ID A0A2Y9QLD6_TRIMA Unreviewed; 454 AA.
AC A0A2Y9QLD6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=LOC101343301 {ECO:0000313|RefSeq:XP_023580209.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023580209.1};
RN [1] {ECO:0000313|RefSeq:XP_023580209.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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_023580209.1; XM_023724441.1.
DR AlphaFoldDB; A0A2Y9QLD6; -.
DR STRING; 127582.A0A2Y9QLD6; -.
DR KEGG; tmu:101343301; -.
DR InParanoid; A0A2Y9QLD6; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
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_5016148741"
FT DOMAIN 1..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 416..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 51606 MW; 2DBBF488949DB33A CRC64;
MAALSSAAAL RLCATVILLD MVFSKSVVPD LDDSFKESRK DDIWLVDFYA PWCGHCKKLE
PIWNEVGIEM KNMGSPVKVG KMDATSYASL AAEFGVRGYP TIKLLKGDLA YNYRGPRTKD
DIIDFAHRVS GALIRPLPSK QMFEHVQRRH RVFFVYVGGE SPLKEKYVDA ASELIVYSYF
FAASEDVVPE SVVLREVPAV LVFKDDTYFI YDEFEDGDLE SWITRERFQN YLTVDGFLLY
ELGDTGKLVV IAVIDEKNTS IEHTRLKSII QEVAQDYRAH FRRDFHFGHM DGNEYINSLL
MDELMVPTVV VLNTSNQQYF LLDRQIKNAK DMVRFIDSIL NGTVEAQGGD SILQRLKRIM
FDAKTTVVSI FKSSPLMGCF LFGLPLGVIS IMCYGIYSAD TDGGYIEEQY EISKSEMESQ
DLMEESREQQ EPSDGESVVP PMHEPKDALE KKKD
//