VATB2_MOUSE
ID VATB2_MOUSE Reviewed; 511 AA.
AC P62814; O09045; P50517; Q3TG74; Q3TL62; Q3TVK6; Q3TWR0; Q3U791; Q3U7C8;
AC Q3U9Z0; Q3UAW7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=V-type proton ATPase subunit B, brain isoform;
DE Short=V-ATPase subunit B 2;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B 2;
GN Name=Atp6v1b2; Synonyms=Atp6b2, Vat2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8741845; DOI=10.1091/mbc.7.1.129;
RA Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT "Resorption-cycle-dependent polarization of mRNAs for different subunits of
RT V-ATPase in bone-resorbing osteoclasts.";
RL Mol. Biol. Cell 7:129-142(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Westberg M.S., Lundberg L.G.;
RT "Antisense technology and bone resorption.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Brain, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 49-64; 68-130; 164-185; 189-208; 277-308; 322-337;
RP 387-400; 404-430; 437-457; 461-485 AND 495-506, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15013950; DOI=10.1152/ajpcell.00464.2003;
RA Paunescu T.G., Da Silva N., Marshansky V., McKee M., Breton S., Brown D.;
RT "Expression of the 56-kDa B2 subunit isoform of the vacuolar H(+)-ATPase in
RT proton-secreting cells of the kidney and epididymis.";
RL Am. J. Physiol. 287:C149-C162(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16174750; DOI=10.1073/pnas.0506769102;
RA Finberg K.E., Wagner C.A., Bailey M.A., Paunescu T.G., Breton S., Brown D.,
RA Giebisch G., Geibel J.P., Lifton R.P.;
RT "The B1-subunit of the H(+) ATPase is required for maximal urinary
RT acidification.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13616-13621(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17898041; DOI=10.1152/ajprenal.00160.2007;
RA Paunescu T.G., Russo L.M., Da Silva N., Kovacikova J., Mohebbi N.,
RA Van Hoek A.N., McKee M., Wagner C.A., Breton S., Brown D.;
RT "Compensatory membrane expression of the V-ATPase B2 subunit isoform in
RT renal medullary intercalated cells of B1-deficient mice.";
RL Am. J. Physiol. 293:F1915-F1926(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24913193; DOI=10.1038/cr.2014.77;
RA Yuan Y., Zhang J., Chang Q., Zeng J., Xin F., Wang J., Zhu Q., Wu J.,
RA Lu J., Guo W., Yan X., Jiang H., Zhou B., Li Q., Gao X., Yuan H., Yang S.,
RA Han D., Mao Z., Chen P., Lin X., Dai P.;
RT "De novo mutation in ATP6V1B2 impairs lysosome acidification and causes
RT dominant deafness-onychodystrophy syndrome.";
RL Cell Res. 24:1370-1373(2014).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29993276; DOI=10.1152/ajprenal.00539.2017;
RA Frische S., Chambrey R., Trepiccione F., Zamani R., Marcussen N.,
RA Alexander R.T., Skjoedt K., Svenningsen P., Dimke H.;
RT "H+-ATPase B1 subunit localizes to thick ascending limb and distal
RT convoluted tubule of rodent and human kidney.";
RL Am. J. Physiol. 315:F429-F444(2018).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (PubMed:17898041). V-ATPase is responsible
CC for acidifying and maintaining the pH of intracellular compartments and
CC in some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). In renal intercalated cells, can partially compensate the
CC lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine
CC under base-line conditions but not in conditions of acid load
CC (PubMed:17898041). {ECO:0000250|UniProtKB:P21281,
CC ECO:0000269|PubMed:17898041}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). {ECO:0000250|UniProtKB:P21281}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:15013950, ECO:0000269|PubMed:16174750,
CC ECO:0000269|PubMed:17898041, ECO:0000269|PubMed:29993276}. Melanosome
CC {ECO:0000250|UniProtKB:P21281}. Cytoplasm {ECO:0000269|PubMed:15013950,
CC ECO:0000269|PubMed:17898041}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Kidney; found in early distal nephron, encompassing
CC thick ascending limbs and distal convoluted tubules and in the alpha-
CC intercalated cells of the cortical collecting ducts (at protein level)
CC (PubMed:16174750, PubMed:29993276, PubMed:17898041, PubMed:15013950).
