ID   P2R3A_HUMAN             Reviewed;        1150 AA.
AC   Q06190; A8KAE7; B4DNU1; B7ZAE3; Q06189; Q9NPQ5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha;
DE   AltName: Full=PP2A subunit B isoform PR72/PR130;
DE   AltName: Full=PP2A subunit B isoform R3 isoform;
DE   AltName: Full=PP2A subunit B isoforms B''-PR72/PR130;
DE   AltName: Full=PP2A subunit B isoforms B72/B130;
DE   AltName: Full=Serine/threonine-protein phosphatase 2A 72/130 kDa regulatory subunit B;
GN   Name=PPP2R3A; Synonyms=PPP2R3;
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 [MRNA] (ISOFORMS PR72 AND PR130), PARTIAL PROTEIN
RP   SEQUENCE, AND ALTERNATIVE SPLICING.
RC   TISSUE=Fetal brain;
RX   PubMed=8392071; DOI=10.1016/s0021-9258(18)82465-6;
RA   Hendrix P., Mayer-Jaekel R.E., Cron P., Goris J., Hofsteenge J.,
RA   Merlevede W., Hemmings B.A.;
RT   "Structure and expression of a 72-kDa regulatory subunit of protein
RT   phosphatase 2A. Evidence for different size forms produced by alternative
RT   splicing.";
RL   J. Biol. Chem. 268:15267-15276(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PR72; PR130 AND 3).
RC   TISSUE=Lung, Tongue, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 768-1150.
RG   The European IMAGE consortium;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC       and catalytic activity, and also might direct the localization of the
CC       catalytic enzyme to a particular subcellular compartment.
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC       of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC       regulatory subunit (PR65 or subunit A), that associates with a variety
CC       of regulatory subunits. Proteins that associate with the core dimer
CC       include three families of regulatory subunits B (the R2/B/PR55/B55,
CC       R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC       regulatory subunit, viral proteins, and cell signaling molecules.
CC   -!- INTERACTION:
CC       Q06190-1; Q969G9: NKD1; NbExp=4; IntAct=EBI-949204, EBI-1538217;
CC       Q06190-2; Q969G9: NKD1; NbExp=3; IntAct=EBI-949210, EBI-1538217;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=PR130; Synonyms=130 kDa;
CC         IsoId=Q06190-1; Sequence=Displayed;
CC       Name=PR72; Synonyms=72 kDa;
CC         IsoId=Q06190-2; Sequence=VSP_005107, VSP_005108;
CC       Name=3;
CC         IsoId=Q06190-3; Sequence=VSP_045203;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, muscle
CC       and kidney.
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DR   EMBL; L07590; AAB02613.1; -; mRNA.
DR   EMBL; L12146; AAB02614.1; -; mRNA.
DR   EMBL; AK293012; BAF85701.1; -; mRNA.
DR   EMBL; AK298059; BAG60353.1; -; mRNA.
DR   EMBL; AK316258; BAH14629.1; -; mRNA.
DR   EMBL; AC072039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79122.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79123.1; -; Genomic_DNA.
DR   EMBL; AL389975; CAB97532.1; -; mRNA.
DR   CCDS; CCDS3087.1; -. [Q06190-1]
DR   CCDS; CCDS3088.1; -. [Q06190-2]
DR   CCDS; CCDS54642.1; -. [Q06190-3]
DR   PIR; A47114; A47114.
DR   PIR; B47114; B47114.
DR   RefSeq; NP_001177376.1; NM_001190447.1. [Q06190-3]
DR   RefSeq; NP_002709.2; NM_002718.4. [Q06190-1]
DR   RefSeq; NP_871626.1; NM_181897.2. [Q06190-2]
DR   RefSeq; XP_006713749.1; XM_006713686.3. [Q06190-1]
DR   RefSeq; XP_011511258.1; XM_011512956.2. [Q06190-1]
DR   PDB; 4I5J; X-ray; 2.09 A; A=786-1070.
DR   PDB; 4I5K; X-ray; 2.90 A; A/B=786-1070.
DR   PDBsum; 4I5J; -.
DR   PDBsum; 4I5K; -.
DR   AlphaFoldDB; Q06190; -.
DR   SMR; Q06190; -.
DR   BioGRID; 111515; 51.
DR   CORUM; Q06190; -.
DR   DIP; DIP-29397N; -.
DR   IntAct; Q06190; 25.
DR   MINT; Q06190; -.
DR   STRING; 9606.ENSP00000264977; -.
DR   iPTMnet; Q06190; -.
DR   PhosphoSitePlus; Q06190; -.
DR   BioMuta; PPP2R3A; -.
DR   DMDM; 543720; -.
DR   EPD; Q06190; -.
DR   jPOST; Q06190; -.
DR   MassIVE; Q06190; -.
