ID TSSK2_HUMAN Reviewed; 358 AA. AC Q96PF2; Q8IY55; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 30-APR-2003, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=Testis-specific serine/threonine-protein kinase 2; DE Short=TSK-2; DE Short=TSK2; DE Short=TSSK-2; DE Short=Testis-specific kinase 2; DE EC=2.7.11.1 {ECO:0000269|PubMed:20729278}; DE AltName: Full=DiGeorge syndrome protein G; DE Short=DGS-G; DE AltName: Full=Serine/threonine-protein kinase 22B; GN Name=TSSK2; Synonyms=DGSG, SPOGA2, STK22B; 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]. RX PubMed=8776594; DOI=10.1093/hmg/5.6.789; RA Gong W., Emanuel B.S., Collins J., Kim D.H., Wang Z., Chen F., Zhang G., RA Roe B., Budarf M.L.; RT "A transcription map of the DiGeorge and velo-cardio-facial syndrome RT minimal critical region on 22q11."; RL Hum. Mol. Genet. 5:789-800(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, TISSUE RP SPECIFICITY, AND INTERACTION WITH TSSK1B. RX PubMed=15044604; DOI=10.1093/molehr/gah052; RA Hao Z., Jha K.N., Kim Y.H., Vemuganti S., Westbrook V.A., Chertihin O., RA Markgraf K., Flickinger C.J., Coppola M., Herr J.C., Visconti P.E.; RT "Expression analysis of the human testis-specific serine/threonine kinase RT (TSSK) homologues. A TSSK member is present in the equatorial segment of RT human sperm."; RL Mol. Hum. Reprod. 10:433-444(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 PUTATIVE CONTRACEPTIVE TARGET. RX PubMed=17566264; RA Xu B., Hao Z., Jha K.N., Digilio L., Urekar C., Kim Y.H., Pulido S., RA Flickinger C.J., Herr J.C.; RT "Validation of a testis specific serine/threonine kinase [TSSK] family and RT the substrate of TSSK1 & 2, TSKS, as contraceptive targets."; RL Soc. Reprod. Fertil. Suppl. 63:87-101(2007). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=18495105; DOI=10.1016/j.ydbio.2008.03.043; RA Xu B., Hao Z., Jha K.N., Zhang Z., Urekar C., Digilio L., Pulido S., RA Strauss J.F. III, Flickinger C.J., Herr J.C.; RT "TSKS concentrates in spermatid centrioles during flagellogenesis."; RL Dev. Biol. 319:201-210(2008). RN [8] RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH TSKS. RX PubMed=18533145; DOI=10.1016/j.ydbio.2008.03.047; RA Xu B., Hao Z., Jha K.N., Zhang Z., Urekar C., Digilio L., Pulido S., RA Strauss J.F. III, Flickinger C.J., Herr J.C.; RT "Targeted deletion of Tssk1 and 2 causes male infertility due to RT haploinsufficiency."; RL Dev. Biol. 319:211-222(2008). RN [9] RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AUTOPHOSPHORYLATION, RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=20729278; DOI=10.1093/molehr/gaq071; RA Li Y., Sosnik J., Brassard L., Reese M., Spiridonov N.A., Bates T.C., RA Johnson G.R., Anguita J., Visconti P.E., Salicioni A.M.; RT "Expression and localization of five members of the testis-specific serine RT kinase (Tssk) family in mouse and human sperm and testis."; RL Mol. Hum. Reprod. 17:42-56(2011). RN [10] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-27; VAL-61; CYS-197 AND MET-280. 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). RN [11] RP CHARACTERIZATION OF VARIANT ARG-27. RX PubMed=19926886; DOI=10.2164/jandrol.109.008466; RA Zhang H., Su D., Yang Y., Zhang W., Liu Y., Bai G., Ma M., Ma Y., Zhang S.; RT "Some single-nucleotide polymorphisms of the TSSK2 gene may be associated RT with human spermatogenesis impairment."; RL J. Androl. 31:388-392(2010). CC -!