VATA_MOUSE
ID VATA_MOUSE Reviewed; 617 AA.
AC P50516; Q3TKS0; Q3U5W3; Q3U777; Q3UDZ9; Q3US31; Q8CHX2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2 {ECO:0000269|PubMed:23863464};
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=Atp6v1a; Synonyms=Atp6a1, Atp6a2, Atp6v1a1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 45-56; 143-163; 242-251; 253-262; 266-280; 324-338;
RP 514-530 AND 599-613, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH ATP6V0A4.
RC STRAIN=NOD; TISSUE=Kidney;
RX PubMed=11495928; DOI=10.1074/jbc.m107267200;
RA Smith A.N., Finberg K.E., Wagner C.A., Lifton R.P., Devonald M.A., Su Y.,
RA Karet F.E.;
RT "Molecular cloning and characterization of Atp6n1b: a novel fourth murine
RT vacuolar H+-ATPase a-subunit gene.";
RL J. Biol. Chem. 276:42382-42388(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-384, AND MUTAGENESIS OF SER-384.
RX PubMed=23863464; DOI=10.1152/ajprenal.00303.2013;
RA Alzamora R., Al-Bataineh M.M., Liu W., Gong F., Li H., Thali R.F.,
RA Joho-Auchli Y., Brunisholz R.A., Satlin L.M., Neumann D., Hallows K.R.,
RA Pastor-Soler N.M.;
RT "AMP-activated protein kinase regulates the vacuolar H+-ATPase via direct
RT phosphorylation of the A subunit (ATP6V1A) in the kidney.";
RL Am. J. Physiol. 305:F943-F956(2013).
RN [10]
RP INTERACTION WITH CRYAB AND MTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP SER-411.
RX PubMed=31786107; DOI=10.1016/j.bbagen.2019.129496;
RA Cui X., Feng R., Wang J., Du C., Pi X., Chen D., Li J., Li H., Zhang J.,
RA Zhang J., Mu H., Zhang F., Liu M., Hu Y.;
RT "Heat shock factor 4 regulates lysosome activity by modulating the alphaB-
RT crystallin-ATP6V1A-mTOR complex in ocular lens.";
RL Biochim. Biophys. Acta 1864:129496-129496(2020).
CC -!- FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (PubMed:23863464). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). In aerobic conditions, involved in intracellular iron
CC homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase
CC (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent
CC proteasomal degradation (By similarity). May play a role in neurite
CC development and synaptic connectivity (By similarity).
CC {ECO:0000250|UniProtKB:P38606, ECO:0000269|PubMed:23863464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000269|PubMed:23863464};
CC -!- ACTIVITY REGULATION: ATP hydrolysis occurs at the interface between the
CC nucleotide-binding domains of subunits A and B (By similarity). ATP
CC hydrolysis triggers a conformational change in the subunits D and F,
CC which induces a shift of subunit d (By similarity). The c-ring is
CC subsequently rotated and results in a continuous proton translocation
CC across the membrane (By similarity). {ECO:0000250|UniProtKB:P31404}.
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). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4
CC (PubMed:11495928). Interacts with WFS1 (By similarity). Interacts with
CC alpha-crystallin B chain/CRYAB and with MTOR, forming a ternary complex
CC (PubMed:31786107). {ECO:0000250|UniProtKB:P38606,
CC ECO:0000269|PubMed:11495928, ECO:0000269|PubMed:31786107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23863464}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:31786107}. Cytoplasmic vesicle,
CC secretory vesicle {ECO:0000250|UniProtKB:P38606}. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P31404};
CC Peripheral membrane protein {ECO:0000305}. Lysosome
CC {ECO:0000269|PubMed:31786107}. Note=Co-localizes with WFS1 in the
CC secretory granules in neuroblastoma cell lines.
CC {ECO:0000250|UniProtKB:P38606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50516-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50516-2; Sequence=VSP_024628, VSP_024629;
CC -!- PTM: Phosphorylation at Ser-384 by AMPK down-regulates its enzyme
CC activity. {ECO:0000269|PubMed:23863464}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; U13837; AAC52410.1; -; Genomic_DNA.
