ID   MZB1_RAT                Reviewed;         188 AA.
AC   Q561R0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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. {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, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC       Secreted {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; BC093397; AAH93397.1; -; mRNA.
DR   RefSeq; NP_001019411.1; NM_001024240.1.
DR   AlphaFoldDB; Q561R0; -.
DR   SMR; Q561R0; -.
DR   STRING; 10116.ENSRNOP00000030810; -.
DR   PaxDb; Q561R0; -.
DR   Ensembl; ENSRNOT00000036301; ENSRNOP00000030810; ENSRNOG00000022009.
DR   GeneID; 291675; -.
DR   KEGG; rno:291675; -.
DR   UCSC; RGD:1310251; rat.
DR   CTD; 51237; -.
DR   RGD; 1310251; Mzb1.
DR   eggNOG; ENOG502S4B7; Eukaryota.
DR   GeneTree; ENSGT00390000002716; -.
DR   HOGENOM; CLU_113467_1_0_1; -.
DR   InParanoid; Q561R0; -.
DR   OMA; MWQHLAK; -.
DR   OrthoDB; 1464647at2759; -.
DR   PhylomeDB; Q561R0; -.
DR   TreeFam; TF329450; -.
DR   PRO; PR:Q561R0; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000022009; Expressed in spleen and 15 other tissues.
DR   Genevisible; Q561R0; RN.
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.
DR   InterPro; IPR021852; DUF3456.
DR   Pfam; PF11938; DUF3456; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..188
FT                   /note="Marginal zone B- and B1-cell-specific protein"
FT                   /id="PRO_0000318742"
FT   MOTIF           185..188
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   DISULFID        49..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        94..142
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  20712 MW;  9C29308904B277A7 CRC64;
     MRLPLPLLLL FGCRAILGSF GDRVSLSATA PTLDDEEKYA SHMPTHLRCD ACRAVAYQMG
     QHLAKAEAKS HTPDSSGSQE LSESTYTDVL DRTCSQNWQS YGVQEVNQMK RLMGPGLSKG
     PEPSISVMIT GGPWPNRLSM TCFHYLGEFG EDQIYEAYRQ GHETLEALLC GGTHGSCSQE
     IPAQREEL