protein C959.05c
Names
Putative protein disulfide isomerase C959.05c
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC959.05c
EC number
5.3.4.1: Transposing S-S bonds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

114-201 (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 Q9P4X1

Entry ID Method Resolution Chain Position Source
AF-Q9P4X1-F1 Predicted AlphaFoldDB

16 variants for Q9P4X1

Variant ID(s) Position Change Description Diseaes Association Provenance
I_3397586_C_T 18 S>N No Jeffares_SNPs
I_3397472_T_C 56 D>G No Jeffares_SNPs
I_3397246_T_C 113 E>G No Jeffares_SNPs
I_3397157_C_T 143 D>N No Jeffares_SNPs
I_3397117_C_T 156 S>N No Jeffares_SNPs
I_3397093_A_G 164 L>P No Jeffares_SNPs
I_3396608_T_C 326 K>E No Jeffares_SNPs
I_3396523_C_T 354 S>N No Jeffares_SNPs
I_3396403_T_G 394 E>A No Jeffares_SNPs
I_3396264_C_T 440 M>I No Jeffares_SNPs
I_3396080_C_T 502 V>M No Jeffares_SNPs
I_3395911_G_A 558 S>L No Jeffares_SNPs
I_3395891_G_A 565 R>C No Jeffares_SNPs
I_3395881_C_T 568 G>D No Jeffares_SNPs
I_3395825_T_A 587 N>Y No Jeffares_SNPs
I_3395714_G_C 624 H>D No Jeffares_SNPs

No associated diseases with Q9P4X1

1 regional properties for Q9P4X1

Type Name Position InterPro Accession
domain Thioredoxin domain 153 - 284 IPR013766

Functions

Description
EC Number 5.3.4.1 Transposing S-S bonds
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

2 GO annotations of molecular function

Name Definition
protein disulfide isomerase activity Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.
protein-disulfide reductase activity Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.

4 GO annotations of biological process

Name Definition
polyamine metabolic process The chemical reactions and pathways involving polyamines, any organic compound containing two or more amino groups.
protein retention in ER lumen The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.
response to endoplasmic reticulum stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLFLYHFTF IVYYFIISFS YAFSIKQEII VSSHNASSIL NTTAFWFVEF TESKYDKEEF
70 80 90 100 110 120
SVIWNEVSME FPDIRRAKVF CDLDLEFCAQ QEIYDHPKVV VLKNGMWMRH VLEKNQITTK
130 140 150 160 170 180
SARQFVKSHL GNCDLEQAEN ETDCFSDDGE YNSDSSSTDP AFELKEDQSW KHSSILRPLE
190 200 210 220 230 240
TLNFKRFLFG NEIMSKTRAF VMFVSLKHCE DCFHWEAVWS SITRNTDERL KMAQVNCDEE
250 260 270 280 290 300
KEMCNHFHIK KFPTFRVFQG FDSIQYNGPL KYQQLLSYSN QVASYQAIKI EEGDIESIEN
310 320 330 340 350 360
SHPVFFLVLY DFATTSEDFS IIERLKLQLA GVAPLYICNS KALANKYGAQ SQPSIIAVRN
370 380 390 400 410 420
GMPIVYQAIT PREFRDYKRI TEWINIVSSP FITELTPTKC HSLLNRKLTV LTLLQPDSEQ
430 440 450 460 470 480
FFSSQEELLR LGKRWFRFQM QRQRNDIVWS RIKKYSAIAE AKKKGFARKV KRIKYSKISH
490 500 510 520 530 540
PTYTESVSFL WLDSSLWLDW IVENLDHTVY VDSITPPVFV IDHSKGVIYV SDRNGNSLTL
550 560 570 580 590 600
EEDSLFSTLR IILEHPNSSR LQKLRAPGLC PNGSPNYRNR YKLIVFNLLI ALLILSILTI
610 620 630
ISASRLSRRR RQLLNKQPVF GFYHSLVIAK SD