PDIA1_CHICK
ID PDIA1_CHICK Reviewed; 515 AA.
AC P09102; Q90969;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE EC=5.3.4.1;
DE AltName: Full=Cellular thyroid hormone-binding protein;
DE AltName: Full=Prolyl 4-hydroxylase subunit beta;
DE AltName: Full=Retina cognin;
DE Short=R-cognin;
DE Flags: Precursor;
GN Name=P4HB; Synonyms=PDI, PDIA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 315; 356; 488; 491-493
RP AND 497.
RA Hausman R.E.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-515.
RC TISSUE=Retina;
RX PubMed=7681992; DOI=10.1073/pnas.90.7.2950;
RA Krishna Rao A.S., Hausman R.E.;
RT "cDNA for R-cognin: homology with a multifunctional protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2950-2954(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-129; 163-172; 209-218; 244-253; 286-295; 353-463
RP AND 483-515.
RX PubMed=2852147; DOI=10.1016/0378-1119(88)90062-5;
RA Nakazawa M., Aida T., Everson W.V., Gonda M.A., Hughes S.H., Kao W.W.;
RT "Structure of the gene encoding the beta-subunit of chicken prolyl 4-
RT hydroxylase.";
RL Gene 71:451-460(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-515, AND PROTEIN SEQUENCE OF 23-31 AND
RP 95-109.
RX PubMed=2851999; DOI=10.1042/bj2561005;
RA Parkkonen T., Kivirikko K.Z., Pihlajaniemi T.;
RT "Molecular cloning of a multifunctional chicken protein acting as the
RT prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a
RT cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino
RT acid sequences with those in other species.";
RL Biochem. J. 256:1005-1011(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-459.
RA Bassuk J.A.;
RL Submitted (FEB-1988) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This multifunctional protein catalyzes the formation,
CC breakage and rearrangement of disulfide bonds. At the cell surface,
CC seems to act as a reductase that cleaves disulfide bonds of proteins
CC attached to the cell. May therefore cause structural modifications of
CC exofacial proteins. Inside the cell, seems to form/rearrange disulfide
CC bonds of nascent proteins. At high concentrations, functions as a
CC chaperone that inhibits aggregation of misfolded proteins. At low
CC concentrations, facilitates aggregation (anti-chaperone activity). Also
CC acts a structural subunit of various enzymes such as prolyl 4-
CC hydroxylase (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Heterodimer; heterodimerizes with the protein microsomal
CC triglyceride transfer MTTP. Homodimer. Monomers and homotetramers may
CC also occur. Also constitutes the structural subunit of prolyl 4-
CC hydroxylase. Stabilizes this enzyme and retains it in the ER without
CC contributing to the catalytic activity. Binds UBQLN1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P07237}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49054.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L11147; AAA49054.2; ALT_INIT; mRNA.
DR EMBL; X13110; CAA31502.1; -; mRNA.
DR EMBL; X06768; CAB57801.1; -; Genomic_DNA.
DR PIR; S02084; ISCHSS.
DR AlphaFoldDB; P09102; -.
DR SMR; P09102; -.
DR STRING; 9031.ENSGALP00000011689; -.
DR PaxDb; P09102; -.
DR VEuPathDB; HostDB:geneid_374091; -.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; P09102; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; P09102; -.
DR SABIO-RK; P09102; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Isomerase; Membrane; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2851999"
FT CHAIN 23..515
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000269|PubMed:2851999"
FT /id="PRO_0000034200"
FT DOMAIN 23..139
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 351..480
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 477..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 512..515
FT /note="Prevents secretion from ER"
FT COMPBIAS 483..515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 403
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 404
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 466
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 402..405
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 23
FT /note="E -> Q (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="EL -> DV (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="H -> Q (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="T -> M (in Ref. 5; CAB57801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 57410 MW; E7CC978A5109C2CE CRC64;
MAVVRVRAIV ALLCLVAALG LAEPLEEEDG VLVLRAANFE QALAAHRHLL VEFYAPWCGH
CKALAPEYAK AAAQLKAEGS EIRLAKVDAT EEAELAQQFG VRGYPTIKFF RNGDKAAPRE
YTAGREADDI VSWLKKRTGP AATTLTDAAA AETLVDSSEV VVIGFFKDVT SDAAKEFLLA
AESVDDIPFG ISSSADVFSK YQLSQDGVVL FKKFDEGRNN FEGDLTKDNL LNFIKSNQLP
LVIEFTEQTA PKIFGGEIKT HILLFLPKSV SDYEGKLDNF KTAAGNFKGK ILFIFIDSDH
SDNQRILEFF GLKKEECPAV RLITLEEEMT KYKPESDDLT ADKIKEFCNK FLEGKIKPHL
MSQDLPEDWD KQPVKVLVGK NFEEVAFDEN KNVFVEFYAP WCGHCKQLAP IWDKLGETYR
DHENIVIAKM DSTANEVEAV KIHSFPTLKF FPAGSGRNVI DYNGERTLEG FKKFLESGGQ
DGAAADDDLE DLETDEETDL EEGDDDEQKI QKDEL
