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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

  1. integrin activation Source: UniProtKB
  2. negative regulation of glucose import in response to insulin stimulus Source: UniProtKB
  3. positive regulation of cell proliferation Source: UniProtKB
  4. positive regulation of immunoglobulin biosynthetic process Source: UniProtKB
  5. regulation of B cell proliferation Source: UniProtKB
  6. 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
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1917066. Mzb1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum chaperone complex Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB
  4. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491C → A: Reduced electrophoretic mobility; when associated with A-52. 1 Publication
Mutagenesisi52 – 521C → A: Reduced electrophoretic mobility; when associated with A-49. 1 Publication
Mutagenesisi94 – 941C → A: Small loss of electrophoretic mobility. 1 Publication
Mutagenesisi142 – 1421C → A: Small loss of electrophoretic mobility. 1 Publication
Mutagenesisi170 – 1701C → A: Reduced electrophoretic mobility; when associated with A-177. 1 Publication
Mutagenesisi177 – 1771C → A: Reduced electrophoretic mobility; when associated with A-170. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 188168Marginal zone B- and B1-cell-specific proteinPRO_0000318741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.
PRIDEiQ9D8I1.

PTM databases

PhosphoSiteiQ9D8I1.

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

BgeeiQ9D8I1.
CleanExiMM_2010001M09RIK.
GenevestigatoriQ9D8I1.

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.

Structurei

3D structure databases

ProteinModelPortaliQ9D8I1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 1884Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the MZB1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG74024.
GeneTreeiENSGT00390000002716.
HOGENOMiHOG000068171.
HOVERGENiHBG108230.
InParanoidiQ9D8I1.
OMAiEKYSAHM.
OrthoDBiEOG7D2FFZ.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61P → T in BAC40141 (PubMed:16141072).Curated
Sequence conflicti11 – 111F → L in ACY74344 (PubMed:19805157).Curated
Sequence conflicti11 – 111F → L in BAB25410 (PubMed:16141072).Curated
Sequence conflicti31 – 311P → H in ACY74344 (PubMed:19805157).Curated
Sequence conflicti31 – 311P → H in BAB25410 (PubMed:16141072).Curated
Sequence conflicti136 – 1361N → S in BAB25410 (PubMed:16141072).Curated

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.

PTM databases

PhosphoSiteiQ9D8I1.

Proteomic databases

MaxQBiQ9D8I1.
PaxDbiQ9D8I1.
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

eggNOGiNOG74024.
GeneTreeiENSGT00390000002716.
HOGENOMiHOG000068171.
HOVERGENiHBG108230.
InParanoidiQ9D8I1.
OMAiEKYSAHM.
OrthoDBiEOG7D2FFZ.
PhylomeDBiQ9D8I1.
TreeFamiTF329450.

Miscellaneous databases

NextBioi330410.
PROiQ9D8I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8I1.
CleanExiMM_2010001M09RIK.
GenevestigatoriQ9D8I1.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin."
    Shimizu Y., Meunier L., Hendershot L.M.
    Proc. Natl. Acad. Sci. U.S.A. 106:17013-17018(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN ER CHAPERONE COMPLEX, DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS SPECTROMETRY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Small intestine and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISULFIDE BONDS, MUTAGENESIS OF CYS-49; CYS-52; CYS-94; CYS-142; CYS-170 AND CYS-177, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Mzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cells."
    Flach H., Rosenbaum M., Duchniewicz M., Kim S., Zhang S.L., Cahalan M.D., Mittler G., Grosschedl R.
    Immunity 33:723-735(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HSP90B1 AND PDIA3.
  6. "Novel hormone-regulated genes in visceral adipose tissue: cloning and identification of proinflammatory cytokine-like mouse and human MEDA-7: implications for obesity, insulin resistance and the metabolic syndrome."
    Zhang H., Chen X., Sairam M.R.
    Diabetologia 54:2368-2380(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.

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: February 4, 2015
This is version 81 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

External Data

Dasty 3

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 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.