TSSK2_HUMAN
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 03-AUG-2022, entry version 188.
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 -!- 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}.
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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; 12.
DR IntAct; Q96PF2; 21.
DR MINT; Q96PF2; -.
DR STRING; 9606.ENSP00000382544; -.
DR BindingDB; Q96PF2; -.
DR ChEMBL; CHEMBL6014; -.
DR GuidetoPHARMACOLOGY; 2258; -.
DR iPTMnet; Q96PF2; -.
DR PhosphoSitePlus; Q96PF2; -.
DR BioMuta; TSSK2; -.
DR DMDM; 30316269; -.
DR MassIVE; Q96PF2; -.
DR PaxDb; Q96PF2; -.
DR PeptideAtlas; Q96PF2; -.
DR PRIDE; Q96PF2; -.
DR ProteomicsDB; 77687; -.
DR Antibodypedia; 22857; 71 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 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; 1378245at2759; -.
DR PhylomeDB; Q96PF2; -.
DR TreeFam; TF352374; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q96PF2; -.
DR SignaLink; Q96PF2; -.
DR BioGRID-ORCS; 23617; 27 hits in 1043 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 102 other tissues.
DR ExpressionAtlas; Q96PF2; baseline and differential.
DR Genevisible; Q96PF2; HS.
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: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
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 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 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
