ID   PDI1_DICDI              Reviewed;         363 AA.
AC   Q86IA3; O15735; Q552H4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Protein disulfide-isomerase 1;
DE            Short=PDI1;
DE            EC=5.3.4.1;
DE   Flags: Precursor;
GN   Name=pdi1; ORFNames=DDB_G0276141;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=AX2;
RX   PubMed=9428745; DOI=10.1016/s0014-5793(97)01415-4;
RA   Monnat J., Hacker U., Geissler H., Rauchenberger R., Neuhaus E.M.,
RA   Maniak M., Soldati T.;
RT   "Dictyostelium discoideum protein disulfide isomerase, an endoplasmic
RT   reticulum resident enzyme lacking a KDEL-type retrieval signal.";
RL   FEBS Lett. 418:357-362(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC       bonds, may be involved in glycosylation, prolyl hydroxylation and
CC       triglyceride transfer. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:9428745}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AF019112; AAB86685.1; -; mRNA.
DR   EMBL; AAFI02000014; EAL69370.1; -; Genomic_DNA.
DR   RefSeq; XP_643357.1; XM_638265.1.
DR   AlphaFoldDB; Q86IA3; -.
DR   SMR; Q86IA3; -.
DR   STRING; 44689.DDB0185040; -.
DR   PaxDb; Q86IA3; -.
DR   ABCD; Q86IA3; 2 sequenced antibodies.
DR   EnsemblProtists; EAL69370; EAL69370; DDB_G0276141.
DR   GeneID; 8620407; -.
DR   KEGG; ddi:DDB_G0276141; -.
DR   dictyBase; DDB_G0276141; pdi1.
DR   eggNOG; KOG0191; Eukaryota.
DR   HOGENOM; CLU_038617_1_0_1; -.
DR   InParanoid; Q86IA3; -.
DR   OMA; FINEHAG; -.
DR   PhylomeDB; Q86IA3; -.
DR   PRO; PR:Q86IA3; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IGI:dictyBase.
DR   GO; GO:0006457; P:protein folding; ISS:dictyBase.
DR   CDD; cd00238; ERp29c; 1.
DR   Gene3D; 1.20.1150.12; -; 1.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR011679; ERp29_C.
DR   InterPro; IPR036356; ERp29_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF47933; SSF47933; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..363
FT                   /note="Protein disulfide-isomerase 1"
FT                   /id="PRO_0000327718"
FT   DOMAIN          21..132
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          133..285
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..54
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        172..175
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        307
FT                   /note="T -> I (in Ref. 1; AAB86685)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  39905 MW;  774E3D9AC0434A91 CRC64;
     MKILLFVTLI ALAFVALCSA EGNVVVLSPD NFDTVVDGSK TVFVKFYAPW CGHCKKLAPD
     FEILADTFAP VSNKVVIAKV DCDQADNKAL CSKYDVSGYP TLKIFDKSTT AKDYNGARSV
     DELLTYINNH AKTNVKVKKA PSNVVDLSPS NFDSVVLDKS KNVLVEFYAP WCGHCKKLMP
     DYEILGNTYA NEKDVVIAKI DCDAADNKAI CSKYGVTGFP TLKWFGKQSK DGEKYEQGRD
     LDTFINYINK QAGVNRVKGG KLAVGAGRVE QLDTIATEFI AAAAEVRKEL VKKAQTVVDS
     LPEELRTEGS YYVKVMKTIA EKSIDFVTTE IARITKLVSG SMSGKKADEF AKKLNILESF
     KSK