ID SGK2_HUMAN Reviewed; 367 AA. AC Q9HBY8; Q52PK5; Q5H8Y6; Q5H8Z1; Q5TZR3; Q9UKG6; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2021, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Serine/threonine-protein kinase Sgk2; DE EC=2.7.11.1; DE AltName: Full=Serum/glucocorticoid-regulated kinase 2; GN Name=SGK2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, RP PHOSPHORYLATION AT THR-193, AND MUTAGENESIS OF SER-356. RX PubMed=10548550; DOI=10.1042/bj3440189; RA Kobayashi T., Deak M., Morrice N., Cohen P.; RT "Characterization of the structure and regulation of two novel isoforms of RT serum- and glucocorticoid-induced protein kinase."; RL Biochem. J. 344:189-197(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Xiao W., Lin L., Yang S.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Colon; 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 [6] RP FUNCTION IN THE REGULATION OF NA(+)/K(+) ATPASE. RX PubMed=12590200; DOI=10.1159/000068699; RA Henke G., Setiawan I., Boehmer C., Lang F.; RT "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent RT kinase isoforms."; RL Kidney Blood Press. Res. 25:370-374(2002). RN [7] RP FUNCTION. RX PubMed=12397388; DOI=10.1007/s00424-002-0873-2; RA Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G., RA Huber S.M., Kobayashi T., Cohen P., Lang F.; RT "K(+) channel activation by all three isoforms of serum- and RT glucocorticoid-dependent protein kinase SGK."; RL Pflugers Arch. 445:60-66(2002). RN [8] RP FUNCTION IN THE REGULATION OF KCNE1 AND KCNQ1. RX PubMed=12634932; DOI=10.1007/s00424-002-0982-y; RA Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.; RT "Regulation of KCNE1-dependent K(+) current by the serum and RT glucocorticoid-inducible kinase (SGK) isoforms."; RL Pflugers Arch. 445:601-606(2003). RN [9] RP FUNCTION IN THE REGULATION OF SCNN1A/ENAC. RX PubMed=12632189; DOI=10.1007/s00424-002-0993-8; RA Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S., RA Wang J., Pearce D., Lang F.; RT "The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the RT epithelial Na+ channel alpha,beta,gamma-ENaC."; RL Pflugers Arch. 445:693-696(2003). RN [10] RP FUNCTION IN THE REGULATION OF KCNA3/KV1.3. RX PubMed=15040001; DOI=10.1002/jcp.10430; RA Henke G., Maier G., Wallisch S., Boehmer C., Lang F.; RT "Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase RT Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1."; RL J. Cell. Physiol. 199:194-199(2004). RN [11] RP FUNCTION IN THE REGULATION OF SLC6A19. RX PubMed=20511718; DOI=10.1159/000315092; RA Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S., RA Lang F., Palmada M.; RT "The serum and glucocorticoid inducible kinases SGK1-3 stimulate the RT neutral amino acid transporter SLC6A19."; RL Cell. Physiol. Biochem. 25:723-732(2010). RN [12] 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). RN [13] RP REVIEW. RX PubMed=16460280; DOI=10.1146/annurev.physiol.68.040104.131654; RA Loffing J., Flores S.Y., Staub O.; RT "Sgk kinases and their role in epithelial transport."; RL Annu. Rev. Physiol. 