PDIA4_BOVIN
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 25-MAY-2022, entry version 106.
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; Q29RV1; -.
DR PeptideAtlas; Q29RV1; -.
DR PRIDE; Q29RV1; -.
DR GeneID; 415110; -.
DR KEGG; bta:415110; -.
DR CTD; 9601; -.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; Q29RV1; -.
DR OrthoDB; 462118at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:UniProtKB-EC.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
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 Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
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
