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   27-MAR-2024, entry version 166.
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 T2D 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: Type 2 diabetes mellitus (T2D) [MIM:125853]: A multifactorial
CC       disorder of glucose homeostasis caused by a lack of sensitivity to the
CC       body's own insulin. Affected individuals usually have an obese body
CC       habitus and manifestations of a metabolic syndrome characterized by
CC       diabetes, insulin resistance, hypertension and hypertriglyceridemia.
CC       The disease results in long-term complications that affect the eyes,
CC       kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:7926294}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 52.
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; 9606-ENSP00000284601; -.
DR   PeptideAtlas; Q16821; -.
DR   ProteomicsDB; 61080; -. [Q16821-1]
DR   ProteomicsDB; 61081; -. [Q16821-2]
DR   Antibodypedia; 45888; 146 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   AGR; HGNC:9291; -.
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; DCWELPS; -.
DR   OrthoDB; 5357390at2759; -.
DR   PhylomeDB; Q16821; -.
DR   TreeFam; TF105537; -.
DR   PathwayCommons; Q16821; -.
DR   SignaLink; Q16821; -.
DR   SIGNOR; Q16821; -.
DR   BioGRID-ORCS; 5506; 14 hits in 1149 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 66 other cell types or tissues.
DR   ExpressionAtlas; Q16821; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd22255; PBD_PPP1R3A; 1.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   PANTHER; PTHR12307; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR12307:SF2; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 3A; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
DR   Genevisible; Q16821; HS.
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 (probable risk factor for 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 T2D; 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
//