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Q9D8I1 (MZB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Mzb1
Synonyms:Pacap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.5 Ref.6

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. Ref.1 Ref.4 Ref.5 Ref.6

Subunit structure

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. Ref.1 Ref.5

Subcellular location

Endoplasmic reticulum. Endoplasmic reticulum lumen. Secreted Ref.4 Ref.5 Ref.6.

Tissue specificity

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. Ref.4 Ref.5 Ref.6

Developmental stage

Up-regulated during plasma cell differentiation. Ref.1 Ref.4

Post-translational modification

Forms an interchain disulfide bond with IgM monomers.

Sequence similarities

Belongs to the MZB1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 188168Marginal zone B- and B1-cell-specific protein
PRO_0000318741

Regions

Motif185 – 1884Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond49 ↔ 177 Ref.4
Disulfide bond52 ↔ 170 Ref.4
Disulfide bond94 ↔ 142 Ref.4

Experimental info

Mutagenesis491C → A: Reduced electrophoretic mobility; when associated with A-52. Ref.4
Mutagenesis521C → A: Reduced electrophoretic mobility; when associated with A-49. Ref.4
Mutagenesis941C → A: Small loss of electrophoretic mobility. Ref.4
Mutagenesis1421C → A: Small loss of electrophoretic mobility. Ref.4
Mutagenesis1701C → A: Reduced electrophoretic mobility; when associated with A-177. Ref.4
Mutagenesis1771C → A: Reduced electrophoretic mobility; when associated with A-170. Ref.4
Sequence conflict61P → T in BAC40141. Ref.2
Sequence conflict111F → L in ACY74344. Ref.1
Sequence conflict111F → L in BAB25410. Ref.2
Sequence conflict311P → H in ACY74344. Ref.1
Sequence conflict311P → H in BAB25410. Ref.2
Sequence conflict1361N → S in BAB25410. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D8I1 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 101640BE6E9B0A93

FASTA18820,580
        10         20         30         40         50         60 
MRLPLPLLLL FGCRAILGSA GDRVSLSASA PTLDDEEKYS AHMPAHLRCD ACRAVAFQMG 

        70         80         90        100        110        120 
QRLAKAEAKS HTPDASGLQE LSESTYTDVL DQTCSQNWQS YGVHEVNQMK RLTGPGLSKG 

       130        140        150        160        170        180 
PEPRISVMIS GGPWPNRLSK TCFHYLGEFG EDQIYEAYRQ GQANLEALLC GGTHGPCSQE 


ILAQREEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1."
van Anken E., Pena F., Hafkemeijer N., Christis C., Romijn E.P., Grauschopf U., Oorschot V.M., Pertel T., Engels S., Ora A., Lastun V., Glockshuber R., Klumperman J., Heck A.J., Luban J., Braakman I.
Proc. Natl. Acad. Sci. U.S.A. 106:17019-17024(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_081498.2. NM_027222.3.
UniGeneMm.27252.

3D structure databases

ProteinModelPortalQ9D8I1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48984N.

PTM databases

PhosphoSiteQ9D8I1.

Proteomic databases

PaxDbQ9D8I1.
PRIDEQ9D8I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025211; ENSMUSP00000025211; ENSMUSG00000024353.
GeneID69816.
KEGGmmu:69816.
UCSCuc008emm.2. mouse.

Organism-specific databases

CTD51237.
MGIMGI:1917066. Mzb1.

Phylogenomic databases

eggNOGNOG74024.
GeneTreeENSGT00390000002716.
HOGENOMHOG000068171.
HOVERGENHBG108230.
InParanoidQ9D8I1.
OMAEKYSAHM.
OrthoDBEOG7D2FFZ.
PhylomeDBQ9D8I1.
TreeFamTF329450.

Gene expression databases

BgeeQ9D8I1.
CleanExMM_2010001M09RIK.
GenevestigatorQ9D8I1.

Family and domain databases

InterProIPR021852. DUF3456.
[Graphical view]
PfamPF11938. DUF3456. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio330410.
PROQ9D8I1.
SOURCESearch...

Entry information

Entry nameMZB1_MOUSE
AccessionPrimary (citable) accession number: Q9D8I1
Secondary accession number(s): D2IYS1 expand/collapse secondary AC list , Q6P3D3, Q8BU13, Q8K2M5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot