ID F2U1C9_SALR5 Unreviewed; 374 AA.
AC F2U1C9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN ORFNames=PTSG_02152 {ECO:0000313|EMBL:EGD81431.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|EMBL:EGD81431.1, ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; GL832959; EGD81431.1; -; Genomic_DNA.
DR RefSeq; XP_004996635.1; XM_004996578.1.
DR AlphaFoldDB; F2U1C9; -.
DR STRING; 946362.F2U1C9; -.
DR EnsemblProtists; EGD81431; EGD81431; PTSG_02152.
DR GeneID; 16077227; -.
DR KEGG; sre:PTSG_02152; -.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; F2U1C9; -.
DR OMA; HEAANQY; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 20..374
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005129360"
FT DOMAIN 6..127
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 374 AA; 40635 MW; 82BB5F8E77A2CE0A CRC64;
MFKSALVIAL VALACVAHAA DDDVLTLTSD NFDSTIEQND FVVVEFFAPW CGHCKKLAPE
YAKAATILKE DGIVLGAVDA TVESDLASRF GVRGYPTLKL FKHGEATEYK GGRTVDTIVS
YVRKATGPPA VELADVDAVN SFKESGKVVV VGYFDKLDGH EYKAFIDAAK ADEDISYGVT
TNADAASDAG VTAPAVVLYK KFDEGKNVFD AEWSRFNIAD FVTANKLPSV IPFTMDVAGE
IFQSKIGKIA FLFTDEENEA YSEIAKEYKG KFVFATSDSS QTRLTSYLGV EKSDFPTFYI
LETGAQMKKF PIPEGGADAD AIRAHIEEYL AGNLKPHFKS EPVPEPNDGP VTVIVGKNFD
EIVMDESKDV SSRP
//
