ID A0CLM8_PARTE Unreviewed; 345 AA.
AC A0CLM8;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Chromosome undetermined scaffold_20, whole genome shotgun sequence {ECO:0000313|EMBL:CAK71695.1};
GN ORFNames=GSPATT00008244001 {ECO:0000313|EMBL:CAK71695.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK71695.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK71695.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK71695.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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; CT868097; CAK71695.1; -; Genomic_DNA.
DR RefSeq; XP_001439092.1; XM_001439055.1.
DR AlphaFoldDB; A0CLM8; -.
DR STRING; 5888.A0CLM8; -.
DR EnsemblProtists; CAK71695; CAK71695; GSPATT00008244001.
DR GeneID; 5024877; -.
DR KEGG; ptm:GSPATT00008244001; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_805249_0_0_1; -.
DR InParanoid; A0CLM8; -.
DR OMA; YGSQISR; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..345
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013265878"
FT DOMAIN 12..128
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 345 AA; 40237 MW; 786F10C5AC96D01C CRC64;
MKYLLTLLFF SLVLGQQVPE ENGVLILSDQ NFEYVLKKYE FVLVDFYAHW CGHCHHLAPV
FASSARQVRN QNVQFAKINC PQYEHLCRKY QVTGFPTLKL FGDGQLLMEY QGDRTEKAIV
DWMRKKTNKG SVEAKSLDQL KKFSESPNLV MVFFGEQKES YEFMQYYQFS QKNKHIPALH
TFNQNFANEM RAQVPSIVVY KPYDERKAAI FDNFEISYIE QFVKKHSYPV LMNFDIQTAK
RIFKGDQPTL ILVQNSQTSQ AEKHLRLALS KIKDQILICI ANTDNKYGLR LMQYFGIQND
YLPQIVAFNP ISDSFNLLSE ITKDGIINFT QSFLGLQQRS QKSDL
//
