SGK3_MOUSE
ID SGK3_MOUSE Reviewed; 496 AA.
AC Q9ERE3; Q3UAY2;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Serine/threonine-protein kinase Sgk3;
DE EC=2.7.11.1;
DE AltName: Full=Cytokine-independent survival kinase;
DE AltName: Full=Serum/glucocorticoid-regulated kinase 3;
DE AltName: Full=Serum/glucocorticoid-regulated kinase-like;
GN Name=Sgk3; Synonyms=Cisk, Sgkl;
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 OF LYS-191.
RX PubMed=11050396; DOI=10.1016/s0960-9822(00)00733-8;
RA Liu D., Yang X., Songyang Z.;
RT "Identification of CISK, a new member of the SGK kinase family that
RT promotes IL-3-dependent survival.";
RL Curr. Biol. 10:1233-1236(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Bone marrow, Forelimb, 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 [3]
RP CHARACTERIZATION, AND MUTAGENESIS OF ARG-90.
RX PubMed=11514587; DOI=10.1083/jcb.200105089;
RA Xu J., Liu D., Gill G., Songyang Z.;
RT "Regulation of cytokine-independent survival kinase (CISK) by the Phox
RT homology domain and phosphoinositides.";
RL J. Cell Biol. 154:699-705(2001).
RN [4]
RP FUNCTION IN THE REGULATION OF GRIA1/GLUR1.
RX PubMed=15774536; DOI=10.1113/jphysiol.2004.079582;
RA Strutz-Seebohm N., Seebohm G., Mack A.F., Wagner H.J., Just L.,
RA Skutella T., Lang U.E., Henke G., Striegel M., Hollmann M., Rouach N.,
RA Nicoll R.A., McCormick J.A., Wang J., Pearce D., Lang F.;
RT "Regulation of GluR1 abundance in murine hippocampal neurones by serum- and
RT glucocorticoid-inducible kinase 3.";
RL J. Physiol. (Lond.) 565:381-390(2005).
RN [5]
RP FUNCTION IN THE REGULATION OF GRIK2/GLUR6.
RX PubMed=15774535; DOI=10.1113/jphysiol.2004.079624;
RA Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J.,
RA Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M.,
RA Lang F.;
RT "Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase
RT isoforms in the regulation of GluR6 expression.";
RL J. Physiol. (Lond.) 565:391-401(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP FUNCTION.
RX PubMed=21113728; DOI=10.1007/s00535-010-0348-8;
RA Pasham V., Rotte A., Bhandaru M., Eichenmueller M., Froehlich H.,
RA Mack A.F., Bobbala D., Yang W., Pearce D., Lang F.;
RT "Regulation of gastric acid secretion by the serum and glucocorticoid
RT inducible kinase isoform SGK3.";
RL J. Gastroenterol. 46:305-317(2011).
RN [9]
RP FUNCTION.
RX PubMed=21451460; DOI=10.1038/ki.2011.67;
RA Bhandaru M., Kempe D.S., Rotte A., Capuano P., Pathare G., Sopjani M.,
RA Alesutan I., Tyan L., Huang D.Y., Siraskar B., Judenhofer M.S., Stange G.,
RA Pichler B.J., Biber J., Quintanilla-Martinez L., Wagner C.A., Pearce D.,
RA Foeller M., Lang F.;
RT "Decreased bone density and increased phosphaturia in gene-targeted mice
RT lacking functional serum- and glucocorticoid-inducible kinase 3.";
RL Kidney Int. 80:61-67(2011).
RN [10]
RP FUNCTION IN THE REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
RX PubMed=21865597; DOI=10.1091/mbc.e11-04-0328;
RA He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
RA Naray-Fejes-Toth A., Yun C.C.;
RT "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates
RT acute activation of Na+/H+ exchanger NHE3 by glucocorticoids.";
RL Mol. Biol. Cell 22:3812-3825(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase which is involved in the
CC regulation of a wide variety of ion channels, membrane transporters,
CC cell growth, proliferation, survival and migration. Up-regulates Na(+)
CC channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1,
CC KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6,
CC chloride channel: BSND, creatine transporter: SLC6A8,
CC Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent
CC phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters:
CC SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1,
CC SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and
CC GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+)
CC ATPase. Plays a role in the regulation of renal tubular phosphate
CC transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively
CC regulates ER transcription activity through phosphorylation of FLII.
CC Negatively regulates the function of ITCH/AIP4 via its phosphorylation
CC and thereby prevents CXCR4 from being efficiently sorted to lysosomes.
CC {ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:15774536,
CC ECO:0000269|PubMed:21113728, ECO:0000269|PubMed:21451460,
CC ECO:0000269|PubMed:21865597}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr-
CC 320) and the other in the C-terminal regulatory region (Ser-486), need
CC to be phosphorylated for its full activation.
CC -!- SUBUNIT: Interacts with GSK3B and FLII. Interacts with PDPK1 in a
CC phosphorylation-dependent manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:21865597}. Early endosome
CC {ECO:0000269|PubMed:21865597}. Recycling endosome {ECO:0000250}.
CC Note=Endosomal localization is a prerequisite for complete kinase
CC activity. It is essential for its colocalization with the kinase
CC responsible for phosphorylating Ser-486 thus allowing PDPK1
CC phosphorylation of Thr-320 resulting in complete activation of SGK3.