- FUNCTION: Testis-specific serine/threonine-protein kinase required CC during spermatid development. Phosphorylates TSKS at 'Ser-288' and CC SPAG16. Involved in the late stages of spermatogenesis, during the CC reconstruction of the cytoplasm. During spermatogenesis, required for CC the transformation of a ring-shaped structure around the base of the CC flagellum originating from the chromatoid body. CC {ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:18533145, CC ECO:0000269|PubMed:20729278}. 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 Evidence={ECO:0000269|PubMed:20729278}; 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; Evidence={ECO:0000269|PubMed:20729278}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20729278}; CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-174, CC potentially by autophosphorylation. {ECO:0000250}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10 uM for ATP {ECO:0000269|PubMed:20729278}; CC -!- SUBUNIT: Interacts with TSSK1B. Interacts with HSP90; this interaction CC stabilizes TSSK2 (By similarity). {ECO:0000250|UniProtKB:O54863, CC ECO:0000269|PubMed:15044604, ECO:0000269|PubMed:18533145}. CC -!- INTERACTION: CC Q96PF2; Q4G0N7: FAM229B; NbExp=3; IntAct=EBI-852089, EBI-18340430; CC Q96PF2; P08238: HSP90AB1; NbExp=2; IntAct=EBI-852089, EBI-352572; CC Q96PF2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-852089, EBI-741037; CC Q96PF2; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-852089, EBI-372432; CC Q96PF2; Q9UJT2: TSKS; NbExp=9; IntAct=EBI-852089, EBI-852101; CC Q96PF2; Q9UJT2-2: TSKS; NbExp=2; IntAct=EBI-852089, EBI-852113; CC Q96PF2; P62258: YWHAE; NbExp=2; IntAct=EBI-852089, EBI-356498; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome, centriole CC {ECO:0000269|PubMed:18495105}. Note=Present in the cytoplasm of CC elongating spermatids. In spermatozoa, localizes in the equatorial CC segment, neck, the midpiece and in a specific sperm head compartment CC (By similarity). In spermatids, concentrates in centrioles during CC flagellogenesis. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Testis-specific. Present in mature spermatozoa (at CC protein level). {ECO:0000269|PubMed:15044604, CC ECO:0000269|PubMed:18533145, ECO:0000269|PubMed:20729278}. CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15044604}. CC -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination CC and degradation. {ECO:0000250|UniProtKB:O54863}. CC -!- MISCELLANEOUS: TSSK1B might be used as a target for male contraception CC or and intra-vaginal spermicides. {ECO:0000305|PubMed:17566264}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase 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; L77564; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF362953; AAK98531.1; -; mRNA. DR EMBL; CR456587; CAG30473.1; -; mRNA. DR EMBL; AC004471; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC037781; AAH37781.1; -; mRNA. DR CCDS; CCDS13755.1; -. DR RefSeq; NP_443732.3; NM_053006.4. DR AlphaFoldDB; Q96PF2; -. DR SMR; Q96PF2; -. DR BioGRID; 117150; 25. DR IntAct; Q96PF2; 23. DR MINT; Q96PF2; -. DR STRING; 9606.ENSP00000382544; -. DR BindingDB; Q96PF2; -. DR ChEMBL; CHEMBL6014; -. DR GuidetoPHARMACOLOGY; 2258; -. DR GlyGen; Q96PF2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96PF2; -. DR PhosphoSitePlus; Q96PF2; -. DR BioMuta; TSSK2; -. DR DMDM; 30316269; -. DR MassIVE; Q96PF2; -. DR PaxDb; 9606-ENSP00000382544; -. DR PeptideAtlas; Q96PF2; -. DR ProteomicsDB; 77687; -. DR Antibodypedia; 