PPR3A_HUMAN
ID PPR3A_HUMAN Reviewed; 1122 AA.
AC Q16821; A0AVQ2; A4D0T6; O43476; Q75LN8; Q7KYM8; Q86UI6;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3A;
DE AltName: Full=Protein phosphatase 1 glycogen-associated regulatory subunit;
DE AltName: Full=Protein phosphatase type-1 glycogen targeting subunit;
DE Short=RG1;
GN Name=PPP1R3A; Synonyms=PP1G;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY, AND VARIANTS MET-451; LYS-476; HIS-882; SER-883 AND TYR-905.
RC TISSUE=Skeletal muscle;
RX PubMed=9726244; DOI=10.2337/diabetes.47.9.1519;
RA Xia J., Scherer S.W., Cohen P.T.W., Majer M., Xi T., Norman R.A.,
RA Knowler W.C., Bogardus C., Prochazka M.;
RT "A common variant in PPP1R3 associated with insulin resistance and type 2
RT diabetes.";
RL Diabetes 47:1519-1524(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS MET-451;
RP LYS-476 AND HIS-882.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-451;
RP LYS-476 AND HIS-882.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 2-1122 (ISOFORM 1), VARIANTS MET-451; LYS-476
RP AND HIS-882, AND VARIANT NIDDM GLU-931.
RC TISSUE=Skeletal muscle;
RX PubMed=7926294; DOI=10.2337/diabetes.43.10.1234;
RA Chen Y.H., Hansen L., Chen M.X., Bjorbaek C., Vestergaard H., Hansen T.,
RA Cohen P.T.W., Pederson O.;
RT "Sequence of the human glycogen-associated regulatory subunit of type I
RT protein phosphatase and analysis of its coding region and mRNA level in
RT muscle from patients with non-insulin-dependent diabetes.";
RL Diabetes 43:1234-1241(1994).
RN [6]
RP VARIANT TYR-905.
RX PubMed=7581368; DOI=10.1093/hmg/4.8.1313;
RA Hansen L., Hansen T., Vestergaard H., Bjorbaek C., Echwald S.M.,
RA Clausen J.O., Chen Y.H., Chen M.X., Cohen P.T.W., Pedersen O.;
RT "A widespread amino acid polymorphism at codon 905 of the glycogen-
RT associated regulatory subunit of protein phosphatase-1 is associated with
RT insulin resistance and hypersecretion of insulin.";
RL Hum. Mol. Genet. 4:1313-1320(1995).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-554.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis. Plays
CC an important role in glycogen synthesis but is not essential for
CC insulin activation of glycogen synthase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and associates
CC with glycogen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16821-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16821-2; Sequence=VSP_011585, VSP_011586;
CC -!- TISSUE SPECIFICITY: Skeletal muscle and heart.
CC {ECO:0000269|PubMed:9726244}.
CC -!- DOMAIN: The CBM21 domain is known to be involved in the localization to
CC glycogen and is characteristic of some regulatory subunit of
CC phosphatase complexes.
CC -!- PTM: Phosphorylation at Ser-46 by ISPK stimulates the dephosphorylation
CC of glycogen synthase and phosphorylase kinase. {ECO:0000250}.
CC -!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]:
CC A multifactorial disorder of glucose homeostasis caused by a lack of
CC sensitivity to the body's own insulin. Affected individuals usually
CC have an obese body habitus and manifestations of a metabolic syndrome
CC characterized by diabetes, insulin resistance, hypertension and
CC hypertriglyceridemia. The disease results in long-term complications
CC that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:7926294}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS07492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF024578; AAB94596.1; -; Genomic_DNA.
DR EMBL; AF024576; AAB94596.1; JOINED; Genomic_DNA.
DR EMBL; AF024577; AAB94596.1; JOINED; Genomic_DNA.
DR EMBL; AF024579; AAB94597.1; -; mRNA.
DR EMBL; AC092465; AAS07492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC093598; AAP22361.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24370.1; -; Genomic_DNA.
DR EMBL; BC126451; AAI26452.1; -; mRNA.
DR EMBL; BC126453; AAI26454.1; -; mRNA.
DR EMBL; X78578; CAA55316.1; -; mRNA.
