Q8WU39 (MZB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Marginal zone B- and B1-cell-specific protein

Alternative name(s):
Mesenteric estrogen-dependent adipose 7
Short name=MEDA-7
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:	MEDA7, PACAP
ORF Names:	HSPC190

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. Isoform 2 may be involved in regulation of apoptosis. Helps to diversify peripheral B-cell functions by regulating Ca2+ stores, antibody secretion and integrin activation. Ref.1 Ref.10 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.10
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 By similarity. Isoform 2 interacts with CASP2 and CASP9. Interacts with HSP90B1 and PDIA3 in a calcium-dependent manner By similarity. Ref.1
Subcellular location	Isoform 1: Endoplasmic reticulum lumen By similarity. Secreted Ref.1 Ref.3 Ref.10. Isoform 2: Cytoplasm. Note: Diffuse granular localization in the cytoplasm surrounding the nucleus. Ref.1 Ref.3 Ref.10
Tissue specificity	Widely expressed with highest levels in adult brain, small intestine and lymphoid tissues such as thymus and spleen. Expression is frequently lower in intestinal-type gastric cancer. In obese patients, more abundant in omental than in subcutaneous fat. Ref.1 Ref.3 Ref.8
Induction	Down-regulated in primary B-cells early after ligand-stimulated activation. Up-regulated in bacterial lipopolysaccharides (LPS)-stimulated peritoneal macrophages. Ref.1 Ref.10
Post-translational modification	Forms an interchain disulfide bond with IgM monomers By similarity.
Sequence similarities	Belongs to the MZB1 family.
Sequence caution	The sequence AAF36110.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Endoplasmic reticulum Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW integrin activation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of glucose import in response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of immunoglobulin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of B cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB endoplasmic reticulum chaperone complex Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum lumen Inferred from sequence or structural similarity. Source: UniProtKB extracellular region Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WU39-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Major.

Isoform 2 (identifier: Q8WU39-2)

The sequence of this isoform differs from the canonical sequence as follows:
     60-189: MWQNLAKAET...EKVSATREEL → SLLVPDVAKS...PSETSHRPRT

Isoform 3 (identifier: Q8WU39-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
     93-101: RSCSRNWQD → MPAELWLTS

Isoform 4 (identifier: Q8WU39-4)

The sequence of this isoform differs from the canonical sequence as follows:
     60-75: MWQNLAKAETKLHTSN → RLCSYPPHLPLTEQQS
     76-189: Missing.

Isoform 5 (identifier: Q8WU39-5)

