PDI2_DICDI
ID PDI2_DICDI Reviewed; 513 AA.
AC Q54EN4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein disulfide-isomerase 2;
DE Short=PDI2;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=pdi2; ORFNames=DDB_G0291434;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
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 {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61701.1; -; Genomic_DNA.
DR RefSeq; XP_635206.1; XM_630114.1.
DR AlphaFoldDB; Q54EN4; -.
DR SMR; Q54EN4; -.
DR STRING; 44689.DDB0231409; -.
DR PaxDb; Q54EN4; -.
DR EnsemblProtists; EAL61701; EAL61701; DDB_G0291434.
DR GeneID; 8628151; -.
DR KEGG; ddi:DDB_G0291434; -.
DR dictyBase; DDB_G0291434; pdi2.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR InParanoid; Q54EN4; -.
DR OMA; YIAKHAT; -.
DR PhylomeDB; Q54EN4; -.
DR Reactome; R-DDI-901042; Calnexin/calreticulin cycle.
DR PRO; PR:Q54EN4; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:dictyBase.
DR GO; GO:0006457; P:protein folding; ISS:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
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; 3.
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 3: Inferred from homology;
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..513
FT /note="Protein disulfide-isomerase 2"
FT /id="PRO_0000327613"
FT DOMAIN 21..147
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 355..486
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 510..513
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 497..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 70..73
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 406..409
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 513 AA; 57753 MW; 8AAB6B6926069852 CRC64;
MNKFLALLFV LALFANIAFS CEGHPEHDHG DGDHEHDHDE SFVKILDSDN FHNSVSEHDV
TLVMFYAPWC GHCKTLKPLY EEAAKQLSAN KKIAIAKVDC TQHEQLCKQN KVQGYPTLVV
FKNGKAEPYE GDRTTKSIVQ TLEEELKPTI STLESNEDIE EFKKQHPISV VGFFDNDHDD
RFKLFSELAG NNKKSAKFAV VIDKDFSKEH VESTPNVVLF RSFDEPTVAH KGEFDSESLI
KFIKGNSVPL LGEINRNTYK KYESIAVPLA YLFIDSTQDN TQVLEDVKKI ATSQKGNAVF
CWVDMKKFPQ QATHMGLSGK VVPAISVDSV ANKARYNFDE KETFSFDTVS KWIQDVIGGK
VSPFVKSQPE PESNDAPVKV AVGTTFKKLV LDSPKDVLVE FYAPWCGHCK NLAPIYDKLG
EYLKDVESVS IVKIDADSND VPSDIEIRGY PTIMLFKADD KENPISYEGQ RNDHMNFVEF
IQDNAAIEFK LPSSQTDDNV ESKKDSSAKH DEL
