ANM6_MOUSE
ID ANM6_MOUSE Reviewed; 378 AA.
AC Q6NZB1; Q3TA42; Q8BN52; Q8BSC2; Q8R5D7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein arginine N-methyltransferase 6;
DE EC=2.1.1.319 {ECO:0000269|PubMed:26070566};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT6;
GN Name=Prmt6; Synonyms=Hrmt1l6;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Embryo, and Mammary tumor;
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 DISRUPTION PHENOTYPE.
RX PubMed=22904064; DOI=10.1093/nar/gks764;
RA Neault M., Mallette F.A., Vogel G., Michaud-Levesque J., Richard S.;
RT "Ablation of PRMT6 reveals a role as a negative transcriptional regulator
RT of the p53 tumor suppressor.";
RL Nucleic Acids Res. 40:9513-9521(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24570487; DOI=10.1126/scisignal.2004479;
RA Han H.S., Jung C.Y., Yoon Y.S., Choi S., Choi D., Kang G., Park K.G.,
RA Kim S.T., Koo S.H.;
RT "Arginine methylation of CRTC2 is critical in the transcriptional control
RT of hepatic glucose metabolism.";
RL Sci. Signal. 7:RA19-RA19(2014).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26070566; DOI=10.1074/jbc.m115.637660;
RA Huang J., Cardamone M.D., Johnson H.E., Neault M., Chan M., Floyd Z.E.,
RA Mallette F.A., Perissi V.;
RT "Exchange factor TBL1 and arginine methyltransferase PRMT6 cooperate in
RT protecting G protein pathway suppressor 2 (GPS2) from proteasomal
RT degradation.";
RL J. Biol. Chem. 290:19044-19054(2015).
CC -!- FUNCTION: Arginine methyltransferase that can catalyze the formation of
CC both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine
CC (aDMA), with a strong preference for the formation of aDMA
CC (PubMed:22904064, PubMed:26070566). Preferentially methylates arginyl
CC residues present in a glycine and arginine-rich domain and displays
CC preference for monomethylated substrates (By similarity). Specifically
CC mediates the asymmetric dimethylation of histone H3 'Arg-2' to form
CC H3R2me2a (By similarity). H3R2me2a represents a specific tag for
CC epigenetic transcriptional repression and is mutually exclusive with
CC methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3) (By
CC similarity). Acts as a transcriptional repressor of various genes such
CC as HOXA2, THBS1 and TP53 (PubMed:22904064). Repression of TP53 blocks
CC cellular senescence (PubMed:22904064). Also methylates histone H2A and
CC H4 'Arg-3' (H2AR3me and H4R3me, respectively) (By similarity). Acts as
CC a regulator of DNA base excision during DNA repair by mediating the
CC methylation of DNA polymerase beta (POLB), leading to the stimulation
CC of its polymerase activity by enhancing DNA binding and processivity
CC (By similarity). Methylates HMGA1 (By similarity). Regulates
CC alternative splicing events (By similarity). Acts as a transcriptional
CC coactivator of a number of steroid hormone receptors including ESR1,
CC ESR2, PGR and NR3C1 (By similarity). Promotes fasting-induced
CC transcriptional activation of the gluconeogenic program through
CC methylation of the CRTC2 transcription coactivator (PubMed:24570487).
CC Methylates GPS2, protecting GPS2 from ubiquitination and degradation
CC (PubMed:26070566). Methylates SIRT7, inhibiting SIRT7 histone
CC deacetylase activity and promoting mitochondria biogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q96LA8,
CC ECO:0000269|PubMed:22904064, ECO:0000269|PubMed:24570487,
CC ECO:0000269|PubMed:26070566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000269|PubMed:26070566};
CC -!- SUBUNIT: Interacts with (and methylates) HIV-1 Tat, Rev and
CC Nucleocapsid protein p7 (NC). Interacts with EPB41L3 and NCOA1.
CC {ECO:0000250|UniProtKB:Q96LA8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LA8}.
CC -!- PTM: Automethylation enhances its stability. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic fibroblasts from mutant mice display
CC growth defects, premature senescence and increased levels of TP53 and
CC multiple TP53 targets. In liver, knockdown disrupts the formation of a
CC cAMP-mediated transcription complex involving CRTC2, reduces the
CC expression of genes encoding gluconeogenic factors and decreases
CC glucose output in primary hepatocytes, it also restores euglycemia in
CC insulin-resistant mice. {ECO:0000269|PubMed:22904064,
CC ECO:0000269|PubMed:24570487}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT6
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28811.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC39923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK034732; BAC28811.1; ALT_INIT; mRNA.
DR EMBL; AK087551; BAC39923.1; ALT_INIT; mRNA.
DR EMBL; AK172003; BAE42769.1; -; mRNA.
DR EMBL; AK172105; BAE42828.1; -; mRNA.
DR EMBL; AK172722; BAE43144.1; -; mRNA.
DR EMBL; BC022899; AAH22899.1; -; mRNA.
DR EMBL; BC066221; AAH66221.1; -; mRNA.
DR CCDS; CCDS38605.1; -.
DR RefSeq; NP_849222.3; NM_178891.5.
DR PDB; 4C03; X-ray; 1.58 A; A/B=1-378.
DR PDB; 4C04; X-ray; 1.58 A; A=1-378.
DR PDB; 4C05; X-ray; 2.20 A; A=1-378.
DR PDB; 4C06; X-ray; 1.60 A; A=1-378.
DR PDB; 4C07; X-ray; 1.50 A; A=1-378.
DR PDB; 4C08; X-ray; 1.34 A; A=1-378.
