TXND_THEPA
ID TXND_THEPA Reviewed; 220 AA.
AC Q4N4N8; Q8WPN8;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Thioredoxin domain-containing protein;
DE AltName: Full=Membrane protein 23 {ECO:0000303|PubMed:12034460};
DE Short=mp23 {ECO:0000303|PubMed:12034460};
DE Flags: Precursor;
GN OrderedLocusNames=TP02_0602;
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC83099.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=12034460; DOI=10.1016/s0166-6851(02)00036-1;
RA Ebel T., Bender K., Bocskor U., Binder B.R., Lipp J.;
RT "mp23, a Theileria parva transmembrane protein with homology to the protein
RT disulfide isomerase family.";
RL Mol. Biochem. Parasitol. 121:265-268(2002).
RN [2] {ECO:0000312|EMBL:EAN32885.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga;
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12034460}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12034460}.
CC -!- DEVELOPMENTAL STAGE: Expressed in schizonts (at protein level).
CC {ECO:0000269|PubMed:12034460}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250|UniProtKB:P68978}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC83099.1; Type=Erroneous initiation; Evidence={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; AJ300678; CAC83099.1; ALT_INIT; mRNA.
DR EMBL; AAGK01000002; EAN32885.1; -; Genomic_DNA.
DR RefSeq; XP_765168.1; XM_760075.1.
DR AlphaFoldDB; Q4N4N8; -.
DR SMR; Q4N4N8; -.
DR STRING; 5875.XP_765168.1; -.
DR EnsemblProtists; EAN32885; EAN32885; TP02_0602.
DR GeneID; 3501428; -.
DR KEGG; tpv:TP02_0602; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_02g00602; -.
DR eggNOG; KOG0191; Eukaryota.
DR InParanoid; Q4N4N8; -.
DR OMA; FKDMANE; -.
DR Proteomes; UP000001949; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Membrane; Redox-active center;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..220
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390500"
FT TOPO_DOM 20..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..141
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000305"
FT MOTIF 217..220
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q2TBU2"
FT DISULFID 64..67
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 220 AA; 24679 MW; 62E4833A9351C1D8 CRC64;
MKFLILNCLI LFSLISSEAT NVKLDREDQN HLVLLNEKNF EKLTQASTGA TTGTWFVKFY
APWCSHCRKM APAWESLAKA LKGQVNVADV DVTRNLNLGK RFQIRGYPTL LLFHKGKMYQ
YEGGERTVEK LSEFALGDFK NAVGAPVPQP LSLFALVSDF VVSGVNEALR VYDAALAGFV
TISSFSFLFG LLVGLMLSLF LFTRRATRKP KVLTERKKDK
