NFAC1_MOUSE
ID NFAC1_MOUSE Reviewed; 717 AA.
AC O88942; O70345;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 1;
DE Short=NF-ATc1;
DE Short=NFATc1;
DE AltName: Full=NFAT transcription complex cytosolic component;
DE Short=NF-ATc;
DE Short=NFATc {ECO:0000303|PubMed:9388475};
GN Name=Nfatc1; Synonyms=Nfat2, Nfatc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9388475; DOI=10.1006/bbrc.1997.7381;
RA Pan S., Koyano-Nakagawa N., Tsuruta L., Amasaki Y., Yokota T., Mori S.,
RA Arai N., Arai K.;
RT "Molecular cloning and functional characterization of murine cDNA encoding
RT transcription factor NFATc.";
RL Biochem. Biophys. Res. Commun. 240:314-323(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Fetal liver, and Mast cell;
RX PubMed=10072529;
RA Sherman M.A., Powell D.R., Weiss D.L., Brown M.A.;
RT "NF-ATc Isoforms are differentially expressed and regulated in murine T and
RT mast cells.";
RL J. Immunol. 162:2820-2828(1999).
RN [3]
RP INDUCTION BY TNFSF11-INDUCED OSTEOCLASTOGENESIS.
RX PubMed=16968888; DOI=10.1152/ajprenal.00415.2005;
RA Sun L., Peng Y., Zaidi N., Zhu L.L., Iqbal J., Yamoah K., Wang X., Liu P.,
RA Abe E., Moonga B.S., Epstein S., Zaidi M.;
RT "Evidence that calcineurin is required for the genesis of bone-resorbing
RT osteoclasts.";
RL Am. J. Physiol. 292:F285-F291(2007).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=17198697; DOI=10.1016/j.ydbio.2006.11.036;
RA Yang X.Y., Yang T.T.C., Schubert W., Factor S.M., Chow C.-W.;
RT "Dosage-dependent transcriptional regulation by the calcineurin/NFAT
RT signaling in developing myocardium transition.";
RL Dev. Biol. 303:825-837(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19626032; DOI=10.1038/jid.2009.222;
RA Pena J.A., Losi-Sasaki J.L., Gooch J.L.;
RT "Loss of calcineurin Aalpha alters keratinocyte survival and
RT differentiation.";
RL J. Invest. Dermatol. 130:135-140(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=21435446; DOI=10.1016/j.ajpath.2010.12.054;
RA Reddy R.N., Pena J.A., Roberts B.R., Williams S.R., Price S.R., Gooch J.L.;
RT "Rescue of calcineurin Aalpha(-/-) mice reveals a novel role for the alpha
RT isoform in the salivary gland.";
RL Am. J. Pathol. 178:1605-1613(2011).
RN [8]
RP FUNCTION, INTERACTION WITH TLE6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY TNFSF11-INDUCED OSTEOCLASTOGENESIS.
RX PubMed=23990468; DOI=10.1074/jbc.m113.461848;
RA Kogawa M., Hisatake K., Atkins G.J., Findlay D.M., Enoki Y., Sato T.,
RA Gray P.C., Kanesaki-Yatsuka Y., Anderson P.H., Wada S., Kato N., Fukuda A.,
RA Katayama S., Tsujimoto M., Yoda T., Suda T., Okazaki Y., Matsumoto M.;
RT "The paired-box homeodomain transcription factor Pax6 binds to the upstream
RT region of the TRAP gene promoter and suppresses receptor activator of NF-
RT kappaB ligand (RANKL)-induced osteoclast differentiation.";
RL J. Biol. Chem. 288:31299-31312(2013).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=24039232; DOI=10.1242/jcs.127571;
RA Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
RA Reinhardt D.P., Komarova S.V.;
RT "Fibrillin-1 directly regulates osteoclast formation and function by a dual
RT mechanism.";
RL J. Cell Sci. 126:4187-4194(2013).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=26644563; DOI=10.1073/pnas.1511285112;
RA Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C., Mellins E.D.,
RA Novack D.V., Faccio R.;
RT "Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
RT regulate bone mass.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=28341745; DOI=10.1074/jbc.m117.784777;
RA Murakami A., Matsuda M., Harada Y., Hirata M.;
RT "Phospholipase C-related, but catalytically inactive protein (PRIP)
RT upregulates osteoclast differentiation via calcium-calcineurin-NFATc1
RT signaling.";
RL J. Biol. Chem. 292:7994-8006(2017).
CC -!- FUNCTION: Plays a role in the inducible expression of cytokine genes in
CC T-cells, especially in the induction of the IL-2 or IL-4 gene
CC transcription (PubMed:9388475). Also controls gene expression in
CC embryonic cardiac cells. Could regulate not only the activation and
CC proliferation but also the differentiation and programmed death of T-
CC lymphocytes as well as lymphoid and non-lymphoid cells (By similarity).
