ATP4A_MOUSE
ID ATP4A_MOUSE Reviewed; 1034 AA.
AC Q64436; E9QNX7; Q9CV46;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Potassium-transporting ATPase alpha chain 1;
DE EC=7.2.2.19 {ECO:0000269|PubMed:7762614};
DE AltName: Full=Gastric H(+)/K(+) ATPase subunit alpha {ECO:0000303|PubMed:10764766};
DE AltName: Full=Proton pump;
GN Name=Atp4a {ECO:0000312|MGI:MGI:88113};
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=BALB/cJ; TISSUE=Gastric mucosa;
RX PubMed=7762614; DOI=10.1152/ajpcell.1995.268.5.c1207;
RA Mathews P.M., Claeys D., Jaisser F., Geering K., Horisberger J.-D.,
RA Kraehenbuhl J.-P., Rossier B.C.;
RT "Primary structure and functional expression of the mouse and frog alpha-
RT subunit of the gastric H(+)-K(+)-ATPase.";
RL Am. J. Physiol. 268:C1207-C1214(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 223-250; 370-387; 487-497; 623-635; 660-668 AND
RP 777-784, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1034.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10764766; DOI=10.1074/jbc.m001558200;
RA Spicer Z., Miller M.L., Andringa A., Riddle T.M., Duffy J.J.,
RA Doetschman T., Shull G.E.;
RT "Stomachs of mice lacking the gastric H,K-ATPase alpha -subunit have
RT achlorhydria, abnormal parietal cells, and ciliated metaplasia.";
RL J. Biol. Chem. 275:21555-21565(2000).
CC -!- FUNCTION: The catalytic subunit of the gastric H(+)/K(+) ATPase pump
CC which transports H(+) ions in exchange for K(+) ions across the apical
CC membrane of parietal cells (PubMed:7762614). Uses ATP as an energy
CC source to pump H(+) ions to the gastric lumen while transporting K(+)
CC ion from the lumen into the cell (PubMed:7762614). Remarkably generates
CC a million-fold proton gradient across the gastric parietal cell
CC membrane, acidifying the gastric juice down to pH 1 (PubMed:10764766).
CC Within a transport cycle, the transfer of a H(+) ion across the
CC membrane is coupled to ATP hydrolysis and is associated with a
CC transient phosphorylation that shifts the pump conformation from
CC inward-facing (E1) to outward-facing state (E2). The release of the
CC H(+) ion in the stomach lumen is followed by binding of K(+) ion
CC converting the pump conformation back to the E1 state (PubMed:7762614)
CC (By similarity). {ECO:0000250|UniProtKB:P19156,
CC ECO:0000269|PubMed:10764766, ECO:0000269|PubMed:7762614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) +
CC K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
CC Evidence={ECO:0000269|PubMed:7762614};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
CC Evidence={ECO:0000305|PubMed:7762614};
CC -!- SUBUNIT: The gastric H(+)/K(+) ATPase pump is composed of the catalytic
CC alpha subunit ATP4A and the regulatory beta subunit ATP4B. Interacts
CC (via the P-domain) with ATP4B (via N-terminus); this interaction
CC stabilizes the lumenal-open E2 conformation state and prevents the
CC reverse reaction of the transport cycle.
CC {ECO:0000250|UniProtKB:P19156}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized in the apical canalicular membrane of
CC parietal cells (By similarity). Localized in the apical canalicular
CC membrane of parietal cells (By similarity).
CC {ECO:0000250|UniProtKB:P20648}.
CC -!- TISSUE SPECIFICITY: Expressed in parietal cells (at protein level).
CC {ECO:0000269|PubMed:10764766}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate. They develop achlorhydria, hypergastrinemia and ciliated
CC metaplasia. The parietal cell viability or chief cell differentiation
CC are normal when compared to wild-type littermates. Mutant parietal
CC cells have abnormal morphology characterized by dilated canaliculi with
CC few microvilli, spherical vesicles rather than normal tubulovesicles
CC and enlarged mitochondria filled with concentric cristae.
CC {ECO:0000269|PubMed:10764766}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; U17282; AAA79514.1; -; mRNA.
DR EMBL; JH584274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK009676; BAB26432.1; -; mRNA.
DR CCDS; CCDS71932.1; -.
DR PIR; I49143; I49143.
DR RefSeq; NP_001277556.1; NM_001290627.1.
DR AlphaFoldDB; Q64436; -.
DR SMR; Q64436; -.
