ID ILKAP_HUMAN Reviewed; 392 AA. AC Q9H0C8; B3KM39; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Integrin-linked kinase-associated serine/threonine phosphatase 2C; DE Short=ILKAP; DE EC=3.1.3.16; GN Name=ILKAP; 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], COFACTOR, INTERACTION WITH ILK, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF ASP-152 AND RP HIS-154, AND POSSIBLE FUNCTION. RX PubMed=11331582; DOI=10.1093/emboj/20.9.2160; RA Leung-Hagesteijn C., Mahendra A., Naruszewicz I., Hannigan G.E.; RT "Modulation of integrin signal transduction by ILKAP, a protein phosphatase RT 2C associating with the integrin-linked kinase, ILK1."; RL EMBO J. 20:2160-2170(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-66. RC TISSUE=Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 [7] RP INTERACTION WITH ILK, ROLE IN ONCOGENIC TRANSFORMATION, AND POSSIBLE RP FUNCTION. RX PubMed=14990992; DOI=10.1038/sj.onc.1207473; RA Kumar A.S., Naruszewicz I., Wang P., Leung-Hagesteijn C., Hannigan G.E.; RT "ILKAP regulates ILK signaling and inhibits anchorage-independent growth."; RL Oncogene 23:3454-3461(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-210, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-13, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-13, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Protein phosphatase that may play a role in regulation of CC cell cycle progression via dephosphorylation of its substrates whose CC appropriate phosphorylation states might be crucial for cell CC proliferation. Selectively associates with integrin linked kinase CC (ILK), to modulate cell adhesion and growth factor signaling. Inhibits CC the ILK-GSK3B signaling axis and may play an important role in CC inhibiting oncogenic transformation. {ECO:0000269|PubMed:14990992}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited rather than stimulated by magnesium. CC -!- SUBUNIT: Interacts with ILK. Specific association with ILK is CC independent of the catalytic activity of either partner. CC {ECO:0000269|PubMed:11331582, ECO:0000269|PubMed:14990992}. CC -!- INTERACTION: CC Q9H0C8; Q13418: ILK; NbExp=3; IntAct=EBI-2620298, EBI-747644; CC Q9H0C8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2620298, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331582}. CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels expressed in CC striated muscle. Much lower levels evident in various smooth muscle CC tissues. {ECO:0000269|PubMed:11331582}. CC -!- SIMILARITY: Belongs to the PP2C family. {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; AY024365; AAK07736.1; -; mRNA. DR EMBL; AL136850; CAB66784.1; -; mRNA. DR EMBL; CR533533; CAG38564.1; -; mRNA. DR EMBL; AK001043; BAG50851.1; -; mRNA. DR EMBL; AC016757; AAY24336.1; -; Genomic_DNA. DR EMBL; BC006576; AAH06576.1; -; mRNA. DR CCDS; CCDS2526.1; -. DR RefSeq; NP_110395.1; NM_030768.2. DR AlphaFoldDB; Q9H0C8; -. DR SMR; Q9H0C8; -. DR BioGRID; 123343; 115. DR IntAct; Q9H0C8; 46. DR MINT; Q9H0C8; -. DR STRING; 9606.ENSP00000254654; -. DR DEPOD; ILKAP; -. DR GlyGen; Q9H0C8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H0C8; -. DR MetOSite; Q9H0C8; -. DR PhosphoSitePlus; Q9H0C8; -. DR SwissPalm; Q9H0C8; -. DR BioMuta; ILKAP; -. DR DMDM; 74752560; -. DR EPD; Q9H0C8; -. DR jPOST; Q9H0C8; -. DR MassIVE; Q9H0C8; -. DR MaxQB; Q9H0C8; -. DR PaxDb; 9606-ENSP00000254654; -. DR PeptideAtlas; Q9H0C8; -. DR ProteomicsDB; 80254; -. DR Pumba; Q9H0C8; -. DR Antibodypedia; 1494; 340 antibodies from 31 providers. DR DNASU; 80895; -. DR Ensembl; ENST00000254654.8; ENSP00000254654.3; ENSG00000132323.9. DR GeneID; 80895; -. DR KEGG; hsa:80895; -. DR MANE-Select; ENST00000254654.8; ENSP00000254654.3; NM_030768.3; NP_110395.1. DR UCSC; uc002vxv.4; human. DR AGR; HGNC:15566; -. DR CTD; 80895; -. DR DisGeNET; 80895; -. DR GeneCards; ILKAP; -. DR HGNC; HGNC:15566; ILKAP. DR HPA; ENSG00000132323; Low tissue specificity. DR MIM; 618909; gene. DR neXtProt; NX_Q9H0C8; -. DR OpenTargets; ENSG00000132323; -. DR PharmGKB; PA29856; -. DR VEuPathDB; HostDB:ENSG00000132323; -. DR eggNOG; KOG0698; Eukaryota. DR GeneTree; ENSGT00940000157403; -. DR InParanoid; Q9H0C8; -. DR OMA; TYEDEFF; -. DR OrthoDB; 202023at2759; -. DR PhylomeDB; Q9H0C8; -. DR TreeFam; TF313513; -. DR PathwayCommons; Q9H0C8; -. DR SignaLink; Q9H0C8; -. DR BioGRID-ORCS; 80895; 10 hits in 1170 CRISPR screens. DR ChiTaRS; ILKAP; human. DR GeneWiki; ILKAP; -. DR GenomeRNAi; 80895; -. DR Pharos; Q9H0C8; Tbio. DR PRO; PR:Q9H0C8; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9H0C8; Protein. DR Bgee; ENSG00000132323; Expressed in cerebellar hemisphere and 195 other cell types or tissues. DR ExpressionAtlas; Q9H0C8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR47992:SF105; PROTEIN PHOSPHATASE 1B; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q9H0C8; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; KW Phosphoprotein; Protein phosphatase; Reference proteome. FT CHAIN 1..392 FT /note="Integrin-linked kinase-associated serine/threonine FT phosphatase 2C" FT /id="PRO_0000272271" FT DOMAIN 108..390 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 1..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 57..71 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..90 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 152 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 153 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 326 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 381 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 210 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 66 FT /note="I -> M (in dbSNP:rs34371548)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_061542" FT MUTAGEN 152 FT /note="D->A: Loss of >90% of activity." FT /evidence="ECO:0000269|PubMed:11331582" FT MUTAGEN 154 FT /note="H->D: Loss of >90% of activity." FT /evidence="ECO:0000269|PubMed:11331582" FT MUTAGEN 154 FT /note="H->L: Loss of >90% of activity." FT /evidence="ECO:0000269|PubMed:11331582" SQ SEQUENCE 392 AA; 42907 MW; AF6ACC98508CBEA3 CRC64; MDLFGDLPEP ERSPRPAAGK EAQKGPLLFD DLPPASSTDS GSGGPLLFDD LPPASSGDSG SLATSISQMV KTEGKGAKRK TSEEEKNGSE ELVEKKVCKA SSVIFGLKGY VAERKGEREE MQDAHVILND ITEECRPPSS LITRVSYFAV FDGHGGIRAS KFAAQNLHQN LIRKFPKGDV ISVEKTVKRC LLDTFKHTDE EFLKQASSQK PAWKDGSTAT CVLAVDNILY IANLGDSRAI LCRYNEESQK HAALSLSKEH NPTQYEERMR IQKAGGNVRD GRVLGVLEVS RSIGDGQYKR CGVTSVPDIR RCQLTPNDRF ILLACDGLFK VFTPEEAVNF ILSCLEDEKI QTREGKSAAD ARYEAACNRL ANKAVQRGSA DNVTVMVVRI GH //