P4hb
entrez
25506
canonical
uniprot
P04785
canonical
ensembl
ENSRNOG00000036689
resolver
ensembl
ENSRNOG00055032801
resolver
ensembl
ENSRNOG00060030940
resolver
ensembl
ENSRNOG00065003976
resolver
ensp
ENSRNOP00000051841
resolver
ensp
ENSRNOP00055046830
resolver
ensp
ENSRNOP00060044619
resolver
ensp
ENSRNOP00065004180
resolver
enst
ENSRNOT00000054958
resolver
enst
ENSRNOT00055056725
resolver
enst
ENSRNOT00060053755
resolver
enst
ENSRNOT00065005811
resolver
genesymbol
P4hb
resolver
genesymbol_syn
Pdia1
resolver
uniprot
P13700
resolver
uniprot_entry
PDIA1_RAT
resolver
uniprot_sec
P13700
resolver
amino_acid_sequence
MLSRALLCLALAWAARVGADALEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAESLVDSSEVTVIGFFKDAGSDSAKQFLLAAEAVDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEITKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITQFCHHFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDNDDLDLEEALEPDMEEDDDQKAVKDEL
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. 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. {ECO:0000250|UniProtKB:P07237}.
uniprot
proteins
mass_dalton
56951
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
2757644
uniprot
proteins
pubmed
2841089
uniprot
proteins
pubmed
3178809
uniprot
proteins
pubmed
3840230
uniprot
proteins
pubmed
8251535
uniprot
proteins
pubmed
8366073
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:0000250|UniProtKB:P09103}; 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