DR   MaxQB; Q06190; -.
DR   PaxDb; 9606-ENSP00000264977; -.
DR   PeptideAtlas; Q06190; -.
DR   ProteomicsDB; 4724; -.
DR   ProteomicsDB; 58420; -. [Q06190-1]
DR   ProteomicsDB; 58421; -. [Q06190-2]
DR   Pumba; Q06190; -.
DR   Antibodypedia; 33406; 263 antibodies from 30 providers.
DR   DNASU; 5523; -.
DR   Ensembl; ENST00000264977.8; ENSP00000264977.3; ENSG00000073711.11. [Q06190-1]
DR   Ensembl; ENST00000334546.6; ENSP00000334748.2; ENSG00000073711.11. [Q06190-2]
DR   Ensembl; ENST00000490467.5; ENSP00000419344.1; ENSG00000073711.11. [Q06190-3]
DR   GeneID; 5523; -.
DR   KEGG; hsa:5523; -.
DR   MANE-Select; ENST00000264977.8; ENSP00000264977.3; NM_002718.5; NP_002709.2.
DR   UCSC; uc003eqv.3; human. [Q06190-1]
DR   AGR; HGNC:9307; -.
DR   CTD; 5523; -.
DR   DisGeNET; 5523; -.
DR   GeneCards; PPP2R3A; -.
DR   HGNC; HGNC:9307; PPP2R3A.
DR   HPA; ENSG00000073711; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MIM; 604944; gene.
DR   neXtProt; NX_Q06190; -.
DR   OpenTargets; ENSG00000073711; -.
DR   PharmGKB; PA35523; -.
DR   VEuPathDB; HostDB:ENSG00000073711; -.
DR   eggNOG; KOG2562; Eukaryota.
DR   GeneTree; ENSGT00940000154659; -.
DR   HOGENOM; CLU_276803_0_0_1; -.
DR   InParanoid; Q06190; -.
DR   OMA; VQKPASH; -.
DR   OrthoDB; 918215at2759; -.
DR   PhylomeDB; Q06190; -.
DR   TreeFam; TF105554; -.
DR   PathwayCommons; Q06190; -.
DR   SignaLink; Q06190; -.
DR   BioGRID-ORCS; 5523; 11 hits in 1151 CRISPR screens.
DR   ChiTaRS; PPP2R3A; human.
DR   GeneWiki; PPP2R3A; -.
DR   GenomeRNAi; 5523; -.
DR   Pharos; Q06190; Tbio.
DR   PRO; PR:Q06190; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q06190; Protein.
DR   Bgee; ENSG00000073711; Expressed in biceps brachii and 209 other cell types or tissues.
DR   ExpressionAtlas; Q06190; baseline and differential.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR   GO; GO:0001754; P:eye photoreceptor cell differentiation; IGI:BHF-UCL.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:BHF-UCL.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:BHF-UCL.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0090249; P:regulation of cell migration involved in somitogenic axis elongation; IGI:BHF-UCL.
DR   GO; GO:0007525; P:somatic muscle development; IGI:BHF-UCL.
DR   GO; GO:0061053; P:somite development; ISS:BHF-UCL.
DR   GO; GO:0001756; P:somitogenesis; IGI:BHF-UCL.
DR   CDD; cd21506; PPP2R3A; 1.
DR   Gene3D; 1.10.238.220; -; 1.
DR   Gene3D; 1.10.238.230; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR041534; EF-hand_13.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR048855; P2R3A_B_D_EF-hand.
DR   PANTHER; PTHR14095; PHOSPHATASE 2A REGULATORY SUBUNIT-RELATED; 1.
DR   PANTHER; PTHR14095:SF3; SERINE_THREONINE-PROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT B'' SUBUNIT ALPHA; 1.
