ID H3ACS8_LATCH Unreviewed; 527 AA.
AC H3ACS8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN Name=PDIA2 {ECO:0000313|Ensembl:ENSLACP00000007449.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007449.1, 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:ENSLACP00000007449.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; AFYH01121163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01121166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3ACS8; -.
DR STRING; 7897.ENSLACP00000007449; -.
DR Ensembl; ENSLACT00000007511.1; ENSLACP00000007449.1; ENSLACG00000006605.1.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000165626; -.
DR HOGENOM; CLU_025879_1_0_1; -.
DR InParanoid; H3ACS8; -.
DR OMA; FCHSVFS; -.
DR TreeFam; TF106381; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006605; Expressed in mesonephros.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF93; PROTEIN DISULFIDE-ISOMERASE A2; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 20..527
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005134166"
FT DOMAIN 13..155
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 357..499
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 74..77
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 421..424
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 527 AA; 60271 MW; 2145B2CD39A29E26 CRC64;
MKNFCLPLLT FALFLAVQAN ETEVKEEETS AKEDAQISDE ITEEEDVLIL NQHNFDRALK
ESKFLLVEFY APWCGHCQAI APEYAKAAGL LKNESSEIKL AKVDATEEEE LSAEFEIKGF
PTLKFFKDGD RKNPIDYKGK RTADGIVLWL QRRIGPSATI LNSVASAEEF IESKEIVIVA
FFEDLEDKDV ETFYEVASDT IDATFGITSS AEIFNKYGIS KDTVTLFKKF DEKRADFEVD
EDLGLDKEEL VKFISINSLE LVTEFSEEQN SRKIFEAKIP NHILLFINKT LEQHREILED
FRNVAPSFRG KILFVHIDIN GNNEHVLKYF GLKNEDVPTI RLINIETVKK YIISRKELSA
ETIKNFCQDA VDGKLKPHLM SEDIPEDWDK DPVKVLVGIN FEEVAFHESK NVFVEFYAPW
CEHCKELTPI WDQLGEKYKD HENIVIAKID ATANEVEGIQ VQGFPTIKYF PAGSERKIID
YGAARDLETF SKFLDNGGEL PEEEDETLVS FIFSTIHYSL LDSQPQL
//
