MYPT1_RAT
ID MYPT1_RAT Reviewed; 1032 AA.
AC Q10728; Q62937; Q9WU33;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
DE AltName: Full=MBSP;
DE AltName: Full=Myosin phosphatase-targeting subunit 1;
DE Short=Myosin phosphatase target subunit 1;
DE AltName: Full=Protein phosphatase myosin-binding subunit;
DE AltName: Full=Protein phosphatase subunit 1M;
DE Short=PP-1M;
DE AltName: Full=Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110;
GN Name=Ppp1r12a {ECO:0000312|RGD:620013}; Synonyms=Mbs, Mypt1 {ECO:0000305};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Aorta;
RX PubMed=7988720; DOI=10.1016/0014-5793(94)01231-8;
RA Chen Y.H., Chen M.X., Alessi D.R., Campbell D.G., Shanahan C., Cohen P.,
RA Cohen P.T.W.;
RT "Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory
RT subunits of smooth muscle protein phosphatase 1M.";
RL FEBS Lett. 356:51-55(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-728 (ISOFORM 2), AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=8543033; DOI=10.1016/0014-5793(95)01318-0;
RA Haystead C.M.M., Gailly P., Somlyo A.P., Somlyo A.V., Haystead T.A.J.;
RT "Molecular cloning and functional expression of a recombinant 72.5 kDa
RT fragment of the 110 kDa regulatory subunit of smooth muscle protein
RT phosphatase 1M.";
RL FEBS Lett. 377:123-127(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-665 (ISOFORM 1), TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley;
RX PubMed=10712248; DOI=10.1152/ajpcell.2000.278.3.c589;
RA Dirksen W.P., Vladic F., Fisher S.A.;
RT "A myosin phosphatase targeting subunit isoform transition defines a smooth
RT muscle developmental phenotypic switch.";
RL Am. J. Physiol. 278:C589-C600(2000).
RN [4]
RP PHOSPHORYLATION, AND INTERACTION WITH ARHA AND CIT.
RX PubMed=8662509; DOI=10.1126/science.273.5272.245;
RA Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M.,
RA Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
RT "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-
RT kinase).";
RL Science 273:245-248(1996).
RN [5]
RP PHOSPHORYLATION AT THR-697 AND SER-854, AND INTERACTION WITH ROCK1.
RX PubMed=10579722; DOI=10.1083/jcb.147.5.1023;
RA Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M.,
RA Matsumura F., Inagaki M., Kaibuchi K.;
RT "Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by
RT Rho-kinase in vivo.";
RL J. Cell Biol. 147:1023-1038(1999).
RN [6]
RP PHOSPHORYLATION AT THR-697 BY ZIPK/DAPK3.
RX PubMed=11384979; DOI=10.1074/jbc.m102753200;
RA Niiro N., Ikebe M.;
RT "Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle
RT contraction via myosin light chain phosphorylation.";
RL J. Biol. Chem. 276:29567-29574(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-997, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [8]
RP PHOSPHORYLATION, AND INTERACTION WITH ROCK1 AND ROCK2.
RX PubMed=19131646; DOI=10.1161/circresaha.108.188524;
RA Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K.;
RT "ROCK isoform regulation of myosin phosphatase and contractility in
RT vascular smooth muscle cells.";
RL Circ. Res. 104:531-540(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-445; SER-507;
RP SER-864; SER-873; SER-912 AND SER-997, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates
CC binding to myosin. As part of the PPP1C complex, involved in
CC dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent
CC suppression of HIF1A activity (By similarity).
CC {ECO:0000250|UniProtKB:O14974, ECO:0000269|PubMed:8543033}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12A mediates
CC binding to myosin. Interacts with ARHA and CIT (By similarity). Binds
CC PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent
CC dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with
CC SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is
CC direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910)
CC with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1
CC and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN
CC (By similarity). Interacts with NCKAP1L (By similarity).
CC {ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q9DBR7}.
CC -!- INTERACTION:
CC Q10728; O43293-2: DAPK3; Xeno; NbExp=2; IntAct=EBI-918263, EBI-9691390;
CC Q10728; Q6WCQ1: MPRIP; Xeno; NbExp=6; IntAct=EBI-918263, EBI-1022605;
CC Q10728; P35240: NF2; Xeno; NbExp=2; IntAct=EBI-918263, EBI-1014472;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}.
CC Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q10728-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q10728-2; Sequence=VSP_009254;
CC Name=3;
CC IsoId=Q10728-3; Sequence=VSP_009255;
CC -!- TISSUE SPECIFICITY: Smooth muscle. Detected in aorta, portal vein,
CC stomach, intestine, bladder and lung. {ECO:0000269|PubMed:10712248}.
CC -!- DOMAIN: Heterotetramerization is mediated by the interaction between a
CC coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS,
CC the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.
CC -!- DOMAIN: The KVKF motif mediates interaction with PPP1CB.
CC {ECO:0000250|UniProtKB:O14974}.