22857; 75 antibodies from 15 providers. DR DNASU; 23617; -. DR Ensembl; ENST00000399635.4; ENSP00000382544.2; ENSG00000206203.5. DR GeneID; 23617; -. DR KEGG; hsa:23617; -. DR MANE-Select; ENST00000399635.4; ENSP00000382544.2; NM_053006.5; NP_443732.3. DR UCSC; uc002zow.2; human. DR AGR; HGNC:11401; -. DR CTD; 23617; -. DR DisGeNET; 23617; -. DR GeneCards; TSSK2; -. DR HGNC; HGNC:11401; TSSK2. DR HPA; ENSG00000206203; Tissue enriched (testis). DR MIM; 610710; gene. DR neXtProt; NX_Q96PF2; -. DR OpenTargets; ENSG00000206203; -. DR PharmGKB; PA36208; -. DR VEuPathDB; HostDB:ENSG00000206203; -. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00940000162226; -. DR HOGENOM; CLU_000288_63_0_1; -. DR InParanoid; Q96PF2; -. DR OMA; WMQPPKP; -. DR OrthoDB; 227821at2759; -. DR PhylomeDB; Q96PF2; -. DR TreeFam; TF352374; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; Q96PF2; -. DR SignaLink; Q96PF2; -. DR BioGRID-ORCS; 23617; 28 hits in 1104 CRISPR screens. DR GeneWiki; TSSK2; -. DR GenomeRNAi; 23617; -. DR Pharos; Q96PF2; Tchem. DR PRO; PR:Q96PF2; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q96PF2; Protein. DR Bgee; ENSG00000206203; Expressed in left testis and 104 other cell types or tissues. DR ExpressionAtlas; Q96PF2; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0032007; P:negative regulation of TOR signaling; IBA:GO_Central. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB. DR CDD; cd14165; STKc_TSSK1_2-like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF100; TESTIS-SPECIFIC SERINE_THREONINE-PROTEIN KINASE 1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q96PF2; HS. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Cytoskeleton; Developmental protein; KW Differentiation; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Spermatogenesis; Transferase; Ubl conjugation. FT CHAIN 1..358 FT /note="Testis-specific serine/threonine-protein kinase 2" FT /id="PRO_0000086768" FT DOMAIN 12..272 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 302..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..351 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 18..26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT VARIANT 27 FT /note="K -> R (may be associated with infertility; FT dbSNP:rs3747052)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:19926886" FT /id="VAR_041241" FT VARIANT 61 FT /note="M -> V (in dbSNP:rs35532431)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041242" FT VARIANT 197 FT /note="Y -> C (in dbSNP:rs56279111)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041243" FT VARIANT 244 FT /note="E -> K (in dbSNP:rs35048893)" FT /id="VAR_051677" FT VARIANT 245 FT /note="C -> S (in dbSNP:rs8140743)" FT /id="VAR_059770" FT VARIANT 280 FT /note="T -> M (in dbSNP:rs1052763)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041244" FT CONFLICT 279 FT /note="A -> P (in Ref. 2; AAK98531)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="G -> D (in Ref. 4; AAH37781)" FT /evidence="ECO:0000305" SQ SEQUENCE 358 AA; 40939 MW; F231433AA78B2FE9 CRC64; MDDATVLRKK GYIVGINLGK GSYAKVKSAY SERLKFNVAV KIIDRKKTPT DFVERFLPRE MDILATVNHG SIIKTYEIFE TSDGRIYIIM ELGVQGDLLE FIKCQGALHE DVARKMFRQL SSAVKYCHDL DIVHRDLKCE NLLLDKDFNI KLSDFGFSKR CLRDSNGRII LSKTFCGSAA YAAPEVLQSI PYQPKVYDIW SLGVILYIMV CGSMPYDDSD IRKMLRIQKE HRVDFPRSKN LTCECKDLIY RMLQPDVSQR LHIDEILSHS WLQPPKPKAT SSASFKREGE GKYRAECKLD TKTGLRPDHR PDHKLGAKTQ HRLLVVPENE NRMEDRLAET SRAKDHHISG AEVGKAST //