CC Required for osteoclastogenesis and regulates many genes important for
CC osteoclast differentiation and function (PubMed:23990468,
CC PubMed:26644563). {ECO:0000250|UniProtKB:O95644,
CC ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:9388475,
CC ECO:0000303|PubMed:26644563}.
CC -!- SUBUNIT: Member of the multicomponent NFATC transcription complex that
CC consists of at least two components, a pre-existing cytoplasmic
CC component NFATC2 and an inducible nuclear component NFATC1. Other
CC members such as NFATC4, NFATC3 or members of the activating protein-1
CC family, MAF, GATA4 and Cbp/p300 can also bind the complex. NFATC
CC proteins bind to DNA as monomers (By similarity). Interacts with HOMER2
CC and HOMER3; this interaction may compete with calcineurin/PPP3CA-
CC binding and hence prevent NFATC1 dephosphorylation and activation (By
CC similarity). Interacts with TLE6/GRG6 (PubMed:23990468). {ECO:0000250,
CC ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:23990468}.
CC -!- INTERACTION:
CC O88942; PRO_0000278754 [Q913V3]; Xeno; NbExp=2; IntAct=EBI-8073353, EBI-10053030;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19626032,
CC ECO:0000269|PubMed:28341745}. Nucleus {ECO:0000269|PubMed:19626032,
CC ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:24039232,
CC ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:28341745}.
CC Note=Cytoplasmic for the phosphorylated form and nuclear after
CC activation that is controlled by calcineurin-mediated
CC dephosphorylation. Rapid nuclear exit of NFATC is thought to be one
CC mechanism by which cells distinguish between sustained and transient
CC calcium signals. The subcellular localization of NFATC plays a key role
CC in the regulation of gene transcription (By similarity). Nuclear
CC translocation of NFATC1 is enhanced in the presence of TNFSF11
CC (PubMed:26644563). Nuclear translocation is decreased in the presence
CC of FBN1 which can bind and sequester TNFSF11 (PubMed:24039232).
CC {ECO:0000250|UniProtKB:O95644, ECO:0000269|PubMed:24039232,
CC ECO:0000269|PubMed:26644563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=Alpha;
CC IsoId=O88942-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O88942-2; Sequence=VSP_005594;
CC Name=Alpha';
CC IsoId=O88942-3; Sequence=VSP_018867;
CC -!- TISSUE SPECIFICITY: Expressed in the submandibular gland (at protein
CC level) (PubMed:21435446). Expressed in basal epidermal cells (at
CC protein level) (PubMed:19626032). Expressed in spleen, lung, skeletal
CC muscle, thymus and skin (PubMed:9388475). Weakly expressed in heart,
CC brain, liver and kidney. Not expressed in testis (PubMed:10072529).
CC Expressed in osteoclasts (PubMed:23990468).
CC {ECO:0000269|PubMed:10072529, ECO:0000269|PubMed:19626032,
CC ECO:0000269|PubMed:21435446, ECO:0000269|PubMed:23990468,
CC ECO:0000269|PubMed:9388475}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels at 7 dpc and increases
CC until 17 dpc. At 17 dpc, strongly expressed in thymus, lung and
CC submandibular gland and weakly in skeletal muscle and heart
CC (PubMed:9388475). Expressed in the developing heart at 13.5 and 16.5
CC dpc, during the transition from spongy to compact myocardium
CC (PubMed:17198697). {ECO:0000269|PubMed:17198697,
CC ECO:0000269|PubMed:9388475}.
CC -!- INDUCTION: Inducibly expressed in T-lymphocytes upon activation of the
CC T-cell receptor (TCR) complex. Induced after addition of phorbol 12-
CC myristate 13-acetate (PMA) (PubMed:9388475, PubMed:10072529). Expressed
CC during osteoclastogenesis, its induction and activation is regulated by
CC TNFSF11/RANKL (PubMed:16968888, PubMed:23990468, PubMed:26644563).
CC {ECO:0000269|PubMed:10072529, ECO:0000269|PubMed:16968888,
CC ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:26644563,
CC ECO:0000269|PubMed:9388475}.
CC -!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative
CC interactions with AP1 factors. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal transactivation domain (TAD-A) binds to and is
CC activated by Cbp/p300. The dephosphorylated form contains two unmasked
CC nuclear localization signals (NLS), which allow translocation of the
CC protein to the nucleus (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation induces
CC NFATC1 nuclear exit and dephosphorylation by calcineurin promotes
CC nuclear import. Phosphorylation by PKA and DYRK2 negatively modulates
CC nuclear accumulation, and promotes subsequent phosphorylation by GSK3B
CC or casein kinase 1 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Alpha']: Produced by alternative initiation at
CC Met-37 of isoform Alpha. {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; AF049606; AAC05505.1; -; mRNA.
DR EMBL; AF087434; AAC36725.1; -; mRNA.
DR CCDS; CCDS29369.1; -. [O88942-2]
DR CCDS; CCDS89287.1; -. [O88942-1]
DR AlphaFoldDB; O88942; -.