CC -!- PTM: Phosphorylated on upon DNA damage, probably by ATM or ATR (By
CC similarity). Phosphorylated by CIT (Rho-associated kinase).
CC Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697. In vitro,
CC phosphorylation of Ser-696 by PKA and PKG appears to prevent
CC phosphorylation of the inhibitory site Thr-697, probably mediated by
CC PRKG1 (By similarity). Phosphorylated on upon DNA damage, probably by
CC ATM or ATR (By similarity). Phosphorylated by CIT (Rho-associated
CC kinase). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697.
CC May be phosphorylated at Thr-697 by DMPK; may inhibit the myosin
CC phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis,
CC creating docking sites for the POLO box domains of PLK1. Subsequently,
CC PLK1 binds and phosphorylates PPP1R12A (By similarity).
CC {ECO:0000250|UniProtKB:O14974}.
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DR EMBL; S74907; AAB32731.1; -; mRNA.
DR EMBL; U50185; AAA92961.1; -; mRNA.
DR EMBL; AF110176; AAD34326.1; -; Genomic_DNA.
DR PIR; S68418; S68418.
DR RefSeq; NP_446342.1; NM_053890.1. [Q10728-3]
DR RefSeq; XP_006241377.1; XM_006241315.2. [Q10728-2]
DR AlphaFoldDB; Q10728; -.
DR BMRB; Q10728; -.
DR SMR; Q10728; -.
DR IntAct; Q10728; 5.
DR MINT; Q10728; -.
DR STRING; 10116.ENSRNOP00000006773; -.
DR iPTMnet; Q10728; -.
DR PhosphoSitePlus; Q10728; -.
DR jPOST; Q10728; -.
DR PaxDb; Q10728; -.
DR PRIDE; Q10728; -.
DR Ensembl; ENSRNOT00000041473; ENSRNOP00000045260; ENSRNOG00000004925. [Q10728-2]
DR GeneID; 116670; -.
DR KEGG; rno:116670; -.
DR UCSC; RGD:620013; rat. [Q10728-1]
DR CTD; 4659; -.
DR RGD; 620013; Ppp1r12a.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000156120; -.
DR InParanoid; Q10728; -.
DR OrthoDB; 477969at2759; -.
DR PhylomeDB; Q10728; -.
DR BRENDA; 3.1.3.53; 5301.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q10728; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0031672; C:A band; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0019208; F:phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0035508; P:positive regulation of myosin-light-chain-phosphatase activity; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1032
FT /note="Protein phosphatase 1 regulatory subunit 12A"
FT /id="PRO_0000067027"
FT REPEAT 39..68
FT /note="ANK 1"
FT REPEAT 72..101
FT /note="ANK 2"
FT REPEAT 105..134
FT /note="ANK 3"
FT REPEAT 138..164
FT /note="ANK 4"
FT REPEAT 198..227
FT /note="ANK 5"
FT REPEAT 231..260
FT /note="ANK 6"
FT REGION 290..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..866
FT /note="Interaction with ROCK2"
FT /evidence="ECO:0000269|PubMed:19131646"
FT MOTIF 35..38
FT /note="KVKF motif"
FT COMPBIAS 303..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 446
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 472
FT /note="Phosphoserine; by NUAK1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 473
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 693
FT /note="Phosphoserine; by PKA and PKG; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 696
FT /note="Phosphoserine; by PKA and PKG; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 697
FT /note="Phosphothreonine; by ROCK1, ROCK2, CDC42BP,
FT ZIPK/DAPK3 and RAF1"
FT /evidence="ECO:0000269|PubMed:10579722,
FT ECO:0000269|PubMed:11384979"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR7"
FT MOD_RES 854
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000269|PubMed:10579722"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 912
FT /note="Phosphoserine; by NUAK1"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:22673903"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT VAR_SEQ 552..607
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7988720"
FT /id="VSP_009255"
FT VAR_SEQ 608..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8543033"
FT /id="VSP_009254"
FT CONFLICT 11
FT /note="N -> R (in Ref. 2; AAA92961)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="T -> N (in Ref. 2; AAA92961)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="K -> E (in Ref. 2; AAA92961)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="A -> P (in Ref. 2; AAA92961)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="Q -> H (in Ref. 2; AAA92961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 115283 MW; 43B9FC1569CD5DDB CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK DESSCSSEED
EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL SSNQGTPTSP VKKFPTSTTK
ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL
DNKEKEKDNK GTRLAYVAPT IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN
SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS
SPAGTQSSTS NRLWAEDSTE KEKDSAPTAA TILVAPTVVS AAASSTTALT TTTAGTLSST
SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK TIGRSRSTRT
REQENEEKDK EEKEKQDKEK QEEKKESEVS REDEYKQKYS RTYDETYARY RPVSTSSSST
PSSSSLSTLG SSLYASSQLN RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK
SIRERRRPRE KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS
DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA QLHDTNMELT
DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME EELKMLPDLK ADNQRLKDEN
GALIRVISKL SK
