SRF_MOUSE
ID SRF_MOUSE Reviewed; 504 AA.
AC Q9JM73;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serum response factor;
DE Short=SRF;
GN Name=Srf;
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 [GENOMIC DNA].
RA Miwa T.;
RT "Serum response factor.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP FUNCTION, AND INTERACTION WITH MRTFA.
RX PubMed=12732141; DOI=10.1016/s0092-8674(03)00278-2;
RA Miralles F., Posern G., Zaromytidou A.I., Treisman R.;
RT "Actin dynamics control SRF activity by regulation of its coactivator
RT MAL.";
RL Cell 113:329-342(2003).
RN [4]
RP INTERACTION WITH SRFBP1, AND SUBUNIT.
RX PubMed=15492011; DOI=10.1074/jbc.m405945200;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Identification of a novel serum response factor cofactor in cardiac gene
RT regulation.";
RL J. Biol. Chem. 279:55626-55632(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15169892; DOI=10.1128/mcb.24.12.5281-5289.2004;
RA Parlakian A., Tuil D., Hamard G., Tavernier G., Hentzen D.,
RA Concordet J.-P., Paulin D., Li Z., Daegelen D.;
RT "Targeted inactivation of serum response factor in the developing heart
RT results in myocardial defects and embryonic lethality.";
RL Mol. Cell. Biol. 24:5281-5289(2004).
RN [6]
RP INTERACTION WITH ARID2, AND SUBUNIT.
RX PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Zipzap/p200 is a novel zinc finger protein contributing to cardiac gene
RT regulation.";
RL Biochem. Biophys. Res. Commun. 346:794-801(2006).
RN [7]
RP INTERACTION WITH KAT5.
RX PubMed=16597624; DOI=10.1074/jbc.m513593200;
RA Kim M.S., Merlo X., Wilson C., Lough J.;
RT "Co-activation of atrial natriuretic factor promoter by Tip60 and serum
RT response factor.";
RL J. Biol. Chem. 281:15082-15089(2006).
RN [8]
RP INTERACTION WITH NKX3-1.
RX PubMed=16814806; DOI=10.1016/j.jmb.2006.05.064;
RA Ju J.H., Maeng J.S., Zemedkun M., Ahronovitz N., Mack J.W., Ferretti J.A.,
RA Gelmann E.P., Gruschus J.M.;
RT "Physical and functional interactions between the prostate suppressor
RT homeoprotein NKX3.1 and serum response factor.";
RL J. Mol. Biol. 360:989-999(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP FUNCTION, INTERACTION WITH MRTFA AND SCAI, AND SUBCELLULAR LOCATION.
RX PubMed=19350017; DOI=10.1038/ncb1862;
RA Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P.,
RA Grosse R.;
RT "SCAI acts as a suppressor of cancer cell invasion through the
RT transcriptional control of beta1-integrin.";
RL Nat. Cell Biol. 11:557-568(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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 [13]
RP FUNCTION.
RX PubMed=24732378; DOI=10.1101/gad.239327.114;
RA Esnault C., Stewart A., Gualdrini F., East P., Horswell S., Matthews N.,
RA Treisman R.;
RT "Rho-actin signaling to the MRTF coactivators dominates the immediate
RT transcriptional response to serum in fibroblasts.";
RL Genes Dev. 28:943-958(2014).
CC -!- FUNCTION: SRF is a transcription factor that binds to the serum
CC response element (SRE), a short sequence of dyad symmetry located 300
CC bp to the 5' of the site of transcription initiation of some genes
CC (such as FOS) (PubMed:24732378). Together with MRTFA transcription
CC coactivator, controls expression of genes regulating the cytoskeleton
CC during development, morphogenesis and cell migration (PubMed:12732141,
CC PubMed:19350017, PubMed:24732378). The SRF-MRTFA complex activity
CC responds to Rho GTPase-induced changes in cellular globular actin (G-
CC actin) concentration, thereby coupling cytoskeletal gene expression to
CC cytoskeletal dynamics (PubMed:24732378). Required for cardiac
CC differentiation and maturation (PubMed:15169892).
CC {ECO:0000269|PubMed:12732141, ECO:0000269|PubMed:15169892,
CC ECO:0000269|PubMed:19350017, ECO:0000269|PubMed:24732378}.
CC -!- SUBUNIT: Binds DNA as a multimer, probably a dimer (PubMed:15492011,
CC PubMed:16782067). Interacts with MRTFA, forming the SRF-MRTFA nuclear
CC complex which binds the 5'-CArG-3' consensus motif (CArG box) on DNA
CC via SRF (PubMed:12732141, PubMed:19350017). Forms a nuclear ternary
CC complex with MRTFA and SCAI (PubMed:19350017). Interacts with MRTFB (By
CC similarity). Interacts with MLLT7/FOXO4, NKX3A and SSRP1 (By
CC similarity). Interacts with ARID2 (PubMed:16782067). Interacts with
CC SRFBP1 (PubMed:15492011). Interacts with FOXK1 (By similarity).
CC Interacts with LPXN (By similarity). Interacts with OLFM2; the
CC interaction promotes dissociation of SRF from the transcriptional
CC repressor HEY2, facilitates binding of SRF to target genes and promotes
CC smooth muscle differentiation (By similarity). Interacts with NKX3-1
CC (PubMed:16814806). Interacts with KAT5 (PubMed:16597624).
CC {ECO:0000250|UniProtKB:P11831, ECO:0000269|PubMed:12732141,
CC ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16597624,
CC ECO:0000269|PubMed:16782067, ECO:0000269|PubMed:16814806,
CC ECO:0000269|PubMed:19350017}.