CC Expressed in epididymal clear cells (at protein level)
CC (PubMed:15013950). Mainly expressed in the organ of Corti and spiral
CC ganglion neurons, in both the early postnatal cochlea (P2) and the
CC adult cochlea (P30) (PubMed:24913193). {ECO:0000269|PubMed:15013950,
CC ECO:0000269|PubMed:16174750, ECO:0000269|PubMed:17898041,
CC ECO:0000269|PubMed:24913193, ECO:0000269|PubMed:29993276}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown in the whole cochlea,
CC especially in hair cells and spiral ganglion neurons causes a dose-
CC dependent hearing loss. {ECO:0000269|PubMed:24913193}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE30303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30526.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31441.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U13838; AAC52411.1; -; Genomic_DNA.
DR EMBL; Y12634; CAA73182.1; -; mRNA.
DR EMBL; AK146499; BAE27215.1; -; mRNA.
DR EMBL; AK151200; BAE30197.1; -; mRNA.
DR EMBL; AK151322; BAE30303.1; ALT_INIT; mRNA.
DR EMBL; AK151586; BAE30526.1; ALT_INIT; mRNA.
DR EMBL; AK152718; BAE31441.1; ALT_INIT; mRNA.
DR EMBL; AK152766; BAE31479.1; -; mRNA.
DR EMBL; AK159133; BAE34845.1; -; mRNA.
DR EMBL; AK159153; BAE34860.1; -; mRNA.
DR EMBL; AK159586; BAE35206.1; -; mRNA.
DR EMBL; AK159701; BAE35300.1; -; mRNA.
DR EMBL; AK159986; BAE35536.1; -; mRNA.
DR EMBL; AK160080; BAE35612.1; -; mRNA.
DR EMBL; AK160854; BAE36047.1; -; mRNA.
DR EMBL; AK166669; BAE38930.1; -; mRNA.
DR EMBL; AK168852; BAE40674.1; -; mRNA.
DR EMBL; AK169155; BAE40934.1; -; mRNA.
DR EMBL; AK169270; BAE41031.1; -; mRNA.
DR EMBL; BC012497; AAH12497.1; -; mRNA.
DR EMBL; BC046302; AAH46302.1; -; mRNA.
DR EMBL; BC085300; AAH85300.1; -; mRNA.
DR CCDS; CCDS40358.1; -.
DR RefSeq; NP_031535.2; NM_007509.3.
DR AlphaFoldDB; P62814; -.
DR SMR; P62814; -.
DR BioGRID; 198262; 23.
DR IntAct; P62814; 7.
DR MINT; P62814; -.
DR STRING; 10090.ENSMUSP00000006435; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P62814; -.
DR PhosphoSitePlus; P62814; -.
DR SwissPalm; P62814; -.
DR REPRODUCTION-2DPAGE; P62814; -.
DR UCD-2DPAGE; P62814; -.
DR EPD; P62814; -.
DR jPOST; P62814; -.
DR MaxQB; P62814; -.
DR PaxDb; P62814; -.
DR PeptideAtlas; P62814; -.
DR PRIDE; P62814; -.
DR ProteomicsDB; 297957; -.
DR Antibodypedia; 9185; 256 antibodies from 31 providers.
DR DNASU; 11966; -.
DR Ensembl; ENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
DR GeneID; 11966; -.
DR KEGG; mmu:11966; -.
DR UCSC; uc009lww.2; mouse.
DR CTD; 526; -.
DR MGI; MGI:109618; Atp6v1b2.
DR VEuPathDB; HostDB:ENSMUSG00000006273; -.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00940000155068; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P62814; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 541116at2759; -.
DR PhylomeDB; P62814; -.
DR TreeFam; TF300313; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 11966; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Atp6v1b2; mouse.
DR PRO; PR:P62814; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P62814; protein.
DR Bgee; ENSMUSG00000006273; Expressed in pontine nuclear group and 270 other tissues.
DR Genevisible; P62814; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Synapse; Transport.
FT CHAIN 1..511
FT /note="V-type proton ATPase subunit B, brain isoform"
FT /id="PRO_0000144627"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT CONFLICT 22..23
FT /note="GG -> RP (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="S -> G (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="T -> A (in Ref. 3; BAE35206)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..86
FT /note="QV -> AS (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..264
FT /note="NLA -> ILP (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> K (in Ref. 3; BAE35536/BAE35612)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="R -> C (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="M -> T (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> P (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="P -> H (in Ref. 3; BAE35536/BAE35612)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="I -> M (in Ref. 3; BAE40674)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Y -> C (in Ref. 3; BAE35206)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="T -> I (in Ref. 3; BAE30303/BAE30526)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="A -> P (in Ref. 1; AAC52411)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> V (in Ref. 3; BAE30197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56551 MW; E116BF9A36EEF36B CRC64;
MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFEK NFITQGPYEN RTVYETLDIG
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