DR EMBL; AK140873; BAE24506.1; -; mRNA.
DR EMBL; AK149833; BAE29112.1; -; mRNA.
DR EMBL; AK152785; BAE31494.1; -; mRNA.
DR EMBL; AK153403; BAE31963.1; -; mRNA.
DR EMBL; AK154869; BAE32890.1; -; mRNA.
DR EMBL; AK160792; BAE36015.1; -; mRNA.
DR EMBL; AK166857; BAE39074.1; -; mRNA.
DR EMBL; AK170721; BAE41978.1; -; mRNA.
DR EMBL; BC038392; AAH38392.1; -; mRNA.
DR CCDS; CCDS28182.1; -. [P50516-1]
DR RefSeq; NP_031534.2; NM_007508.5. [P50516-1]
DR RefSeq; XP_006521783.1; XM_006521720.3.
DR RefSeq; XP_006521784.1; XM_006521721.2. [P50516-1]
DR RefSeq; XP_011244111.1; XM_011245809.2.
DR AlphaFoldDB; P50516; -.
DR SMR; P50516; -.
DR BioGRID; 198261; 34.
DR IntAct; P50516; 105.
DR MINT; P50516; -.
DR STRING; 10090.ENSMUSP00000110314; -.
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; P50516; -.
DR PhosphoSitePlus; P50516; -.
DR SwissPalm; P50516; -.
DR EPD; P50516; -.
DR jPOST; P50516; -.
DR MaxQB; P50516; -.
DR PaxDb; P50516; -.
DR PeptideAtlas; P50516; -.
DR PRIDE; P50516; -.
DR ProteomicsDB; 297534; -. [P50516-1]
DR ProteomicsDB; 297535; -. [P50516-2]
DR TopDownProteomics; P50516-1; -. [P50516-1]
DR Antibodypedia; 32600; 201 antibodies from 31 providers.
DR Ensembl; ENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459. [P50516-1]
DR Ensembl; ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459. [P50516-1]
DR GeneID; 11964; -.
DR KEGG; mmu:11964; -.
DR UCSC; uc007zgu.1; mouse. [P50516-1]
DR UCSC; uc007zgw.1; mouse. [P50516-2]
DR CTD; 523; -.
DR MGI; MGI:1201780; Atp6v1a.
DR VEuPathDB; HostDB:ENSMUSG00000052459; -.
DR eggNOG; KOG1352; Eukaryota.
DR GeneTree; ENSGT00550000074787; -.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; P50516; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 241249at2759; -.
DR PhylomeDB; P50516; -.
DR TreeFam; TF300811; -.
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; 11964; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Atp6v1a; mouse.
DR PRO; PR:P50516; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P50516; protein.
DR Bgee; ENSMUSG00000052459; Expressed in cingulate cortex and 262 other tissues.
DR ExpressionAtlas; P50516; baseline and differential.
DR Genevisible; P50516; MM.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; 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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Lysosome;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..617
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144561"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 384
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:23863464"
FT VAR_SEQ 499..509
FT /note="ASLAETDKITL -> VRGGCTGCHAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024628"
FT VAR_SEQ 510..617
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024629"
FT MUTAGEN 384
FT /note="S->A: Significant loss in AMPK-mediated
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:23863464"
FT MUTAGEN 411
FT /note="S->A: Reduces the interaction with CRYAB and MTOR."
FT /evidence="ECO:0000269|PubMed:31786107"
FT CONFLICT 86
FT /note="L -> R (in Ref. 1; AAC52410)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> N (in Ref. 1; AAC52410)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="V -> A (in Ref. 1; AAC52410)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="G -> V (in Ref. 2; BAE39074)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="E -> G (in Ref. 1; AAC52410)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="E -> G (in Ref. 2; BAE31963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 68326 MW; D46AC76D9C7580A7 CRC64;
MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
GVNVSALSRD IKWEFIPSKN LRVGSHITGG DIYGIVNENS LIKHKIMLPP RNRGSVTYIA
PPGNYDASDV VLELEFEGVK EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
LSNMISFYDM ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD
YAQLLEDMQN AFRSLED