CC -!- INTERACTION:
CC Q9JM73; Q3U1N2: Srebf2; NbExp=3; IntAct=EBI-493266, EBI-645275;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC ECO:0000269|PubMed:19350017}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:P11831}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Srf in cardiac tissue display lethal
CC cardiac defects between 10.5 and 13.5 dpc, characterized by abnormally
CC thin myocardium, dilated cardiac chambers, poor trabeculation and a
CC disorganised interventricular septum. {ECO:0000269|PubMed:15169892}.
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DR EMBL; AB038376; BAA92314.1; -; Genomic_DNA.
DR EMBL; BC051950; AAH51950.1; -; mRNA.
DR CCDS; CCDS28831.1; -.
DR RefSeq; NP_065239.1; NM_020493.2.
DR AlphaFoldDB; Q9JM73; -.
DR SMR; Q9JM73; -.
DR BioGRID; 203497; 6.
DR CORUM; Q9JM73; -.
DR DIP; DIP-49624N; -.
DR IntAct; Q9JM73; 4.
DR STRING; 10090.ENSMUSP00000015749; -.
DR GlyGen; Q9JM73; 5 sites.
DR iPTMnet; Q9JM73; -.
DR PhosphoSitePlus; Q9JM73; -.
DR EPD; Q9JM73; -.
DR jPOST; Q9JM73; -.
DR MaxQB; Q9JM73; -.
DR PaxDb; Q9JM73; -.
DR PeptideAtlas; Q9JM73; -.
DR PRIDE; Q9JM73; -.
DR ProteomicsDB; 257398; -.
DR Antibodypedia; 900; 713 antibodies from 41 providers.
DR DNASU; 20807; -.
DR Ensembl; ENSMUST00000015749; ENSMUSP00000015749; ENSMUSG00000015605.
DR GeneID; 20807; -.
DR KEGG; mmu:20807; -.
DR UCSC; uc008ctg.1; mouse.
DR CTD; 6722; -.
DR MGI; MGI:106658; Srf.
DR VEuPathDB; HostDB:ENSMUSG00000015605; -.
DR eggNOG; KOG0015; Eukaryota.
DR GeneTree; ENSGT00400000022158; -.
DR HOGENOM; CLU_042048_1_0_1; -.
DR InParanoid; Q9JM73; -.
DR OMA; SHAVMYA; -.
DR OrthoDB; 1125296at2759; -.
DR PhylomeDB; Q9JM73; -.
DR TreeFam; TF318482; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR BioGRID-ORCS; 20807; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Srf; mouse.
DR PRO; PR:Q9JM73; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JM73; protein.
DR Bgee; ENSMUSG00000015605; Expressed in embryonic post-anal tail and 154 other tissues.
DR ExpressionAtlas; Q9JM73; baseline and differential.
DR Genevisible; Q9JM73; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA 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:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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:0010736; F:serum response element binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0060532; P:bronchus cartilage development; IMP:MGI.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IGI:BHF-UCL.
DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; ISO:MGI.
DR GO; GO:0030038; P:contractile actin filament bundle assembly; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:MGI.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:MGI.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:MGI.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
DR GO; GO:0060324; P:face development; IMP:MGI.
DR GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0002521; P:leukocyte differentiation; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0061145; P:lung smooth muscle development; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0030220; P:platelet formation; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:0046016; P:positive regulation of transcription by glucose; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR GO; GO:0090009; P:primitive streak formation; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0033561; P:regulation of water loss via skin; IMP:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0043589; P:skin morphogenesis; IMP:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IMP:MGI.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0030878; P:thyroid gland development; IMP:MGI.
DR GO; GO:0060534; P:trachea cartilage development; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:MGI.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Glycoprotein; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..504
FT /note="Serum response factor"
FT /id="PRO_0000245225"
FT DOMAIN 137..197
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 129..218
FT /evidence="ECO:0000250"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..218
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT REGION 215..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 431
FT /note="Phosphoserine; by dsDNA kinase"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT MOD_RES 442
FT /note="Phosphoserine; by dsDNA kinase"
FT /evidence="ECO:0000250|UniProtKB:P11831"
FT CARBOHYD 273
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 303
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 305
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 312
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 379
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 504 AA; 51247 MW; 26353F18A2B46F6B CRC64;
MLPSQAGAAA ALGRGSALGG NLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGQSRLEREA
AAAAAPTAGA LYSGSEGDSE SGEEEELGAE RRGLKRSLSE MELGVVVGGP EAAAAAAGGY
GPVSGAVSGA KPGKKTRGRV KIKMEFIDNK LRRYTTFSKR KTGIMKKAYE LSTLTGTQVL
LLVASETGHV YTFATRKLQP MITSETGKAL IQTCLNSPDS PPRSDPTTDQ RMSATGFEEP
DLTYQVSESD SSGETKDTLK PAFTVTNLPG TTSTIQTAPS TSTTMQVSSG PSFPITNYLA
PVSASVSPSA VSSANGTVLK STGSGPVSSG GLMQLPTSFT LMPGGAVAQQ VPVQAIHVHQ
APQQASPSRD SSTDLTQTSS SGTVTLPATI MTSSVPTTVG GHMMYPSPHA VMYAPTSGLA
DGSLTVLNAF SQAPSTMQVS HSQVQEPGGV PQVFLTAPSG TVQIPVSAVQ LHQMAVIGQQ
AGSSSNLTEL QVVNLDATHS TKSE