DR CCDS; CCDS5759.1; -. [Q16821-1]
DR PIR; I38127; I38127.
DR RefSeq; NP_002702.2; NM_002711.3. [Q16821-1]
DR PDB; 5ZQV; X-ray; 2.95 A; E/F/G/H=1-99.
DR PDBsum; 5ZQV; -.
DR AlphaFoldDB; Q16821; -.
DR SMR; Q16821; -.
DR BioGRID; 111499; 51.
DR IntAct; Q16821; 2.
DR STRING; 9606.ENSP00000284601; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q16821; -.
DR PhosphoSitePlus; Q16821; -.
DR BioMuta; PPP1R3A; -.
DR DMDM; 298286906; -.
DR EPD; Q16821; -.
DR MassIVE; Q16821; -.
DR PaxDb; Q16821; -.
DR PeptideAtlas; Q16821; -.
DR PRIDE; Q16821; -.
DR ProteomicsDB; 61080; -. [Q16821-1]
DR ProteomicsDB; 61081; -. [Q16821-2]
DR Antibodypedia; 45888; 133 antibodies from 23 providers.
DR DNASU; 5506; -.
DR Ensembl; ENST00000284601.4; ENSP00000284601.3; ENSG00000154415.8. [Q16821-1]
DR Ensembl; ENST00000284602.1; ENSP00000284602.1; ENSG00000154415.8. [Q16821-2]
DR GeneID; 5506; -.
DR KEGG; hsa:5506; -.
DR MANE-Select; ENST00000284601.4; ENSP00000284601.3; NM_002711.4; NP_002702.2.
DR UCSC; uc010ljy.2; human. [Q16821-1]
DR CTD; 5506; -.
DR DisGeNET; 5506; -.
DR GeneCards; PPP1R3A; -.
DR HGNC; HGNC:9291; PPP1R3A.
DR HPA; ENSG00000154415; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; PPP1R3A; -.
DR MIM; 125853; phenotype.
DR MIM; 600917; gene.
DR neXtProt; NX_Q16821; -.
DR OpenTargets; ENSG00000154415; -.
DR PharmGKB; PA33651; -.
DR VEuPathDB; HostDB:ENSG00000154415; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000157682; -.
DR HOGENOM; CLU_009399_0_0_1; -.
DR InParanoid; Q16821; -.
DR OMA; TFKPGFS; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q16821; -.
DR TreeFam; TF105537; -.
DR PathwayCommons; Q16821; -.
DR SignaLink; Q16821; -.
DR SIGNOR; Q16821; -.
DR BioGRID-ORCS; 5506; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; PPP1R3A; human.
DR GeneWiki; PPP1R3A; -.
DR GenomeRNAi; 5506; -.
DR Pharos; Q16821; Tbio.
DR PRO; PR:Q16821; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16821; protein.
DR Bgee; ENSG00000154415; Expressed in skeletal muscle tissue of rectus abdominis and 65 other tissues.
DR ExpressionAtlas; Q16821; baseline and differential.
DR Genevisible; Q16821; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR Pfam; PF03370; CBM_21; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Diabetes mellitus; Disease variant; Glycogen metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1122
FT /note="Protein phosphatase 1 regulatory subunit 3A"
FT /id="PRO_0000071500"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 122..230
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 32..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..65
FT /note="PP1-binding motif"
FT COMPBIAS 35..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:Q00756"
FT MOD_RES 42
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:Q00756"
FT MOD_RES 46
FT /note="Phosphoserine; by PKA and ISPK"
FT /evidence="ECO:0000250|UniProtKB:Q00756"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT MOD_RES 65