The sequence of this isoform differs from the canonical sequence as follows:
     60-62: MWQ → AHP
     63-189: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 189	167	Marginal zone B- and B1-cell-specific protein		PRO_0000318740
Regions
	Motif	186 – 189	4	Prevents secretion from ER Potential
Amino acid modifications
	Disulfide bond	50 ↔ 178		By similarity
	Disulfide bond	53 ↔ 171		By similarity
	Disulfide bond	95 ↔ 143		By similarity
Natural variations
	Alternative sequence	1 – 92	92	Missing in isoform 3.		VSP_031280
	Alternative sequence	60 – 189	130	MWQNL…TREEL → SLLVPDVAKSGKGRDQTSYL KLWGAAGAERVGLHGCPGPE LLPELAGLRSSRSGPSETSH RPRT in isoform 2.		VSP_031281
	Alternative sequence	60 – 75	16	MWQNL…LHTSN → RLCSYPPHLPLTEQQS in isoform 4.		VSP_038333
	Alternative sequence	60 – 62	3	MWQ → AHP in isoform 5.		VSP_039073
	Alternative sequence	63 – 189	127	Missing in isoform 5.		VSP_039074
	Alternative sequence	76 – 189	114	Missing in isoform 4.		VSP_038334
	Alternative sequence	93 – 101	9	RSCSRNWQD → MPAELWLTS in isoform 3.		VSP_038332
Experimental info
	Mutagenesis	50	1	C → S: Does not affect activity. Ref.3
	Mutagenesis	53	1	C → S: No significant activity. Ref.3
	Mutagenesis	95	1	C → S: No significant activity. Ref.3
	Mutagenesis	143	1	C → S: No significant activity. Ref.3
	Mutagenesis	171	1	C → S: No significant activity. Ref.3
	Mutagenesis	178	1	C → S: Does not affect activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: C71AED212D3393D3	FASTA	189	20,694
	10 20 30 40 50 60 MRLSLPLLLL LLGAWAIPGG LGDRAPLTAT APQLDDEEMY SAHMPAHLRC DACRAVAYQM 70 80 90 100 110 120 WQNLAKAETK LHTSNSGGRR ELSELVYTDV LDRSCSRNWQ DYGVREVDQV KRLTGPGLSE 130 140 150 160 170 180 GPEPSISVMV TGGPWPTRLS RTCLHYLGEF GEDQIYEAHQ QGRGALEALL CGGPQGACSE KVSATREEL
	Isoform 2 [UniParc]. Checksum: C21A354CE08A95CB	FASTA	123	13,066
	10 20 30 40 50 60 MRLSLPLLLL LLGAWAIPGG LGDRAPLTAT APQLDDEEMY SAHMPAHLRC DACRAVAYQS 70 80 90 100 110 120 LLVPDVAKSG KGRDQTSYLK LWGAAGAERV GLHGCPGPEL LPELAGLRSS RSGPSETSHR PRT
	Isoform 3 [UniParc]. Checksum: 8BA52E533824C02C	FASTA	97	10,488
	10 20 30 40 50 60 MPAELWLTSY GVREVDQVKR LTGPGLSEGP EPSISVMVTG GPWPTRLSRT CLHYLGEFGE 70 80 90 DQIYEAHQQG RGALEALLCG GPQGACSEKV SATREEL
	Isoform 4 [UniParc]. Checksum: C43C7E99CF029FF8	FASTA	75	8,227
	10 20 30 40 50 60 MRLSLPLLLL LLGAWAIPGG LGDRAPLTAT APQLDDEEMY SAHMPAHLRC DACRAVAYQR 70 LCSYPPHLPL TEQQS
	Isoform 5 [UniParc]. Checksum: 7E1F097F7B9F33F4	FASTA	62	6,681
	10 20 30 40 50 60 MRLSLPLLLL LLGAWAIPGG LGDRAPLTAT APQLDDEEMY SAHMPAHLRC DACRAVAYQA HP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel proapoptotic caspase-2- and caspase-9-binding protein." Bonfoco E., Li E., Kolbinger F., Cooper N.R. J. Biol. Chem. 276:29242-29250(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH CASP2 AND CASP9.
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Umbilical cord blood.
[3]	"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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-50; CYS-53; CYS-95; CYS-143; CYS-171 AND CYS-178.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Thymus.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[6]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1 AND 3). Tissue: B-cell and Lymph.
[8]	"MGC29506 gene, frequently down-regulated in intestinal-type gastric cancer, encodes secreted-type protein with conserved cysteine residues." Katoh M., Katoh M. Int. J. Oncol. 23:235-241(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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: SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF338109 mRNA. Translation: AAK84085.1. AF151024 mRNA. Translation: AAF36110.1. Sequence problems. BP366737 mRNA. No translation available. GQ477350 mRNA. Translation: ACY74343.1. AK292706 mRNA. Translation: BAF85395.1. AL698690 mRNA. No translation available. AC135457 Genomic DNA. No translation available. BC009931 mRNA. Translation: AAH09931.2. BC021275 mRNA. Translation: AAH21275.1.
IPI	IPI00102821. IPI00382735. IPI00885163. IPI00952710. IPI00966819.
RefSeq	NP_057543.2. NM_016459.3.
UniGene	Hs.409563.
3D structure databases
ProteinModelPortal	Q8WU39.
ModBase	Search...
PTM databases
PhosphoSite	Q8WU39.
Polymorphism databases
DMDM	74730663.
Proteomic databases
PaxDb	Q8WU39.
PRIDE	Q8WU39.
Protocols and materials databases
DNASU	51237.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302125; ENSP00000303920; ENSG00000170476. ENST00000412103; ENSP00000414565; ENSG00000170476. ENST00000417694; ENSP00000415420; ENSG00000170476. ENST00000457570; ENSP00000406529; ENSG00000170476. ENST00000503481; ENSP00000423205; ENSG00000170476.
GeneID	51237.
KEGG	hsa:51237.
UCSC	uc003lei.3. human. uc010jfd.3. human.
Organism-specific databases
CTD	51237.
GeneCards	GC05M138723.
HGNC	HGNC:30125. MZB1.
HPA	HPA043745.
MIM	609447. gene.
neXtProt	NX_Q8WU39.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG74024.
HOGENOM	HOG000068171.
HOVERGEN	HBG108230.
InParanoid	Q8WU39.
OMA	EKYSAHM.
PhylomeDB	Q8WU39.
Gene expression databases
ArrayExpress	Q8WU39.
Bgee	Q8WU39.
Genevestigator	Q8WU39.
Family and domain databases
InterPro	IPR021852. DUF3456. [Graphical view]
Pfam	PF11938. DUF3456. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MZB1. human.
GenomeRNAi	51237.
NextBio	54355.
SOURCE	Search...

Entry information

Entry name

MZB1_HUMAN

Accession

Primary (citable) accession number: Q8WU39
Secondary accession number(s): D2IYS0 , Q7Z6N2, Q96RL5, Q9P0T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.