ID   ERP44_BOVIN             Reviewed;         406 AA.
AC   Q3T0L2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Endoplasmic reticulum resident protein 44;
DE            Short=ER protein 44;
DE            Short=ERp44;
DE   AltName: Full=Thioredoxin domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=ERP44; Synonyms=TXNDC4;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates thiol-dependent retention in the early secretory
CC       pathway, forming mixed disulfides with substrate proteins through its
CC       conserved CRFS motif. Inhibits the calcium channel activity of ITPR1.
CC       May have a role in the control of oxidative protein folding in the
CC       endoplasmic reticulum. Required to retain ERO1A and ERO1B in the
CC       endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BS26}.
CC   -!- SUBUNIT: Forms mixed disulfides with both ERO1A and ERO1B and cargo
CC       folding intermediates; the interactions with ERO1A and ERO1B result in
CC       their retention in the endoplasmic reticulum (By similarity). Directly
CC       interacts with ITPR1 in a pH-, redox state- and calcium-dependent
CC       manner, but not with ITPR2 or ITPR3 (By similarity). The strength of
CC       this interaction inversely correlates with calcium concentration (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BS26,
CC       ECO:0000250|UniProtKB:Q9D1Q6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
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DR   EMBL; BC102349; AAI02350.1; -; mRNA.
DR   RefSeq; NP_001030204.1; NM_001035032.2.
DR   AlphaFoldDB; Q3T0L2; -.
DR   SMR; Q3T0L2; -.
DR   STRING; 9913.ENSBTAP00000012930; -.
DR   PaxDb; Q3T0L2; -.
DR   PeptideAtlas; Q3T0L2; -.
DR   PRIDE; Q3T0L2; -.
DR   Ensembl; ENSBTAT00000012930; ENSBTAP00000012930; ENSBTAG00000009804.
DR   GeneID; 506157; -.
DR   KEGG; bta:506157; -.
DR   CTD; 23071; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009804; -.
DR   VGNC; VGNC:28597; ERP44.
DR   eggNOG; KOG0912; Eukaryota.
DR   GeneTree; ENSGT00930000151031; -.
DR   HOGENOM; CLU_054449_1_0_1; -.
DR   InParanoid; Q3T0L2; -.
DR   OMA; IGKLGPC; -.
DR   OrthoDB; 623253at2759; -.
DR   TreeFam; TF106378; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000009804; Expressed in oocyte and 107 other tissues.
DR   ExpressionAtlas; Q3T0L2; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03072; PDI_b'_ERp44; 1.
DR   CDD; cd03070; PDI_b_ERp44; 1.
DR   InterPro; IPR041862; ERp44_PDI_b.
DR   InterPro; IPR041870; ERp44_PDI_b.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Disulfide bond; Endoplasmic reticulum; Reference proteome;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..406
FT                   /note="Endoplasmic reticulum resident protein 44"
FT                   /id="PRO_0000239989"
FT   DOMAIN          30..138
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          236..285
FT                   /note="Interaction with ITPR1"
FT                   /evidence="ECO:0000250"
FT   REGION          360..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           403..406
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   DISULFID        189..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..318
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  46836 MW;  37158394A8BE4075 CRC64;
     MIPGIFLSLP DLRCSLLLLV TWVFTPVTAE IISLDTENID DILNNADVAL VNFYADWCRF
     SQMLHPIFEE ASNVIKEEYP NANQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
     REYRGQRSVK ALADYIRQQK SDPIQELHDL AEITTPDRSK RNIIGYFEQK DSENYRVFER
     VANILHDDCA FLAAFGVVSK PERYSGDNIV YKPPGHSAPD MVYLGSMTNF DGTYNWIQDK
     CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
     CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFRDVLI PGKLKQFVFD LHSGKLHREF
     HHGPDPTDTA PGEEVQDVAS SPPESSFQKL APSEYRYTLL RDRDEL