P4HB
entrez
5034
canonical
uniprot
P07237
canonical
ensembl
ENSG00000185624
resolver
ensp
ENSP00000327801
resolver
enst
ENST00000331483
resolver
genesymbol
P4HB
resolver
genesymbol_syn
ERBA2L
resolver
genesymbol_syn
PDI
resolver
genesymbol_syn
PDIA1
resolver
genesymbol_syn
PO4DB
resolver
hgnc
HGNC:8548
resolver
uniprot
A0A024R8S5
resolver
uniprot
B2RDQ2
resolver
uniprot
P30037
resolver
uniprot
P32079
resolver
uniprot
Q15205
resolver
uniprot
Q6LDE5
resolver
uniprot_entry
A0A024R8S5_HUMAN
resolver
uniprot_entry
PDIA1_HUMAN
resolver
uniprot_sec
B2RDQ2
resolver
uniprot_sec
P30037
resolver
uniprot_sec
P32079
resolver
uniprot_sec
Q15205
resolver
uniprot_sec
Q6LDE5
resolver
amino_acid_sequence
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
uniprot
proteins
disease_involvement
DISEASE: Cole-Carpenter syndrome 1 (CLCRP1) [MIM:112240]: A form of Cole-Carpenter syndrome, a disorder characterized by features of osteogenesis imperfecta such as bone deformities and severe bone fragility with frequent fractures, in association with craniosynostosis, ocular proptosis, hydrocephalus, growth failure and distinctive facial features. Craniofacial findings include marked frontal bossing, midface hypoplasia, and micrognathia. Despite the craniosynostosis and hydrocephalus, intellectual development is normal. CLCRP1 inheritance is autosomal dominant. {ECO:0000269|PubMed:25683117}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.3.4.1
uniprot
proteins
function
FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:32149426}.
uniprot
proteins
mass_dalton
57116
uniprot
proteins
mutagenesis
MUTAGEN 128; /note="W->I: Reduced interaction with ERN1. Abolishes interaction with ERN1; when associated with W-403."; /evidence="ECO:0000269|PubMed:32149426"; MUTAGEN 331; /note="S->E: Phosphomimetic mutant. Does not affect enzyme or chaperone activity."; /evidence="ECO:0000269|PubMed:32149426"; MUTAGEN 357; /note="S->A: Abolishes phosphorylation at this site but protein is still phosphorylated at other sites. No changes in chaperone or enzyme activity."; /evidence="ECO:0000269|PubMed:32149426"; MUTAGEN 357; /note="S->E: Phosphomimetic mutant. Reduced resistance to protease digestion, sugesting adoption of an open conformation. Increased chaperone activity. Decreased enzyme activity. Increased binding to ERN1."; /evidence="ECO:0000269|PubMed:32149426"; MUTAGEN 403; /note="L->W: Reduced interaction with ERN1. Abolishes interaction with ERN1; when associated with I-128."; /evidence="ECO:0000269|PubMed:32149426"; MUTAGEN 427; /note="S->E: Phosphomimetic mutant. Does not affect enzyme or chaperone activity. Does not increase binding to ERN1."; /evidence="ECO:0000269|PubMed:32149426
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-357 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone (PubMed:32149426). It also promotes interaction with ERN1 (PubMed:32149426). {ECO:0000269|PubMed:32149426}.
uniprot
proteins
protein_family
Protein disulfide isomerase family
uniprot
proteins
pubmed
10383197
uniprot
proteins
pubmed
10636893
uniprot
proteins
pubmed
11181151
uniprot
proteins
pubmed
11707400
uniprot
proteins
pubmed
12095988
uniprot
proteins
pubmed
12218051
uniprot
proteins
pubmed
12218052
uniprot
proteins
pubmed
12485997
uniprot
proteins
pubmed
12643545
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
1286669
uniprot
proteins
pubmed
14592831
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15158710
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15644496
uniprot
proteins
pubmed
1597478
uniprot
proteins
pubmed
16478722
uniprot
proteins
pubmed
1699755
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
2079031
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21670307
uniprot
proteins
pubmed
23475612
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25683117
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
26224785
uniprot
proteins
pubmed
2846539
uniprot
proteins
pubmed
3034602
uniprot
proteins
pubmed
32149426
uniprot
proteins
pubmed
3342239
uniprot
proteins
pubmed
3611107
uniprot
proteins
pubmed
7753822
uniprot
proteins
pubmed
8580850
uniprot
proteins
pubmed
8672469
uniprot
proteins
pubmed
9150948
uniprot
proteins
pubmed
9399589
uniprot
proteins
sequence_length
508
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:32149426}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:23475612}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:21670307}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces (PubMed:11181151). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:10636893). Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612). {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:11181151, ECO:0000269|PubMed:23475612, ECO:0000305}.
uniprot
proteins