ID   TMX3_PONAB              Reviewed;         454 AA.
AC   Q5R875;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein disulfide-isomerase TMX3;
DE            EC=5.3.4.1;
DE   AltName: Full=Thioredoxin domain-containing protein 10;
DE   AltName: Full=Thioredoxin-related transmembrane protein 3;
DE   Flags: Precursor;
GN   Name=TMX3; Synonyms=TXNDC10;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable disulfide isomerase, which participates in the
CC       folding of proteins containing disulfide bonds. May act as a dithiol
CC       oxidase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC       for type I membrane proteins. {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CR859879; CAH92035.1; -; mRNA.
DR   RefSeq; NP_001126183.1; NM_001132711.1.
DR   AlphaFoldDB; Q5R875; -.
DR   SMR; Q5R875; -.
DR   STRING; 9601.ENSPPYP00000010356; -.
DR   GeneID; 100173147; -.
DR   KEGG; pon:100173147; -.
DR   CTD; 54495; -.
DR   eggNOG; KOG4277; Eukaryota.
DR   InParanoid; Q5R875; -.
DR   OrthoDB; 746938at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:UniProtKB-EC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Membrane;
KW   Redox-active center; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..454
FT                   /note="Protein disulfide-isomerase TMX3"
FT                   /id="PRO_0000034187"
FT   TOPO_DOM        25..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..454
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..128
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          412..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           451..454
FT                   /note="Di-lysine motif"
FT   COMPBIAS        412..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..56
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   454 AA;  51844 MW;  174103DD6A9FBE5A CRC64;
     MAAWKSWAAL RLCATVVLLD MVVCKGFVED LDESFKENRN DDIWLVDFYA PWCGHCKKLE
     PIWNEVGLEM KSIGSPVKVG KMDATSYSSI ASEFGVRGYP TIKLLKGDLA YNHRGPRTKD
     DIIEFAHRVS GALIRPLPSQ QMFEHMQKRH RVFFVYIGGE SPLKEKYIDA ASELIVYTYF
     FSASEEVVPE YVTLKEMPAV LVFKDETYFV YDEYEDGDLS SWINRERFQN YLAMDGFLLY
     ELGDTGKLVA LAVIDEKNTS VEHTRLKSII QEVARDYRDL FHRDFQFGHM DGNDYINTLL
     MDELTVPTVV VLNTSNQQYF LLDRQIKNVE DMVQFINNIL DGTVEAQGGD SILQRLKRIV
     FDAKSTIVSI FKSSPLMGCF LFGLPLGVIS IMCYGIYTAD TDGGYIEERY EVSKSENENQ
     EQIEESKEQQ EPSSGGSVVP TVQEPKDVLE KKKD