68:461-490(2006). RN [14] RP REVIEW ON FUNCTION. RX PubMed=20919962; DOI=10.3109/08977194.2010.518616; RA Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E.; RT "Second AKT: the rise of SGK in cancer signalling."; RL Growth Factors 28:394-408(2010). RN [15] RP VARIANTS [LARGE SCALE ANALYSIS] LYS-199 AND TYR-289, AND VARIANT THR-12 RP (ISOFORM 2). RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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, survival and proliferation. Up-regulates Na(+) channels: CC SCNN1A/ENAC, K(+) channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid CC transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate CC receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: CC SLC9A3/NHE3, and the Na(+)/K(+) ATPase. {ECO:0000269|PubMed:12397388, CC ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12632189, CC ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:15040001, CC ECO:0000269|PubMed:20511718, 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 193) and the other in the C-terminal regulatory region (Ser-356), need CC to be phosphorylated for its full activation. CC -!- INTERACTION: CC Q9HBY8; P08238: HSP90AB1; NbExp=2; IntAct=EBI-3914329, EBI-352572; CC Q9HBY8-2; Q9BW71: HIRIP3; NbExp=5; IntAct=EBI-12143041, EBI-723624; CC Q9HBY8-2; O15305: PMM2; NbExp=5; IntAct=EBI-12143041, EBI-10182608; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21865597}. Nucleus CC {ECO:0000269|PubMed:21865597}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=alpha; CC IsoId=Q9HBY8-2; Sequence=Displayed; CC Name=2; Synonyms=beta; CC IsoId=Q9HBY8-1; Sequence=VSP_060876; CC Name=3; CC IsoId=Q9HBY8-3; Sequence=VSP_060877; CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and pancreas, and CC at lower levels in brain. {ECO:0000269|PubMed:10548550}. CC -!- PTM: Activated by phosphorylation on Ser-356 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-193. CC {ECO:0000269|PubMed:10548550}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- CAUTION: Not regulated by serum or glucocorticoids. {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; AF169034; AAF12757.2; -; mRNA. DR EMBL; AF186470; AAG17012.1; -; mRNA. DR EMBL; AY987010; AAX88805.1; -; mRNA. DR EMBL; BT020098; AAV38901.1; -; mRNA. DR EMBL; Z98752; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014037; AAH14037.3; -; mRNA. DR EMBL; BC065511; AAH65511.1; -; mRNA. DR CCDS; CCDS13321.1; -. [Q9HBY8-2] DR RefSeq; NP_001186193.1; NM_001199264.1. [Q9HBY8-2] DR RefSeq; NP_057360.2; NM_016276.3. [Q9HBY8-2] DR RefSeq; NP_733794.1; NM_170693.2. [Q9HBY8-2] DR AlphaFoldDB; Q9HBY8; -. DR SMR; Q9HBY8; -. DR BioGRID; 115416; 42. DR IntAct; Q9HBY8; 20. DR STRING; 9606.ENSP00000340608; -. DR BindingDB; Q9HBY8; -. DR ChEMBL; CHEMBL5794; -. DR GuidetoPHARMACOLOGY; 1535; -. DR iPTMnet; Q9HBY8; -. DR PhosphoSitePlus; Q9HBY8; -. DR BioMuta; SGK2; -. DR DMDM; 28558166; -. DR jPOST; Q9HBY8; -. DR MassIVE; Q9HBY8; -. DR MaxQB; Q9HBY8; -. DR PaxDb; 9606-ENSP00000340608; -. DR PeptideAtlas; Q9HBY8; -. DR ProteomicsDB; 81612; -. [Q9HBY8-1] DR ProteomicsDB; 81613; -. [Q9HBY8-2] DR ProteomicsDB; 81614; -. [Q9HBY8-3] DR Antibodypedia; 1638; 355 antibodies from 32 providers. DR DNASU; 10110; -. DR Ensembl; ENST00000341458.10; ENSP00000340608.5; ENSG00000101049.18. [Q9HBY8-2] DR Ensembl; ENST00000373100.7; ENSP00000362192.1; ENSG00000101049.18. [Q9HBY8-2] DR Ensembl; ENST00000423407.7; ENSP00000392795.3; ENSG00000101049.18. [Q9HBY8-2] DR Ensembl; ENST00000426287.3; ENSP00000412214.2; ENSG00000101049.18. [Q9HBY8-2] DR GeneID; 10110; -. DR KEGG; hsa:10110; -. DR MANE-Select; ENST00000373100.7; ENSP00000362192.1; NM_170693.3; NP_733794.1. DR UCSC; uc002xkr.4; human. [Q9HBY8-2] DR AGR; HGNC:13900; -. DR CTD; 10110; -. DR DisGeNET; 10110; -. DR GeneCards; SGK2; -. DR HGNC; HGNC:13900; SGK2. DR HPA; ENSG00000101049; Tissue enhanced (intestine, kidney, liver). DR MIM; 607589; gene. DR neXtProt; NX_Q9HBY8; -. DR OpenTargets; ENSG00000101049; -. DR