MP2K2_MOUSE
ID MP2K2_MOUSE Reviewed; 401 AA.
AC Q63932; Q9D7B0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
DE Short=MAP kinase kinase 2;
DE Short=MAPKK 2;
DE EC=2.7.12.2 {ECO:0000269|PubMed:10409742};
DE AltName: Full=ERK activator kinase 2;
DE AltName: Full=MAPK/ERK kinase 2;
DE Short=MEK 2;
GN Name=Map2k2; Synonyms=Mek2, Mkk2, Prkmk2;
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], AND MUTAGENESIS.
RC STRAIN=BALB/cJ; TISSUE=Neonatal brain;
RX PubMed=8297798;
RA Brott B.K., Alessandrini A., Largaespada D.A., Copeland N.G., Jenkins N.A.,
RA Crews C.M., Erikson R.L.;
RT "MEK2 is a kinase related to MEK1 and is differentially expressed in murine
RT tissues.";
RL Cell Growth Differ. 4:921-929(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 118-140 AND 210-238.
RC TISSUE=T-cell;
RX PubMed=1381507; DOI=10.1073/pnas.89.17.8205;
RA Crews C.M., Erikson R.L.;
RT "Purification of a murine protein-tyrosine/threonine kinase that
RT phosphorylates and activates the Erk-1 gene product: relationship to the
RT fission yeast byr1 gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992).
RN [5]
RP CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH KSR1, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION AT SER-222.
RX PubMed=10409742; DOI=10.1128/mcb.19.8.5523;
RA Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
RT "Kinase suppressor of Ras forms a multiprotein signaling complex and
RT modulates MEK localization.";
RL Mol. Cell. Biol. 19:5523-5534(1999).
RN [6]
RP INTERACTION WITH MORG1.
RX PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA Bissonette E.A., Weber M.J.;
RT "Modular construction of a signaling scaffold: MORG1 interacts with
RT components of the ERK cascade and links ERK signaling to specific
RT agonists.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
RN [7]
RP INTERACTION WITH MAP2K1/MEK1, PHOSPHORYLATION BY MAP2K1/MEK1, AND FUNCTION
RP IN ERK SIGNALING.
RX PubMed=19219045; DOI=10.1038/nsmb.1564;
RA Catalanotti F., Reyes G., Jesenberger V., Galabova-Kovacs G.,
RA de Matos Simoes R., Carugo O., Baccarini M.;
RT "A Mek1-Mek2 heterodimer determines the strength and duration of the Erk
RT signal.";
RL Nat. Struct. Mol. Biol. 16:294-303(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and
CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases.
CC Activates the ERK1 and ERK2 MAP kinases (PubMed:19219045). Activates
CC BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2
CC releases the inhibitory intramolecular interaction between KSR1 or KSR2
CC protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF
CC dimerization and BRAF activation (By similarity).
CC {ECO:0000250|UniProtKB:P36507, ECO:0000269|PubMed:19219045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:10409742};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2; Evidence={ECO:0000269|PubMed:10409742};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:10409742};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10409742};
CC -!- ACTIVITY REGULATION: Inhibited by serine/threonine phosphatase 2A.
CC -!- SUBUNIT: Interacts with MORG1 (PubMed:15118098). Interacts with SGK1
CC (By similarity). Interacts with KSR1 (PubMed:10409742). Interacts with
CC KSR1 and BRAF; the interaction with KSR1 mediates KSR1-BRAF
CC dimerization (By similarity). Interacts with GLS (By similarity).
CC {ECO:0000250|UniProtKB:P36507, ECO:0000250|UniProtKB:Q02750,
CC ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:15118098}.
CC -!- INTERACTION:
CC Q63932; Q8CGE9: Rgs12; NbExp=3; IntAct=EBI-397724, EBI-7340552;
CC Q63932; P85298-4: ARHGAP8; Xeno; NbExp=5; IntAct=EBI-397724, EBI-9523517;
CC Q63932; Q13526: PIN1; Xeno; NbExp=12; IntAct=EBI-397724, EBI-714158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane
CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably
CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}.
CC -!- TISSUE SPECIFICITY: Expressed in adult intestine, kidney, liver, lung,
CC pancreas, spleen, thymus, and at high levels in the neonatal brain.
CC Lower expression is found in adult brain and heart.