DR ComplexPortal; CPX-3075; Hydrogen:potassium-exchanging ATPase complex.
DR IntAct; Q64436; 1.
DR MINT; Q64436; -.
DR STRING; 10090.ENSMUSP00000005692; -.
DR iPTMnet; Q64436; -.
DR PhosphoSitePlus; Q64436; -.
DR jPOST; Q64436; -.
DR MaxQB; Q64436; -.
DR PaxDb; Q64436; -.
DR PRIDE; Q64436; -.
DR ProteomicsDB; 265166; -.
DR ProteomicsDB; 314823; -.
DR Antibodypedia; 48214; 43 antibodies from 12 providers.
DR DNASU; 11944; -.
DR Ensembl; ENSMUST00000005692; ENSMUSP00000005692; ENSMUSG00000005553.
DR GeneID; 11944; -.
DR KEGG; mmu:11944; -.
DR CTD; 495; -.
DR MGI; MGI:88113; Atp4a.
DR VEuPathDB; HostDB:ENSMUSG00000005553; -.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000160297; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; Q64436; -.
DR OMA; FGIDDYI; -.
DR OrthoDB; 388324at2759; -.
DR TreeFam; TF312838; -.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11944; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q64436; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q64436; protein.
DR Bgee; ENSMUSG00000005553; Expressed in epithelium of stomach and 68 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; IDA:MGI.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0045851; P:pH reduction; IDA:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0010155; P:regulation of proton transport; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR015127; ATPase_P-typ_H/K-transp_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF09040; H-K_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1034
FT /note="Potassium-transporting ATPase alpha chain 1"
FT /id="PRO_0000046254"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..141
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 803..812
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..928
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 949..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..996
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1018..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 14..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 339
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 340
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 342
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 344
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 821
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50993"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09626"
FT MOD_RES 953
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="Missing (in Ref. 1; AAA79514)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="N -> K (in Ref. 1; AAA79514)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="I -> T (in Ref. 1; AAA79514)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="S -> F (in Ref. 4; BAB26432)"
FT /evidence="ECO:0000305"
FT CONFLICT 1031..1032
FT /note="EL -> DF (in Ref. 1; AAA79514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1034 AA; 114065 MW; 39AD71FAFEC4AD42 CRC64;
MGKAENYELY SVELGSGPGG DMTAKMSKKK AGGGGGKKKE KLENMKKEME INDHQLSVSE
LEQKYQTSAT KGLKASLAAE LLLRDGPNAL RPPRGTPEYV KFARQLAGGL QCLMWVAAAI
CLIAFAIQAS EGDLTTDDNL YLAVALIAVV VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT
VIRDGDKFQI NADQLVVGDL VEMKGGDRVP ADIRILSAQG CKVDNSSLTG ESEPQTRSPE
CTHESPLETR NIAFFSTMCL EGTAQGLVVS TGDRTIIGRI ASLASGVENE KTPIAIEIEH
FVDIIAGLAI LFGATFFVVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV TVCLSLTAKR
LASKNCVVKN LEAVETLGST SVICSDKTGT LTQNRMTVSH LWFDNHIHTA DTTEDQSGQT
FDQSSETWRA LCRVLTLCNR AAFKSGQDAV PVPKRIVIGD ASETALLKFS ELTLGNAMGY
RDRFPKVCEI PFNSINKFQL SIHTLEDPRD SRHLLVMKGA PERVLERCSS ILIKGQELPL
DEQWREAFQT AYLSLGGLGE RVLGFCQLYL NEKDYPPGYA FDVEAMNFPS SGLCFAGLVS
MIDPPRATVP DAVLKCRTAG IRVIMVTGDH PITAKAIAAS VGIISEGSET VEDIAARLRM
PVDQVNRKDA RACVINGMQL KDMDPSELVE ALRTHPEMVF ARTSPQQKLV IVESCQRLGA
IVAVTGDGVN DSPALKKADI GVAMGIAGSD AAKNAADMIL LDDNFASIVT GVEQGRLIFD
NLKKSIAYTL TKNIPELTPY LIYITVSVPL PLGCITILFI ELCTDIFPSV SLAYEKAESD
IMHLRPRNPK RDRLVNEPLA AYSYFQIGAI QSFAGFADYF TAMAQEGWFP LLCVGLRPQW
EDHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR RLSVFQQGFF
RNKILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRFQWWL VPMPFGLLIF VYDEIRKLGV
RCCPGSWWDQ ELYY
