ID   SEP2_EMIHU              Reviewed;         223 AA.
AC   Q50KB1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Protein disulfide-isomerase-like protein EhSep2;
DE   Flags: Precursor;
GN   Name=SEP2;
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD98262.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-38 AND 98-112.
RC   STRAIN=NIES-873;
RX   PubMed=15743763; DOI=10.1074/jbc.m501517200;
RA   Obata T., Shiraiwa Y.;
RT   "A novel eukaryotic selenoprotein in the haptophyte alga Emiliania
RT   huxleyi.";
RL   J. Biol. Chem. 280:18462-18468(2005).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000255}.
CC   -!- CAUTION: Contains a selenocysteine rather than a cysteine at one of the
CC       conserved active site positions so does not form the disulfide bond
CC       normally required for protein disulfide isomerase activity.
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; AB205027; BAD98262.1; -; mRNA.
DR   STRING; 2903.EOD27297; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; NAS:UniProtKB.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW   Reference proteome; Selenocysteine; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:15743763"
FT   CHAIN           18..223
FT                   /note="Protein disulfide-isomerase-like protein EhSep2"
FT                   /evidence="ECO:0000269|PubMed:15743763"
FT                   /id="PRO_0000248266"
FT   DOMAIN          18..125
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          197..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          155..201
FT                   /evidence="ECO:0000255"
FT   MOTIF           220..223
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   NON_STD         47
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000312|EMBL:BAD98262.1"
FT   CONFLICT        103
FT                   /note="D -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107..108
FT                   /note="ED -> GA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111..112
FT                   /note="GG -> AL (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  24564 MW;  9744C1A547A86F4C CRC64;
     MALRSLTLLC AAAGASAGAI ELTPDNFDEL VLKSGKAAFI KFLAPWUGHC KKMKPDWDSL
     ASTFEDSKKV LIADVDCTTG GKPLCEKYGV RGYPTIKYFN PPDEEGEDYK GGRSLDELKK
     FAENELGPGC SVDLMDNCSE EQKGKLKEYI DMAPEKRTEM LETLKKELAD AESTHEALLK
     ELQATYKESM DKLEKLKEES APKIKLLKAA TPAPKAEGAK DEV