DR PDB; 5FQN; X-ray; 1.66 A; A=1-378.
DR PDB; 5FQO; X-ray; 1.90 A; A=1-378.
DR PDB; 5LV4; X-ray; 1.66 A; A=1-378.
DR PDB; 5LV5; X-ray; 1.80 A; A=1-378.
DR PDB; 6SQ3; X-ray; 2.15 A; A/B=1-378.
DR PDB; 6SQ4; X-ray; 1.70 A; A/B=1-378.
DR PDB; 6SQH; X-ray; 2.39 A; A/B=1-378.
DR PDB; 6SQI; X-ray; 1.60 A; A=1-378.
DR PDB; 6SQK; X-ray; 1.40 A; A/B=1-378.
DR PDB; 7NUD; X-ray; 1.65 A; A/B=1-378.
DR PDB; 7NUE; X-ray; 2.00 A; A/B=1-378.
DR PDBsum; 4C03; -.
DR PDBsum; 4C04; -.
DR PDBsum; 4C05; -.
DR PDBsum; 4C06; -.
DR PDBsum; 4C07; -.
DR PDBsum; 4C08; -.
DR PDBsum; 5FQN; -.
DR PDBsum; 5FQO; -.
DR PDBsum; 5LV4; -.
DR PDBsum; 5LV5; -.
DR PDBsum; 6SQ3; -.
DR PDBsum; 6SQ4; -.
DR PDBsum; 6SQH; -.
DR PDBsum; 6SQI; -.
DR PDBsum; 6SQK; -.
DR PDBsum; 7NUD; -.
DR PDBsum; 7NUE; -.
DR AlphaFoldDB; Q6NZB1; -.
DR SMR; Q6NZB1; -.
DR BioGRID; 221340; 8.
DR IntAct; Q6NZB1; 6.
DR STRING; 10090.ENSMUSP00000102177; -.
DR PhosphoSitePlus; Q6NZB1; -.
DR EPD; Q6NZB1; -.
DR MaxQB; Q6NZB1; -.
DR PaxDb; Q6NZB1; -.
DR PeptideAtlas; Q6NZB1; -.
DR PRIDE; Q6NZB1; -.
DR ProteomicsDB; 296207; -.
DR Antibodypedia; 21010; 434 antibodies from 42 providers.
DR DNASU; 99890; -.
DR Ensembl; ENSMUST00000106567; ENSMUSP00000102177; ENSMUSG00000049300.
DR Ensembl; ENSMUST00000168412; ENSMUSP00000129801; ENSMUSG00000049300.
DR Ensembl; ENSMUST00000190378; ENSMUSP00000140836; ENSMUSG00000049300.
DR GeneID; 99890; -.
DR KEGG; mmu:99890; -.
DR UCSC; uc008rau.2; mouse.
DR CTD; 55170; -.
DR MGI; MGI:2139971; Prmt6.
DR VEuPathDB; HostDB:ENSMUSG00000049300; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000160961; -.
DR HOGENOM; CLU_017375_1_2_1; -.
DR InParanoid; Q6NZB1; -.
DR OMA; SARHICI; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q6NZB1; -.
DR TreeFam; TF328817; -.
DR BRENDA; 2.1.1.319; 3474.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR BioGRID-ORCS; 99890; 3 hits in 114 CRISPR screens.
DR PRO; PR:Q6NZB1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6NZB1; protein.
DR Bgee; ENSMUSG00000049300; Expressed in metanephric cortical collecting duct and 186 other tissues.
DR Genevisible; Q6NZB1; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0070612; F:histone methyltransferase activity (H2A-R3 specific); ISS:UniProtKB.
DR GO; GO:0070611; F:histone methyltransferase activity (H3-R2 specific); ISS:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034970; P:histone H3-R2 methylation; IMP:MGI.
DR GO; GO:0016571; P:histone methylation; ISO:MGI.
DR GO; GO:0031064; P:negative regulation of histone deacetylation; ISS:UniProtKB.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; ISS:UniProtKB.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IDA:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA damage; DNA repair; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..378
FT /note="Protein arginine N-methyltransferase 6"
FT /id="PRO_0000212333"
FT DOMAIN 47..377
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> W (in Ref. 1; BAC28811)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="E -> D (in Ref. 1; BAC28811)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="F -> L (in Ref. 2; AAH66221)"
FT /evidence="ECO:0000305"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:6SQK"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:4C08"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4C08"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4C08"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 202..218
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 284..299
FT /evidence="ECO:0007829|PDB:4C08"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6SQK"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 323..334
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 352..364
FT /evidence="ECO:0007829|PDB:4C08"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:4C08"
SQ SEQUENCE 378 AA; 41866 MW; F1EB7FCFF9C54242 CRC64;
MSLSKKRKLE SGDSGGAGAG GEGAEEENGG EQEAAPPRPR RTKSERDQLY YECYSDVSVH
EEMIADQVRT EAYRLGILKN WAALRGKTVL DVGAGTGILS IFCAQAGARR VYAVEASAIW
QQAREVVRLN GLEDRVHVLP GPVETVELPE RVDAIVSEWM GYGLLHESML SSVLHARTKW
LKEGGLLLPA SAELFVAPIS DQMLEWRLGF WSQVKQHYGV DMSCMESFAT RCLMGHSEIV
VQDLSGEDVL ARPQRFAQLE LARAGLEQEL EAGVGGRFRC SCYGSAPLHG FAVWFQVTFP
GGDSEKPLVL STSPFHPATH WKQALLYLNE PVPVEQDTDI SGEITLLPSP DNPRRLRILL
RYKVGDHEEK TKDFAMED