DR SMR; O88942; -.
DR IntAct; O88942; 2.
DR MINT; O88942; -.
DR STRING; 10090.ENSMUSP00000129001; -.
DR ChEMBL; CHEMBL6034; -.
DR iPTMnet; O88942; -.
DR PhosphoSitePlus; O88942; -.
DR EPD; O88942; -.
DR jPOST; O88942; -.
DR MaxQB; O88942; -.
DR PaxDb; O88942; -.
DR PRIDE; O88942; -.
DR ProteomicsDB; 287397; -. [O88942-1]
DR ProteomicsDB; 287398; -. [O88942-2]
DR ProteomicsDB; 287399; -. [O88942-3]
DR MGI; MGI:102469; Nfatc1.
DR eggNOG; ENOG502QTX8; Eukaryota.
DR InParanoid; O88942; -.
DR PhylomeDB; O88942; -.
DR Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR ChiTaRS; Nfatc1; mouse.
DR PRO; PR:O88942; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88942; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003176; P:aortic valve development; IMP:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:MGI.
DR GO; GO:0002337; P:B-1a B cell differentiation; IMP:MGI.
DR GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; IMP:MGI.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IGI:BHF-UCL.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IMP:MGI.
DR GO; GO:0003170; P:heart valve development; IMP:BHF-UCL.
DR GO; GO:0003179; P:heart valve morphogenesis; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; IGI:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0003177; P:pulmonary valve development; IMP:BHF-UCL.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:MGI.
DR GO; GO:0042634; P:regulation of hair cycle; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:1905314; P:semi-lunar valve development; IMP:BHF-UCL.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0014883; P:transition between fast and slow fiber; IMP:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR015647; NFAT1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR PANTHER; PTHR12533:SF5; PTHR12533:SF5; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative initiation; Alternative splicing; Cytoplasm;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..717
FT /note="Nuclear factor of activated T-cells, cytoplasmic 1"
FT /id="PRO_0000030331"
FT REPEAT 205..221
FT /note="1"
FT REPEAT 235..251
FT /note="2"
FT REPEAT 284..300
FT /note="3"
FT DOMAIN 411..593
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DNA_BIND 440..447
FT /evidence="ECO:0000250"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..125
FT /note="Calcineurin-binding"
FT REGION 128..220
FT /note="Trans-activation domain A (TAD-A)"
FT REGION 202..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..300
FT /note="3 X SP repeats"
FT MOTIF 267..269
FT /note="Nuclear localization signal"
FT MOTIF 312..323
FT /note="Nuclear export signal"
FT MOTIF 683..685
FT /note="Nuclear localization signal"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95644"
FT MOD_RES 271
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95644"
FT MOD_RES 296
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95644"
FT VAR_SEQ 1..42
FT /note="MPNTSFPVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEE -> MTGLEQ
FT DPEFDFDFLFEFDQSGGGAAAA (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:9388475"
FT /id="VSP_005594"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform Alpha')"
FT /evidence="ECO:0000305"
FT /id="VSP_018867"
SQ SEQUENCE 717 AA; 77833 MW; 58837C6CC085268D CRC64;
MPNTSFPVPS KFPLGPPAAV CGSGETLRPA PPSGGTMKAA EEEHYSYVSP SVTSTLPLPT
AHSALPAACH DLQTSTPGIS AVPSANHPPS YGGAVDSGPS GYFLSSGNTR PNGAPTLESP
RIEITSYLGL HHGSGQFFHD VEVEDVLPSC KRSPSTATLH LPSLEAYRDP SCLSPASSLS
SRSCNSEASS YESNYSYPYA SPQTSPWQSP CVSPKTTDPE EGFPRSLGAC HLLGSPRHSP
STSPRASITE ESWLGARGSR PTSPCNKRKY SLNGRQPSCS PHHSPTPSPH GSPRVSVTED
TWLGNTTQYT SSAIVAAINA LTTDSTLDLG DGVPIKSRKT ALEHAPSVAL KVEPAGEDLG
TTPPTSDFPP EEYTFQHLRK GAFCEQYLSV PQASYQWAKP KSLSPTSYMS PSLPALDWQL
PSHSGPYELR IEVQPKSHHR AHYETEGSRG AVKASAGGHP IVQLHGYLEN EPLTLQLFIG
TADDRLLRPH AFYQVHRITG KTVSTTSHEI ILSNTKVLEI PLLPENNMRA IIDCAGILKL
RNSDIELRKG ETDIGRKNTR VRLVFRVHIP QPNGRTLSLQ VASNPIECSQ RSAQELPLVE
KQSTDSYPVI GGKKMVLSGH NFLQDSKVIF VEKAPDGHHV WEMEAKTDRD LCKPNSLVVE
IPPFRNQRIT SPAQVSFYVC NGKRKRSQYQ RFTYLPANGN SVFLTLSSES ELRGGFY
