ID   MZB1_BOVIN              Reviewed;         189 AA.
AC   A5PJ93;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Marginal zone B- and B1-cell-specific protein;
DE   AltName: Full=Plasma cell-induced resident endoplasmic reticulum protein;
DE            Short=Plasma cell-induced resident ER protein;
DE            Short=pERp1;
DE   AltName: Full=Proapoptotic caspase adapter protein;
DE   Flags: Precursor;
GN   Name=MZB1; Synonyms=PACAP;
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=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Associates with immunoglobulin M (IgM) heavy and light chains
CC       and promotes IgM assembly and secretion. May exert its effect by acting
CC       as a molecular chaperone or as an oxidoreductase as it displays a low
CC       level of oxidoreductase activity (By similarity). Helps to diversify
CC       peripheral B-cell functions by regulating Ca(2+) stores, antibody
CC       secretion, and integrin activation (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Acts as a hormone-regulated adipokine/pro-inflammatory
CC       cytokine that is implicated in causing chronic inflammation, affecting
CC       cellular expansion and blunting insulin response in adipocytes. May
CC       have a role in the onset of insulin resistance (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the ER chaperone complex, a multi-protein complex in
CC       the endoplasmic reticulum containing a large number of molecular
CC       chaperones which associates with unassembled incompletely folded
CC       immunoglobulin heavy chains. Interacts with HSP90B1 and PDIA3 in a
CC       calcium-dependent manner. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:Q8WU39}. Secreted
CC       {ECO:0000250|UniProtKB:Q8WU39}.
CC   -!- PTM: Forms an interchain disulfide bond with IgM monomers.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MZB1 family. {ECO:0000305}.
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DR   EMBL; BC142012; AAI42013.1; -; mRNA.
DR   RefSeq; NP_001092400.1; NM_001098930.2.
DR   AlphaFoldDB; A5PJ93; -.
DR   SMR; A5PJ93; -.
DR   STRING; 9913.ENSBTAP00000047624; -.
DR   PaxDb; A5PJ93; -.
DR   PRIDE; A5PJ93; -.
DR   Ensembl; ENSBTAT00000057188; ENSBTAP00000047624; ENSBTAG00000038337.
DR   GeneID; 510480; -.
DR   KEGG; bta:510480; -.
DR   CTD; 51237; -.
DR   VEuPathDB; HostDB:ENSBTAG00000038337; -.
DR   VGNC; VGNC:31849; MZB1.
DR   eggNOG; ENOG502S4B7; Eukaryota.
DR   GeneTree; ENSGT00390000002716; -.
DR   HOGENOM; CLU_113467_1_0_1; -.
DR   InParanoid; A5PJ93; -.
DR   OMA; MWQHLAK; -.
DR   OrthoDB; 1464647at2759; -.
DR   TreeFam; TF329450; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000038337; Expressed in spleen and 87 other tissues.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR   GO; GO:0030888; P:regulation of B cell proliferation; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..189
FT                   /note="Marginal zone B- and B1-cell-specific protein"
FT                   /id="PRO_0000318739"
FT   MOTIF           186..189
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..171
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..143
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  20699 MW;  A8A717AC1E76DE1E CRC64;
     MRLSLLLLLP LLGAWAIPGG FGDEASLTAT APELDDEEKF STHIPTHLRC DACRAVAYQM
     WQHLTKAEAK LLPLDSGGRR ELSESVYTDV LDQSCSQTWQ GYGVGEVDQV KRLMGPGLST
     GAQPSIMVMI MEGLWPTRLS KTCFHYLGEF GEDQIYEAHQ QGRGTLEALL CGGPRGACSE
     KAPDTRTEL