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Protein

Marginal zone B- and B1-cell-specific protein

Gene

Mzb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity. Helps to diversify peripheral B-cell functions by regulating Ca2+ stores, antibody secretion and integrin activation.
Acts as a hormone-regulated adipokine/proinflammatory cytokine that is implicated in causing chronic inflammation, affecting cellular expansion and blunting insulin response in adipocytes. May have a role in the onset of insulin resistance.

GO - Biological processi

  • integrin activation Source: UniProtKB
  • negative regulation of glucose import in response to insulin stimulus Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of immunoglobulin biosynthetic process Source: UniProtKB
  • regulation of B cell proliferation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Marginal zone B- and B1-cell-specific protein
Alternative name(s):
Plasma cell-induced resident endoplasmic reticulum protein
Short name:
Plasma cell-induced resident ER protein
Short name:
pERp1
Proapoptotic caspase adapter protein
Gene namesi
Name:Mzb1
Synonyms:Pacap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1917066. Mzb1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum chaperone complex Source: UniProtKB
  • endoplasmic reticulum lumen Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49C → A: Reduced electrophoretic mobility; when associated with A-52. 1 Publication1
Mutagenesisi52C → A: Reduced electrophoretic mobility; when associated with A-49. 1 Publication1
Mutagenesisi94C → A: Small loss of electrophoretic mobility. 1 Publication1
Mutagenesisi142C → A: Small loss of electrophoretic mobility. 1 Publication1
Mutagenesisi170C → A: Reduced electrophoretic mobility; when associated with A-177. 1 Publication1
Mutagenesisi177C → A: Reduced electrophoretic mobility; when associated with A-170. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3259485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000031874121 – 188Marginal zone B- and B1-cell-specific proteinAdd BLAST168

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 1771 Publication
Disulfide bondi52 ↔ 1701 Publication
Disulfide bondi94 ↔ 1421 Publication

Post-translational modificationi

Forms an interchain disulfide bond with IgM monomers.

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9D8I1.
PaxDbiQ9D8I1.
PeptideAtlasiQ9D8I1.
PRIDEiQ9D8I1.

PTM databases

PhosphoSitePlusiQ9D8I1.

Expressioni

Tissue specificityi

Expressed predominantly in the spleen and lymph nodes. Abundantly expressed in marginal zone B and B1 cells. High expression in mesenteric adipose tissue (MAT). Expressed also in pancreas, perigonadal adipose tissue (PAT), uterus, subcutaneous adipose tissue, heart, muscle, ovary and liver. Very low expression is detected in brown adipose tissue. In PAT, significantly higher expression in stromal-vascular cell than in adipocytes. Expressed in macrophage RAW 264.7 cell line. Down-regulated in For-knockout female MAT at 5 months (obese state) followed by steep up-regulation at 9 months (prediabetic condition) when mutants progress towards the metabolic syndrome.3 Publications

Developmental stagei

Up-regulated during plasma cell differentiation.2 Publications

Gene expression databases

BgeeiENSMUSG00000024353.
CleanExiMM_2010001M09RIK.
GenevisibleiQ9D8I1. MM.

Interactioni

Subunit structurei

Part of the ER chaperone complex, a multi-protein complex in the endoplasmic reticulum containing a large number of molecular chaperones which associates with unassembled incompletely folded immunoglobulin heavy chains. Interacts with HSP90B1 and PDIA3 in a calcium-dependent manner.2 Publications

Protein-protein interaction databases

DIPiDIP-48984N.
STRINGi10090.ENSMUSP00000025211.

Structurei

3D structure databases

ProteinModelPortaliQ9D8I1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi185 – 188Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the MZB1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J06F. Eukaryota.
ENOG4111YKY. LUCA.
GeneTreeiENSGT00390000002716.
HOGENOMiHOG000068171.
HOVERGENiHBG108230.
InParanoidiQ9D8I1.
OMAiEKYSAHM.
OrthoDBiEOG091G1197.
PhylomeDBiQ9D8I1.
TreeFamiTF329450.