DR   Pfam; PF17958; EF-hand_13; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF21161; P2R3B_EF-hand; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   Genevisible; Q06190; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW   Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..1150
FT                   /note="Serine/threonine-protein phosphatase 2A regulatory
FT                   subunit B"" subunit alpha"
FT                   /id="PRO_0000071443"
FT   DOMAIN          758..793
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          972..1007
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          661..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..692
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         985
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         987
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         989
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         996
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VAR_SEQ         1..736
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045203"
FT   VAR_SEQ         1..621
FT                   /note="Missing (in isoform PR72)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:8392071"
FT                   /id="VSP_005107"
FT   VAR_SEQ         622..665
FT                   /note="MQILQETLTTSSQANLSVCRSPVGDKAKDTTSAVLIQQTPEVIK -> MMIK
FT                   ETSLRRDPDLRGELAFLARGCDFVLPSRFKKRLKSFQQTQ (in isoform PR72)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:8392071"
FT                   /id="VSP_005108"
FT   VARIANT         67
FT                   /note="D -> G (in dbSNP:rs9814557)"
FT                   /id="VAR_051739"
FT   VARIANT         67
FT                   /note="D -> N (in dbSNP:rs57374999)"
FT                   /id="VAR_061760"
FT   VARIANT         108
FT                   /note="N -> S (in dbSNP:rs36020282)"
FT                   /id="VAR_051740"
FT   VARIANT         171
FT                   /note="A -> S (in dbSNP:rs6779903)"
FT                   /id="VAR_051741"
FT   VARIANT         481
FT                   /note="P -> A (in dbSNP:rs34901937)"
FT                   /id="VAR_051742"
FT   VARIANT         642
FT                   /note="S -> G (in dbSNP:rs17197552)"
FT                   /id="VAR_051743"
FT   VARIANT         695
FT                   /note="P -> L (in dbSNP:rs9826032)"
FT                   /id="VAR_051744"
FT   VARIANT         745
FT                   /note="D -> N (in dbSNP:rs16843645)"
FT                   /id="VAR_022095"
FT   HELIX           797..805
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   STRAND          811..813
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           815..818
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           819..828
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   TURN            830..832
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           833..837
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           839..857
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   STRAND          861..863
FT                   /evidence="ECO:0007829|PDB:4I5K"
FT   HELIX           867..871
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           875..882
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           888..890
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   TURN            892..895
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           897..910
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   STRAND          915..919
FT                   /evidence="ECO:0007829|PDB:4I5K"
FT   HELIX           920..923
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   TURN            924..929
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           933..939
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   TURN            940..944
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           958..969
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           974..984
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   STRAND          989..992
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           994..1010
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           1018..1029
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           1039..1045
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           1048..1056
FT                   /evidence="ECO:0007829|PDB:4I5J"
FT   HELIX           1058..1062
FT                   /evidence="ECO:0007829|PDB:4I5J"
SQ   SEQUENCE   1150 AA;  130278 MW;  97A31BA4206518A3 CRC64;
     MAATYRLVVS TVNHYSSVVI DRRFEQAIHY CTGTCHTFTH GIDCIVVHHS VCADLLHIPV
     SQFKDADLNS MFLPHENGLS SAEGDYPQQA FTGIPRVKRG STFQNTYNLK DIAGEAISFA
     SGKIKEFSFE KLKNSNHAAY RKGRKVKSDS FNRRSVDLDL LCGHYNNDGN APSFGLLRSS
     SVEEKPLSHR NSLDTNLTSM FLQNFSEEDL VTQILEKHKI DNFSSGTDIK MCLDILLKCS
     EDLKKCTDII KQCIKKKSGS SISEGSGNDT ISSSETVYMN VMTRLASYLK KLPFEFMQSG
     NNEALDLTEL ISNMPSLQLT PFSPVFGTEQ PPKYEDVVQL SASDSGRFQT IELQNDKPNS
     RKMDTVQSIP NNSTNSLYNL EVNDPRTLKA VQVQSQSLTM NPLENVSSDD LMETLYIEEE
     SDGKKALDKG QKTENGPSHE LLKVNEHRAE FPEHATHLKK CPTPMQNEIG KIFEKSFVNL
     PKEDCKSKVS KFEEGDQRDF TNSSSQEEID KLLMDLESFS QKMETSLREP LAKGKNSNFL
     NSHSQLTGQT LVDLEPKSKV SSPIEKVSPS CLTRIIETNG HKIEEEDRAL LLRILESIED
     FAQELVECKS SRGSLSQEKE MMQILQETLT TSSQANLSVC RSPVGDKAKD TTSAVLIQQT
     PEVIKIQNKP EKKPGTPLPP PATSPSSPRP LSPVPHVNNV VNAPLSINIP RFYFPEGLPD
     TCSNHEQTLS RIETAFMDIE EQKADIYEMG KIAKVCGCPL YWKAPMFRAA GGEKTGFVTA
     QSFIAMWRKL LNNHHDDASK FICLLAKPNC SSLEQEDFIP LLQDVVDTHP GLTFLKDAPE
     FHSRYITTVI QRIFYTVNRS WSGKITSTEI RKSNFLQTLA LLEEEEDINQ ITDYFSYEHF
     YVIYCKFWEL DTDHDLYISQ ADLSRYNDQA SSSRIIERIF SGAVTRGKTI QKEGRMSYAD
     FVWFLISEED KRNPTSIEYW FRCMDVDGDG VLSMYELEYF YEEQCERMEA MGIEPLPFHD
     LLCQMLDLVK PAVDGKITLR DLKRCRMAHI FYDTFFNLEK YLDHEQRDPF AVQKDVENDG
     PEPSDWDRFA AEEYETLVAE ESAQAQFQEG FEDYETDEPA SPSEFGNKSN KILSASLPEK
     CGKLQSVDEE
//