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q00756"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR9"
FT VAR_SEQ 60..74
FT /note="GTRRVSFADSFGFNL -> ERTRAGACKTMERSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9726244"
FT /id="VSP_011585"
FT VAR_SEQ 75..1122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9726244"
FT /id="VSP_011586"
FT VARIANT 45
FT /note="G -> S (in dbSNP:rs8192687)"
FT /id="VAR_027929"
FT VARIANT 231
FT /note="C -> Y (in dbSNP:rs7801819)"
FT /id="VAR_027930"
FT VARIANT 451
FT /note="V -> M (in dbSNP:rs2974942)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7926294,
FT ECO:0000269|PubMed:9726244"
FT /id="VAR_027931"
FT VARIANT 476
FT /note="N -> K (in dbSNP:rs2974944)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7926294,
FT ECO:0000269|PubMed:9726244"
FT /id="VAR_027932"
FT VARIANT 554
FT /note="G -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036287"
FT VARIANT 627
FT /note="R -> K (in dbSNP:rs35067467)"
FT /id="VAR_057128"
FT VARIANT 748
FT /note="E -> K (in dbSNP:rs4304271)"
FT /id="VAR_027933"
FT VARIANT 882
FT /note="L -> H (in dbSNP:rs2974938)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7926294,
FT ECO:0000269|PubMed:9726244"
FT /id="VAR_027934"
FT VARIANT 883
FT /note="R -> S (in dbSNP:rs1800000)"
FT /evidence="ECO:0000269|PubMed:9726244"
FT /id="VAR_019697"
FT VARIANT 905
FT /note="D -> Y (can be associated with insulin resistance;
FT dbSNP:rs1799999)"
FT /evidence="ECO:0000269|PubMed:7581368,
FT ECO:0000269|PubMed:9726244"
FT /id="VAR_019698"
FT VARIANT 931
FT /note="A -> E (in NIDDM; dbSNP:rs35449651)"
FT /evidence="ECO:0000269|PubMed:7926294"
FT /id="VAR_019699"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:5ZQV"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5ZQV"
SQ SEQUENCE 1122 AA; 125767 MW; FACB2CEA7C00E75B CRC64;
MEPSEVPSQI SKDNFLEVPN LSDSLCEDEE VTFQPGFSPQ PSRRGSDSSE DIYLDTPSSG
TRRVSFADSF GFNLVSVKEF DCWELPSAST TFDLGTDIFH TEEYVLAPLF DLPSSKEDLM
QQLQIQKAIL ESTESLLGST SIKGIIRVLN VSFEKLVYVR MSLDDWQTHY DILAEYVPNS
CDGETDQFSF KIVLVPPYQK DGSKVEFCIR YETSVGTFWS NNNGTNYTFI CQKKEQEPEP
VKPWKEVPNR QIKGCLKVKS SKEESSVTSE ENNFENPKNT DTYIPTIICS HEDKEDLEAS
NRNVKDVNRE HDEHNEKELE LMINQHLIRT RSTASRDERN TFSTDPVNFP NKAEGLEKKQ
IHGEICTDLF QRSLSPSSSA ESSVKGDFYC NEKYSSGDDC THQPSEETTS NMGEIKPSLG
DTSSDELVQL HTGSKEVLDD NANPAHGNGT VQIPCPSSDQ LMAGNLNKKH EGGAKNIEVK
DLGCLRRDFH SDTSACLKES TEEGSSKEDY YGNGKDDEEQ RIYLGVNEKQ RKNFQTILHD
QERKMGNPKI SVAGIGASNR DLATLLSEHT AIPTRAITAD VSHSPRTNLS WEEAVLTPEH
HHLTSEGSAL GGITGQVCSS RTGNVLRNDY LFQVEEKSGG INSEDQDNSP QHKQSWNVLE
SQGKSRENKT NITEHIKGQT DCEDVWGKRD NTRSLKATTE ELFTCQETVC CELSSLADHG
ITEKAEAGTA YIIKTTSEST PESMSAREKA IIAKLPQETA RSDRPIEVKE TAFDPHEGRN
DDSHYTLCQR DTVGVIYDND FEKESRLGIC NVRVDEMEKE ETMSMYNPRK THDREKCGTG
NITSVEESSW VITEYQKATS KLDLQLGMLP TDKTVFSENR DLRQVQELSK KTDSDAIVHS
AFNSDTNRAP QNSSPFSKHH TEISVSTNEQ AIAVENAVTT MASQPISTKS ENICNSTREI
QGIEKHPYPE SKPEEVSRSS GIVTSGSRKE RCIGQIFQTE EYSVEKSLGP MILINKPLEN
MEEARHENEG LVSSGQSLYT SGEKESDSSA STSLPVEESQ AQGNESLFSK YTNSKIPYFL
LFLIFLITVY HYDLMIGLTF YVLSLSWLSW EEGRQKESVK KK