Family and domain databases

InterProiIPR021852. DUF3456.
[Graphical view]
PfamiPF11938. DUF3456. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D8I1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPLPLLLL FGCRAILGSA GDRVSLSASA PTLDDEEKYS AHMPAHLRCD
60 70 80 90 100
ACRAVAFQMG QRLAKAEAKS HTPDASGLQE LSESTYTDVL DQTCSQNWQS
110 120 130 140 150
YGVHEVNQMK RLTGPGLSKG PEPRISVMIS GGPWPNRLSK TCFHYLGEFG
160 170 180
EDQIYEAYRQ GQANLEALLC GGTHGPCSQE ILAQREEL
Length:188
Mass (Da):20,580
Last modified:February 26, 2008 - v2
Checksum:i101640BE6E9B0A93
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6P → T in BAC40141 (PubMed:16141072).Curated1
Sequence conflicti11F → L in ACY74344 (PubMed:19805157).Curated1
Sequence conflicti11F → L in BAB25410 (PubMed:16141072).Curated1
Sequence conflicti31P → H in ACY74344 (PubMed:19805157).Curated1
Sequence conflicti31P → H in BAB25410 (PubMed:16141072).Curated1
Sequence conflicti136N → S in BAB25410 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ477351 mRNA. Translation: ACY74344.1.
AK008016 mRNA. Translation: BAB25410.1.
AK088094 mRNA. Translation: BAC40141.1.
BC030674 mRNA. Translation: AAH30674.1.
BC064044 mRNA. Translation: AAH64044.1.
CCDSiCCDS29145.1.
RefSeqiNP_081498.2. NM_027222.3.
UniGeneiMm.27252.

Genome annotation databases

EnsembliENSMUST00000025211; ENSMUSP00000025211; ENSMUSG00000024353.
GeneIDi69816.
KEGGimmu:69816.
UCSCiuc008emm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ477351 mRNA. Translation: ACY74344.1.
AK008016 mRNA. Translation: BAB25410.1.
AK088094 mRNA. Translation: BAC40141.1.
BC030674 mRNA. Translation: AAH30674.1.
BC064044 mRNA. Translation: AAH64044.1.
CCDSiCCDS29145.1.
RefSeqiNP_081498.2. NM_027222.3.
UniGeneiMm.27252.

3D structure databases

ProteinModelPortaliQ9D8I1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48984N.
STRINGi10090.ENSMUSP00000025211.

Chemistry databases

ChEMBLiCHEMBL3259485.

PTM databases

PhosphoSitePlusiQ9D8I1.

Proteomic databases

MaxQBiQ9D8I1.
PaxDbiQ9D8I1.
PeptideAtlasiQ9D8I1.
PRIDEiQ9D8I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025211; ENSMUSP00000025211; ENSMUSG00000024353.
GeneIDi69816.
KEGGimmu:69816.
UCSCiuc008emm.2. mouse.

Organism-specific databases

CTDi51237.
MGIiMGI:1917066. Mzb1.

Phylogenomic databases

eggNOGiENOG410J06F. Eukaryota.
ENOG4111YKY. LUCA.
GeneTreeiENSGT00390000002716.
HOGENOMiHOG000068171.
HOVERGENiHBG108230.
InParanoidiQ9D8I1.
OMAiEKYSAHM.
OrthoDBiEOG091G1197.
PhylomeDBiQ9D8I1.
TreeFamiTF329450.

Miscellaneous databases

PROiQ9D8I1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024353.
CleanExiMM_2010001M09RIK.
GenevisibleiQ9D8I1. MM.

Family and domain databases

InterProiIPR021852. DUF3456.
[Graphical view]
PfamiPF11938. DUF3456. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMZB1_MOUSE
AccessioniPrimary (citable) accession number: Q9D8I1
Secondary accession number(s): D2IYS1
, Q6P3D3, Q8BU13, Q8K2M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.