ID E4YTQ3_OIKDI Unreviewed; 491 AA.
AC E4YTQ3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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};
DE Flags: Fragment;
GN ORFNames=GSOID_T00019368001 {ECO:0000313|EMBL:CBY38842.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY38842.1};
RN [1] {ECO:0000313|EMBL:CBY38842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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; FN655339; CBY38842.1; -; Genomic_DNA.
DR AlphaFoldDB; E4YTQ3; -.
DR Proteomes; UP000011014; 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; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
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; 2.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
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 ECO:0000256|PIRSR:PIRSR605792-51}; 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..491
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005128103"
FT DOMAIN 3..129
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 316..462
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 48..51
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 384..387
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT NON_TER 491
FT /evidence="ECO:0000313|EMBL:CBY38842.1"
SQ SEQUENCE 491 AA; 53056 MW; 85115C001D2DE6F5 CRC64;
MKAIIGLLAL VAAEITTEGG VLVGTKENFD EILENNDFVL VEFYAPWCGH CKSLAPEYES
AAGKLAESNP EIKLVKIDAT EEGDIAGEFD VGGYPTLKFF KNGNRNNGIE YGGGRQADDI
VSWLIKKSGP AAIELSGADA AKAAVSDNDV IVVINGKSDE FMAAADSNDD VTFAILDEEA
AAELKVDAGK IALFKTFDDG RVDYTGADSA DDISAFVNSE SLPLVSEFND ETAPKIFGGD
ITQHVLLFAA KSAETYDENY AAMSTAAKDF KGKTLFVVVD CDVEDNSRVL EFFGLTQENC
PAVRLIQMGD SMAKFKPETE EISATSLTSL VEGVESGAIT RHLMSEDIPE SNDGPVFTIV
GKNFEETVND PAKHVLLEFY APWCGHCKAL EPTYEKLGKH FADRDDVIIA KTDATANEFD
GVDVQGFPTI KFFPKGEDAD VIEYEGDRSL EALILFVESD GTEGNEGGDE DEDYDDEDES
NVSCSAIPYF L
//