VEuPathDB; HostDB:ENSG00000101049; -. DR eggNOG; KOG0598; Eukaryota. DR GeneTree; ENSGT00940000153776; -. DR InParanoid; Q9HBY8; -. DR OrthoDB; 3028764at2759; -. DR PhylomeDB; Q9HBY8; -. DR TreeFam; TF320906; -. DR PathwayCommons; Q9HBY8; -. DR Reactome; R-HSA-2672351; Stimuli-sensing channels. DR SignaLink; Q9HBY8; -. DR SIGNOR; Q9HBY8; -. DR BioGRID-ORCS; 10110; 13 hits in 1184 CRISPR screens. DR ChiTaRS; SGK2; human. DR GeneWiki; SGK2; -. DR GenomeRNAi; 10110; -. DR Pharos; Q9HBY8; Tchem. DR PRO; PR:Q9HBY8; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9HBY8; Protein. DR Bgee; ENSG00000101049; Expressed in mucosa of transverse colon and 143 other cell types or tissues. DR ExpressionAtlas; Q9HBY8; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0017080; F:sodium channel regulator activity; TAS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0032411; P:positive regulation of transporter activity; TAS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc. DR CDD; cd05603; STKc_SGK2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. 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; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR PANTHER; PTHR24351:SF222; SERUM_GLUCOCORTICOID REGULATED KINASE 2; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Genevisible; Q9HBY8; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..367 FT /note="Serine/threonine-protein kinase Sgk2" FT /id="PRO_0000086646" FT DOMAIN 35..292 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 293..367 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 68..78 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT ACT_SITE 159 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 41..49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 64 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R4U9" FT MOD_RES 193 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000269|PubMed:10548550" FT MOD_RES 334 FT /note="Phosphoserine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT MOD_RES 357 FT /note="Phosphotyrosine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT VAR_SEQ 1 FT /note="M -> MQGLLTSGRKPSGGGRCTGRGGWRGQWCLKPWMGGADPPTPTLSCLL FT LPVPPELPDHCYRM (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_060876" FT VAR_SEQ 1 FT /note="M -> MQGLLTSGRKPSGGGRCTELPDHCYRM (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_060877" FT VARIANT 199 FT /note="E -> K (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041074" FT VARIANT 289 FT /note="H -> Y (in dbSNP:rs35793869)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041075" FT MUTAGEN 356 FT /note="S->D: Increased activation." FT /evidence="ECO:0000269|PubMed:10548550" FT CONFLICT 108 FT /note="K -> E (in Ref. 2; AAX88805)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="G -> D (in Ref. 3; AAV38901)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="L -> P (in Ref. 2; AAX88805)" FT /evidence="ECO:0000305" FT VARIANT Q9HBY8-1:12 FT /note="S -> T (in dbSNP:rs33969356)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_083966" SQ SEQUENCE 367 AA; 41175 MW; E53F1ABE253F648B CRC64; MNSSPAGTPS PQPSRANGNI NLGPSANPNA QPTDFDFLKV IGKGNYGKVL LAKRKSDGAF YAVKVLQKKS ILKKKEQSHI MAERSVLLKN VRHPFLVGLR YSFQTPEKLY FVLDYVNGGE LFFHLQRERR FLEPRARFYA AEVASAIGYL HSLNIIYRDL KPENILLDCQ GHVVLTDFGL CKEGVEPEDT TSTFCGTPEY LAPEVLRKEP YDRAVDWWCL GAVLYEMLHG LPPFYSQDVS QMYENILHQP LQIPGGRTVA ACDLLQSLLH KDQRQRLGSK ADFLEIKNHV FFSPINWDDL YHKRLTPPFN PNVTGPADLK HFDPEFTQEA VSKSIGCTPD TVASSSGASS AFLGFSYAPE DDDILDC //