P62814 (VATB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V-type proton ATPase subunit B, brain isoform
Short name=V-ATPase subunit B 2

Alternative name(s):
Endomembrane proton pump 58 kDa subunit
Vacuolar proton pump subunit B 2

Gene names

Name:	Atp6v1b2
Synonyms:	Atp6b2, Vat2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subunit structure	V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).
Subcellular location	Endomembrane system; Peripheral membrane protein. Melanosome By similarity. Note: Endomembrane.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.
Sequence caution	The sequence BAE30303.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE30526.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE31441.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 16177003PubMed 17898041. Source: UniProtKB endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell microvillus Inferred from direct assay PubMed 17898041PubMed 18667600. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 16177003. Source: UniProtKB proton-transporting V-type ATPase, V1 domain Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	V-type proton ATPase subunit B, brain isoform		PRO_0000144627
Amino acid modifications
	Modified residue	404	1	Phosphoserine Ref.7
	Modified residue	498	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	22 – 23	2	GG → RP in AAC52411. Ref.1
	Sequence conflict	36	1	S → G in AAC52411. Ref.1
	Sequence conflict	80	1	T → A in BAE35206. Ref.3
	Sequence conflict	85 – 86	2	QV → AS in AAC52411. Ref.1
	Sequence conflict	262 – 264	3	NLA → ILP in AAC52411. Ref.1
	Sequence conflict	270	1	E → K in BAE35536. Ref.3
	Sequence conflict	270	1	E → K in BAE35612. Ref.3
	Sequence conflict	276	1	R → C in AAC52411. Ref.1
	Sequence conflict	300	1	M → T in AAC52411. Ref.1
	Sequence conflict	304	1	A → P in AAC52411. Ref.1
	Sequence conflict	318	1	P → H in BAE35536. Ref.3
	Sequence conflict	318	1	P → H in BAE35612. Ref.3
	Sequence conflict	365	1	I → M in BAE40674. Ref.3
	Sequence conflict	371	1	Y → C in BAE35206. Ref.3
	Sequence conflict	373	1	T → I in BAE30303. Ref.3
	Sequence conflict	373	1	T → I in BAE30526. Ref.3
	Sequence conflict	405	1	A → P in AAC52411. Ref.1
	Sequence conflict	437	1	A → V in BAE30197. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P62814 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: E116BF9A36EEF36B	FASTA	511	56,551
	10 20 30 40 50 60 MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL 70 80 90 100 110 120 DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR 130 140 150 160 170 180 TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM 190 200 210 220 230 240 NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET 250 260 270 280 290 300 ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM 310 320 330 340 350 360 SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD 370 380 390 400 410 420 ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN 430 440 450 460 470 480 QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFEK NFITQGPYEN RTVYETLDIG 490 500 510 WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts." Laitala T., Howell M.L., Dean G.E., Vaananen H.K. Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Antisense technology and bone resorption." Westberg M.S., Lundberg L.G. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[3]	"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. Tissue: Amnion, Bone marrow, Brain and Heart.
[4]	"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]. Tissue: Eye and Olfactory epithelium.
[5]	Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 49-64; 68-130; 164-185; 189-208; 277-308; 322-337; 387-400; 404-430; 437-457; 461-485 AND 495-506, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[6]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, MASS SPECTROMETRY. Tissue: Brain cortex.
[7]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U13838 Genomic DNA. Translation: AAC52411.1. Y12634 mRNA. Translation: CAA73182.1. AK146499 mRNA. Translation: BAE27215.1. AK151200 mRNA. Translation: BAE30197.1. AK151322 mRNA. Translation: BAE30303.1. Different initiation. AK151586 mRNA. Translation: BAE30526.1. Different initiation. AK152718 mRNA. Translation: BAE31441.1. Different initiation. AK152766 mRNA. Translation: BAE31479.1. AK159133 mRNA. Translation: BAE34845.1. AK159153 mRNA. Translation: BAE34860.1. AK159586 mRNA. Translation: BAE35206.1. AK159701 mRNA. Translation: BAE35300.1. AK159986 mRNA. Translation: BAE35536.1. AK160080 mRNA. Translation: BAE35612.1. AK160854 mRNA. Translation: BAE36047.1. AK166669 mRNA. Translation: BAE38930.1. AK168852 mRNA. Translation: BAE40674.1. AK169155 mRNA. Translation: BAE40934.1. AK169270 mRNA. Translation: BAE41031.1. BC012497 mRNA. Translation: AAH12497.1. BC046302 mRNA. Translation: AAH46302.1. BC085300 mRNA. Translation: AAH85300.1.
IPI	IPI00119113.
RefSeq	NP_031535.2. NM_007509.3.
UniGene	Mm.249096.
3D structure databases
ProteinModelPortal	P62814.
SMR	P62814. Positions 55-505.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62814. 5 interactions.
MINT	MINT-4139762.
PTM databases
PhosphoSite	P62814.
2D gel databases
REPRODUCTION-2DPAGE	P62814.
UCD-2DPAGE	P62814.
Proteomic databases
PaxDb	P62814.
PRIDE	P62814.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
GeneID	11966.
KEGG	mmu:11966.
UCSC	uc009lww.2. mouse.
Organism-specific databases
CTD	526.
MGI	MGI:109618. Atp6v1b2.
Phylogenomic databases
eggNOG	COG1156.
GeneTree	ENSGT00550000074724.
HOVERGEN	HBG002176.
InParanoid	P62814.
KO	K02147.
OMA	LMKEGIG.
OrthoDB	EOG4HMJ93.
Gene expression databases
ArrayExpress	P62814.
Bgee	P62814.
CleanEx	MM_ATP6V1B2.
Genevestigator	P62814.
GermOnline	ENSMUSG00000006273. Mus musculus.
Family and domain databases
InterPro	IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR005723. ATPase_V1-cplx_bsu. IPR027417. P-loop_NTPase. IPR022879. V-ATPase_su_B/beta. [Graphical view]
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR01040. V-ATPase_V1_B. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP6V1B2. mouse.
NextBio	280091.
SOURCE	Search...

Entry information

Entry name

VATB2_MOUSE

Accession

Primary (citable) accession number: P62814
Secondary accession number(s): O09045 , P50517, Q3TG74, Q3TL62, Q3TVK6, Q3TWR0, Q3U791, Q3U7C8, Q3U9Z0, Q3UAW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program