P4hb
entrez
18453
canonical
uniprot
P09103
canonical
ensembl
ENSMUSG00000025130
resolver
ensp
ENSMUSP00000026122
resolver
enst
ENSMUST00000026122
resolver
genesymbol
P4hb
resolver
genesymbol_syn
Pdia1
resolver
uniprot
Q922C8
resolver
uniprot_entry
PDIA1_MOUSE
resolver
uniprot_sec
Q922C8
resolver
amino_acid_sequence
MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFEEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDVESDSAKQFLLAAEAIDDIPFGITSNSGVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSSFKRAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQEVPEDWDKQPVKVLVGANFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIIIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDEDLDLEEALEPDMEEDDDQKAVKDEL
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. 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 (By similarity). 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:0000250|UniProtKB:P07237, ECO:0000269|PubMed:21670307}.
uniprot
proteins
mass_dalton
57058
uniprot
proteins
mutagenesis
MUTAGEN 359; /note="S->A: Homozygotes are born at Mendelian ratios and have no phenotypic abnormalities from birth to adulthood. Increased ERN1 activity."; /evidence="ECO:0000269|PubMed:32149426
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-359 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone. It also promotes interaction with ERN1. {ECO:0000250|UniProtKB:P07237}.
uniprot
proteins
protein_family
Protein disulfide isomerase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21670307
uniprot
proteins
pubmed
2295602
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
2830592
uniprot
proteins
pubmed
29858230
uniprot
proteins
pubmed
32149426
uniprot
proteins
pubmed
33863978
uniprot
proteins
pubmed
7753822
uniprot
proteins
sequence_length
509
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. 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. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}.
uniprot
proteins