CC -!- PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF or
CC MEKK1) regulates positively the kinase activity. Phosphorylated by
CC MAP2K1/MEK1. Low levels of autophosphorylation have been observed.
CC {ECO:0000269|PubMed:19219045}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; S68267; AAC60678.1; -; mRNA.
DR EMBL; AK009392; BAB26261.1; -; mRNA.
DR EMBL; AK080574; BAC37945.1; -; mRNA.
DR EMBL; CH466553; EDL31456.1; -; Genomic_DNA.
DR CCDS; CCDS24044.1; -.
DR RefSeq; NP_075627.2; NM_023138.5.
DR PDB; 1JKY; X-ray; 3.90 A; B=1-16.
DR PDBsum; 1JKY; -.
DR AlphaFoldDB; Q63932; -.
DR SMR; Q63932; -.
DR BioGRID; 204950; 14.
DR DIP; DIP-454N; -.
DR IntAct; Q63932; 6.
DR MINT; Q63932; -.
DR STRING; 10090.ENSMUSP00000121111; -.
DR ChEMBL; CHEMBL3885565; -.
DR iPTMnet; Q63932; -.
DR PhosphoSitePlus; Q63932; -.
DR EPD; Q63932; -.
DR jPOST; Q63932; -.
DR MaxQB; Q63932; -.
DR PaxDb; Q63932; -.
DR PeptideAtlas; Q63932; -.
DR PRIDE; Q63932; -.
DR ProteomicsDB; 291394; -.
DR DNASU; 26396; -.
DR Ensembl; ENSMUST00000143517; ENSMUSP00000121111; ENSMUSG00000035027.
DR GeneID; 26396; -.
DR KEGG; mmu:26396; -.
DR UCSC; uc007gfx.2; mouse.
DR CTD; 5605; -.
DR MGI; MGI:1346867; Map2k2.
DR VEuPathDB; HostDB:ENSMUSG00000035027; -.
DR eggNOG; KOG0581; Eukaryota.
DR GeneTree; ENSGT00940000153487; -.
DR InParanoid; Q63932; -.
DR OMA; IAGWVCK; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q63932; -.
DR TreeFam; TF105137; -.
DR BRENDA; 2.7.12.2; 3474.
DR Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
DR Reactome; R-MMU-170968; Frs2-mediated activation.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5674499; Negative feedback regulation of MAPK pathway.
DR BioGRID-ORCS; 26396; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Map2k2; mouse.
DR PRO; PR:Q63932; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q63932; protein.
DR Bgee; ENSMUSG00000035027; Expressed in hindlimb stylopod muscle and 267 other tissues.
DR ExpressionAtlas; Q63932; baseline and differential.
DR Genevisible; Q63932; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; TAS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005770; C:late endosome; TAS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0060502; P:epithelial cell proliferation involved in lung morphogenesis; IGI:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:0060324; P:face development; IGI:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IGI:MGI.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; ISO:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:BHF-UCL.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
DR GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
DR GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
DR GO; GO:0048538; P:thymus development; IGI:MGI.
DR GO; GO:0030878; P:thyroid gland development; IGI:MGI.
DR GO; GO:0060440; P:trachea formation; IGI:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..401
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 2"
FT /id="PRO_0000086373"
FT DOMAIN 72..370
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 282..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 78..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 10..11
FT /note="Cleavage; by anthrax lethal factor"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 222
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000269|PubMed:10409742"
FT MOD_RES 226
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02750"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36507"
FT MUTAGEN 101
FT /note="K->M: Inactivation."
FT /evidence="ECO:0000269|PubMed:8297798"
FT CONFLICT 96
FT /note="L -> F (in Ref. 1; AAC60678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 44402 MW; F00CD807E86F5B26 CRC64;
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELDLDEQQ RKRLEAFLTQ
KAKVGELKDD DFERISELGA GNGGVVTKAR HRPSGLIMAR KLIHLEIKPA VRNQIIRELQ
VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEDIL GKVSIAVLRG
LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMSPERLQ
GTHYSVQSDI WSMGLSLVEL AIGRYPIPPP DAKELEASFG RPVVDGADGE PHSVSPRPRP
PGRPISVGHG MDSRPAMAIF ELLDYIVNEP PPKLPSGVFS SDFQEFVNKC LIKNPAERAD
LKLLMNHAFI KRSEGEEVDF AGWLCRTLRL KQPSTPTRTA V
