ID M3XI22_LATCH Unreviewed; 453 AA.
AC M3XI22;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:ENSLACP00000022378.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022378.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022378.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AFYH01121385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006001538.1; XM_006001476.2.
DR AlphaFoldDB; M3XI22; -.
DR Ensembl; ENSLACT00000026140.1; ENSLACP00000022378.1; ENSLACG00000009322.2.
DR GeneID; 102346219; -.
DR KEGG; lcm:102346219; -.
DR CTD; 54495; -.
DR GeneTree; ENSGT00930000151022; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009322; Expressed in pelvic fin and 6 other cell types or tissues.
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; 2.
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:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..453
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004043341"
FT DOMAIN 1..127
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 400..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 51324 MW; 767392261386E843 CRC64;
MAAVVSSVVC VEILFWAAVV QGFVEDLDDS FKENRKDNIW LVDFYAPWCG HCKKLEPVWN
EVGMELRTTG SPVRVGKMDA TSYSSIASEF GVRGYPTIKL LKGDMAYNYR GPRTKDDIIE
FANRVSGPIV RPLPSQQMFE HVQKRHPVLF VYAGGESPLK EKYIEVASEL IVYTYFFSAS
EEVLPEYVTL HELPAVLVFK DGTYFVYDEY EDGDLSSWVN KERFQGYLNI DGFTLFELGD
TGKMVAIAVI DDKNTIEEHI RLKSVIQEIA KDYREHFSRD FQFGHMDGSD YINSLIMDEV
KVPSVIVLNT SNQQYFVPKK DIESTQDMVQ FLNEILDGTA DAQGGDGFFQ RIKRVAYDAK
STIVSVFKSS PILGCFLFGL PLGVISIMCY GIWTADSDEG SEETEALRKA AKDPELTDED
SDEELEDEDD RENSPEQTDE EQTEKPASEK KTD
//
