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Database: UniProt
Entry: A0A2K6E9X5_MACNE
LinkDB: A0A2K6E9X5_MACNE
Original site: A0A2K6E9X5_MACNE 
ID   A0A2K6E9X5_MACNE        Unreviewed;       454 AA.
AC   A0A2K6E9X5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   Name=TMX3 {ECO:0000313|Ensembl:ENSMNEP00000044964.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000044964.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000044964.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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DR   RefSeq; XP_011731563.1; XM_011733261.1.
DR   AlphaFoldDB; A0A2K6E9X5; -.
DR   SMR; A0A2K6E9X5; -.
DR   STRING; 9545.ENSMNEP00000044964; -.
DR   Ensembl; ENSMNET00000069475.1; ENSMNEP00000044964.1; ENSMNEG00000045035.1.
DR   GeneID; 105476958; -.
DR   KEGG; mni:105476958; -.
DR   CTD; 54495; -.
DR   GeneTree; ENSGT00930000151022; -.
DR   OMA; NSTTQHH; -.
DR   OrthoDB; 52245at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000045035; Expressed in lymph node and 12 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR   CDD; cd03000; PDI_a_TMX3; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..454
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014343840"
FT   TRANSMEM        375..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..131
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          412..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  51868 MW;  D7583312956CD7AE CRC64;
     MAAWRSWAAL RLCATVVLLD MVVCKGFVED LDESFKENRN DDIWLVDFYA PWCGHCKKLE
     PIWNEVGLEM KSIGSPVKVG KMDATSYSSI ASEFGVRGYP TIKLLKGDLA YNYRGPRTKD
     DIIEFAHRVS GALIRPLPSQ QMFEHMQKRH RVFFVYIGGE SPLKEKYIDA ASELIVYTYF
     FSASEEVVPE YVTLKEMPAV LVFKDETYFV YDEYEDGDLS SWINRERFQN YLAMDGFLLY
     ELGDTGKLVA LAVIDEKNTS VEHARLKSII QEVARDYRDL FHRDFQFGHM DGNDYINTLL
     MDELTVPTVV VLNTSNQQYF LLDRQIKNVE DMVQFINNIL DGTVEAQGGD SILQRLKRIV
     FDAKSTIVSI FKSSPLMGCF LFGLPLGVIS IMCYGIYTAD TDGGYIEERY EVSKSENENQ
     EQIGESKEQQ EPSSGESVVP TVQEPKDVLE KKKD
//
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