P2R3A_HUMAN
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 03-AUG-2022, entry version 192.
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; 45.
DR CORUM; Q06190; -.
DR DIP; DIP-29397N; -.
DR IntAct; Q06190; 23.
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; Q06190; -.
DR PeptideAtlas; Q06190; -.
DR PRIDE; Q06190; -.
DR ProteomicsDB; 4724; -.
DR ProteomicsDB; 58420; -. [Q06190-1]
DR ProteomicsDB; 58421; -. [Q06190-2]
DR Antibodypedia; 33406; 240 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 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 OMA; VQKPASH; -.
DR OrthoDB; 255081at2759; -.
DR PhylomeDB; Q06190; -.
DR TreeFam; TF105554; -.
DR PathwayCommons; Q06190; -.
DR SignaLink; Q06190; -.
DR BioGRID-ORCS; 5523; 11 hits in 1073 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 207 other tissues.
DR ExpressionAtlas; Q06190; baseline and differential.
DR Genevisible; Q06190; HS.
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:0090244; P:Wnt signaling pathway involved in somitogenesis; IC:BHF-UCL.
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 Pfam; PF17958; EF-hand_13; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
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