CC Colocalizes with SLC9A3/NHE3 in the recycling endosomes (By
CC similarity). Localized in vesicle-like structures and in the early
CC endosome. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed, predominantly in the heart,
CC spleen and 7-day embryo.
CC -!- PTM: Activated by phosphorylation on Ser-486 by an unknown kinase (may
CC be mTORC2 but not confirmed), transforming it into a substrate for
CC PDPK1 which then phosphorylates it on Thr-320. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF312007; AAG34115.1; -; mRNA.
DR EMBL; AK030314; BAC26895.1; -; mRNA.
DR EMBL; AK031133; BAC27269.1; -; mRNA.
DR EMBL; AK031328; BAC27349.1; -; mRNA.
DR EMBL; AK146561; BAE27261.1; -; mRNA.
DR EMBL; AK151181; BAE30182.1; -; mRNA.
DR EMBL; AK171120; BAE42262.1; -; mRNA.
DR EMBL; AK171186; BAE42298.1; -; mRNA.
DR EMBL; AK171959; BAE42748.1; -; mRNA.
DR EMBL; AK172323; BAE42945.1; -; mRNA.
DR CCDS; CCDS14816.1; -.
DR RefSeq; NP_001032848.1; NM_001037759.1.
DR RefSeq; NP_573483.1; NM_133220.2.
DR RefSeq; NP_808215.2; NM_177547.3.
DR PDB; 1XTE; X-ray; 1.60 A; A=7-160.
DR PDB; 1XTN; X-ray; 2.20 A; A/B=7-126.
DR PDBsum; 1XTE; -.
DR PDBsum; 1XTN; -.
DR AlphaFoldDB; Q9ERE3; -.
DR SMR; Q9ERE3; -.
DR BioGRID; 228417; 1.
DR CORUM; Q9ERE3; -.
DR ELM; Q9ERE3; -.
DR STRING; 10090.ENSMUSP00000126861; -.
DR iPTMnet; Q9ERE3; -.
DR PhosphoSitePlus; Q9ERE3; -.
DR EPD; Q9ERE3; -.
DR MaxQB; Q9ERE3; -.
DR PaxDb; Q9ERE3; -.
DR PRIDE; Q9ERE3; -.
DR ProteomicsDB; 261336; -.
DR DNASU; 170755; -.
DR Ensembl; ENSMUST00000097826; ENSMUSP00000095437; ENSMUSG00000025915.
DR Ensembl; ENSMUST00000166384; ENSMUSP00000130078; ENSMUSG00000025915.
DR Ensembl; ENSMUST00000168907; ENSMUSP00000126861; ENSMUSG00000025915.
DR Ensembl; ENSMUST00000171265; ENSMUSP00000127462; ENSMUSG00000025915.
DR GeneID; 170755; -.
DR KEGG; mmu:170755; -.
DR UCSC; uc007agu.1; mouse.
DR CTD; 23678; -.
DR MGI; MGI:2182368; Sgk3.
DR VEuPathDB; HostDB:ENSMUSG00000025915; -.
DR eggNOG; KOG0598; Eukaryota.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00940000153776; -.
DR HOGENOM; CLU_000288_63_48_1; -.
DR InParanoid; Q9ERE3; -.
DR OMA; RNEWFVL; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q9ERE3; -.
DR TreeFam; TF320906; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 170755; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Sgk3; mouse.
DR EvolutionaryTrace; Q9ERE3; -.
DR PRO; PR:Q9ERE3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ERE3; protein.
DR Bgee; ENSMUSG00000025915; Expressed in vestibular membrane of cochlear duct and 252 other tissues.
DR ExpressionAtlas; Q9ERE3; baseline and differential.
DR Genevisible; Q9ERE3; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd06870; PX_CISK; 1.
DR CDD; cd05604; STKc_SGK3; 1.
DR DisProt; DP02635; -.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR037900; CISK_PX.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR037709; SGK3_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasmic vesicle; Endosome; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..496
FT /note="Serine/threonine-protein kinase Sgk3"
FT /id="PRO_0000086650"
FT DOMAIN 12..124
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 162..419
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 420..496
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 121..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 195..205
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 124..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 168..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 320
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q96BR1"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BR1"
FT MUTAGEN 90
FT /note="R->A: Diminishes binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:11514587"
FT MUTAGEN 191
FT /note="K->A: No activity."
FT /evidence="ECO:0000269|PubMed:11050396"
FT CONFLICT 114
FT /note="R -> G (in Ref. 2; BAC27349)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="Q -> P (in Ref. 2; BAC27349)"
FT /evidence="ECO:0000305"
FT STRAND 15..26
FT /evidence="ECO:0007829|PDB:1XTE"
FT STRAND 29..40
FT /evidence="ECO:0007829|PDB:1XTE"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:1XTE"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:1XTE"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1XTE"
SQ SEQUENCE 496 AA; 57145 MW; 4B7D2804A5948BAD CRC64;
MQRDCIMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNS
LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD
SPRHQSDPSE DEDERSTSKP HSTSRNINLG PTGNPHAKPT DFDFLKVIGK GSFGKVLLAK
RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL
DFVNGGELFF HLQRERSFPE PRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSMGHV
VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV LYEMLYGLPP
FYCRDVAEMY DNILHKPLNL RPGVSLTAWS ILEELLEKNR QNRLGAKEDF LEIQNHPFFE
SLSWTDLVQK KIPPPFNPNV AGPDDIRNFD AVFTEETVPY SVCVSSDYSI VNASVLEADD
AFVGFSYAPP SEDLFL
