ID A0A087VHV0_BALRE Unreviewed; 616 AA.
AC A0A087VHV0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 49.
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};
DE Flags: Fragment;
GN ORFNames=N312_03446 {ECO:0000313|EMBL:KFO12192.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12192.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO12192.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12192.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL493951; KFO12192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087VHV0; -.
DR Proteomes; UP000053309; Unassembled WGS sequence.
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; 2.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR041866; PDIA4_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
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; 3.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF210; PROTEIN DISULFIDE-ISOMERASE A4; 1.
DR Pfam; PF00085; Thioredoxin; 3.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 5.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
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:UP000053309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..140
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 144..256
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 476..607
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 177..180
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 526..529
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO12192.1"
FT NON_TER 616
FT /evidence="ECO:0000313|EMBL:KFO12192.1"
SQ SEQUENCE 616 AA; 69533 MW; 038755E9E19DC0F0 CRC64;
ESVTKEADDD GDDDDDEDED DDDDDDSEVK EENGVLVLND ANFDTFTADK DTVLLEFYAP
WCGHCKQFAP EYEKIAKTLK ENDPPIPVAK VDATAATSLA SRFDVSGYPT IKILKKGQPV
DYDGSRTEDA IVAKVKEVSD PNWTPPPEAT LVLTQDNFDD VVNGADIILV EFYAPWCGHC
KRLAPEYEKA AQELSKRTPP IPLAKVDATA ETELAKKFDV TGYPTLKIFR KGKPYDYSGP
REKYGIVDYM IEQAGPPSKQ IQATKQVQEF LRDGDDVIII GVFSGENDKA YQLYQEAANS
LREDYKFHHT FSNEIAKLLK ASPGKLVVMQ PEKFQSKHES KMHVLDLKDS TDGSEIKEHV
LKHALPLVGH RKPSNDAKRY AKRPLVVVYY SVDFSFDYRV ATQYWRGKVL EVAKDFPEYV
FAVSDEEDYS SEIKDLGLLE SGEDVNVAIL DEGGKKYAME PEEFDSDVLR QFVLAFKKGK
LKPIVKSQPV PKNNKGPVKV VVGKTFDTIV MDPKNDVLIE FYAPWCGHCK KLEPVYTELG
KKYKNEKNLV IAKMDATAND VTNDHYKVEG FPTIYFAPRD KKNNPIKFEG GDRDLEHLSK
FIEEHATKLS RAKEEL
//
