ID   PDIA4_BOVIN             Reviewed;         643 AA.
AC   Q29RV1; A5D971; Q0V8E1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   08-NOV-2023, entry version 112.
DE   RecName: Full=Protein disulfide-isomerase A4;
DE            EC=5.3.4.1 {ECO:0000250|UniProtKB:P08003};
DE   Flags: Precursor;
GN   Name=PDIA4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478.
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P08003};
CC   -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC       and very small amounts of ERP29, but not, or at very low levels, CALR
CC       nor CANX. Component of a complex containing at least CRELD2, MANF,
CC       MATN3 and PDIA4 (By similarity). {ECO:0000250|UniProtKB:P08003}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P13667}. Melanosome
CC       {ECO:0000250|UniProtKB:P13667}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC114004; AAI14005.1; -; mRNA.
DR   EMBL; BT026278; ABG81434.1; -; mRNA.
DR   EMBL; BT030490; ABQ12930.1; -; mRNA.
DR   RefSeq; NP_001039344.1; NM_001045879.2.
DR   AlphaFoldDB; Q29RV1; -.
DR   SMR; Q29RV1; -.
DR   IntAct; Q29RV1; 2.
DR   STRING; 9913.ENSBTAP00000022782; -.
DR   PaxDb; 9913-ENSBTAP00000022782; -.
DR   PeptideAtlas; Q29RV1; -.
DR   GeneID; 415110; -.
DR   KEGG; bta:415110; -.
DR   CTD; 9601; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   InParanoid; Q29RV1; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW   Redox-active center; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..643
FT                   /note="Protein disulfide-isomerase A4"
FT                   /id="PRO_0000240338"
FT   DOMAIN          21..168
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          170..300
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          503..634
FT                   /note="Thioredoxin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          24..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           90..93
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:P08003"
FT   MOTIF           553..556
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:P08003"
FT   MOTIF           640..643
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        32..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         365
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13667"
FT   DISULFID        90..93
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P08003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        205..208
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        553..556
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P08003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        16
FT                   /note="V -> A (in Ref. 2; ABG81434)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="T -> S (in Ref. 2; ABG81434/ABQ12930)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="V -> I (in Ref. 2; ABG81434)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   643 AA;  72526 MW;  EFBBB755DE97A35E CRC64;
     MRPRKAWMLV LLLALVQLLA VASAGAPDED STDKEDAIEE DEEEDEDDDD DDDDLEVKEE
     NGVLILNDAN FDNFVADKDT VLLEFYAPWC GHCKQFAPEY EKIAATLKEN DPPIPVAKID
     ATSESALASR FDVSGYPTIK ILKKGQEVDY EGSRTQEEIV AKVKEVSQPN WTPPPEVTLV
     LTKDNFDEVV NDADIILVEF YAPWCGHCKK LAPEYEKAAK ELSKSSPPIP LAKVDAIAET
     DLAKRFDVSS YPTLKIFRKG KAFSYNGPRE KYGIVDYMME QSGPPSKQIL ALKQVQEFLK
     DGDDVIIIGV FKSESDPAYQ LYQDAANSLR EDYKFHHTFS TEIAKFLKVS LGKLVVMQPE
     KFQSKYEPKS YVMDIKDSTE AAAITEHVVK HTLPLVGHRK AADAKRYTRR PLVVVYYSVD
     FSFDYRAATQ FWRNKVLEVA KDFPEYTFAV ADEEDFATEL KDLGLSESGE EVNAAILDEG
     GRRFAMEPDD FDADALRDFV TAFKKGKLKP VIKSQPVPKN NKGPVKVVVG KTFDSIVMDP
     KKDVLIEFYA PWCGHCKQLE PVYTSLGKKY KGHKNLVIAK MDATANDVTS DRYKVEGFPT
     IYFAPSGDKK KPIKFEDGNR DLEHLSKFIE EHATKLSRTK EEL
//