ID Y5025_DICDI Reviewed; 409 AA. AC Q869Z0; Q553V3; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Putative protein disulfide-isomerase DDB_G0275025; DE EC=5.3.4.1; DE Flags: Precursor; GN ORFNames=DDB_G0275025; OS Dictyostelium discoideum (Social amoeba). 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=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 [2] 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 [3] RP PROTEIN SEQUENCE OF 146-171; 178-185; 237-243 AND 389-397, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=AX2; RA Bienvenut W.V., Ura S., Insall R.H.; RL Submitted (JUL-2009) to UniProtKB. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000013; EAL69793.1; -; Genomic_DNA. DR RefSeq; XP_643858.1; XM_638766.1. DR AlphaFoldDB; Q869Z0; -. DR SMR; Q869Z0; -. DR STRING; 44689.Q869Z0; -. DR PaxDb; 44689-DDB0167375; -. DR EnsemblProtists; EAL69793; EAL69793; DDB_G0275025. DR GeneID; 8619909; -. DR KEGG; ddi:DDB_G0275025; -. DR dictyBase; DDB_G0275025; -. DR eggNOG; KOG0191; Eukaryota. DR HOGENOM; CLU_030311_0_0_1; -. DR InParanoid; Q869Z0; -. DR OMA; FFISYND; -. DR PhylomeDB; Q869Z0; -. DR PRO; PR:Q869Z0; -. DR Proteomes; UP000002195; Chromosome 2. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central. DR Gene3D; 3.40.30.10; Glutaredoxin; 3. DR InterPro; IPR005788; PDI_thioredoxin-like_dom. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01126; pdi_dom; 1. DR PANTHER; PTHR45815; PROTEIN DISULFIDE-ISOMERASE A6; 1. DR PANTHER; PTHR45815:SF3; PROTEIN DISULFIDE-ISOMERASE A6; 1. DR Pfam; PF00085; Thioredoxin; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 3. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Isomerase; Redox-active center; Reference proteome; Repeat; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..409 FT /note="Putative protein disulfide-isomerase DDB_G0275025" FT /id="PRO_0000388368" FT DOMAIN 28..140 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REGION 245..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 406..409 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT COMPBIAS 245..262 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 57..60 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" SQ SEQUENCE 409 AA; 46536 MW; D631EC73ADC097D5 CRC64; MKLINICIFI FAIICIESTF GFYTDNSNVI NLTKKNFQQQ VLNSQQNWMV EFYAPWCGHC KSLKPEYEKV SNNLKGLVKI GAINCDEEKE LCGQYQIQGF PTLKFFSTNP KTGKKGQPED YQGARSASEI AKFSLAKLPS NHIQKVSQDN INKFLTGTSD AKALLFTDKP KTTDLYKALS VDFFKTLTLG EARNLNKETL EKFNIDKFPT LLVFTNDDGE TFTKFDGKLT HSTIYKFLEP FSKKSNNDNN NNNNNNNNEE STKTTTTEKD PASEKFIEIK DEKSFEKSCS TGLCIVALFD QSSIDDKELN EKYLELLNTV SQNFIGRMKF VWVDVSVHDK IVPQFDLSGT PNIFVINNSK KRYTPFMGSF SDESLNSFFK SVLSGLKKAI PFTDSPKFNS QQKKQKDEL //