NEK2_MOUSE
ID NEK2_MOUSE Reviewed; 443 AA.
AC O35942; O35959; Q3TPD7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine/threonine-protein kinase Nek2;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 2;
DE Short=NimA-related protein kinase 2;
GN Name=Nek2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Testis;
RX PubMed=9187143; DOI=10.1242/dev.124.11.2167;
RA Rhee K., Wolgemuth D.J.;
RT "The NIMA-related kinase 2, Nek2, is expressed in specific stages of the
RT meiotic cell cycle and associates with meiotic chromosomes.";
RL Development 124:2167-2177(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9583679; DOI=10.1038/sj.onc.1201710;
RA Arama E., Yanai A., Kilfin G., Motro B.;
RT "Murine NIMA-related kinases are expressed in patterns suggesting distinct
RT functions in gametogenesis and a role in the nervous system.";
RL Oncogene 16:1813-1823(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9434622; DOI=10.1006/excr.1997.3788;
RA Tanaka K., Parvinen M., Nigg E.A.;
RT "The in vivo expression pattern of mouse Nek2, a NIMA-related kinase,
RT indicates a role in both mitosis and meiosis.";
RL Exp. Cell Res. 237:264-274(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Heart;
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 [5]
RP FUNCTION, AND INTERACTION WITH NECAB3.
RX PubMed=14697346; DOI=10.1016/j.yexcr.2003.09.025;
RA Yoo J.C., Chang J.R., Kim S.H., Jang S.K., Wolgemuth D.J., Kim K., Rhee K.;
RT "NIP1/XB51/NECAB3 is a potential substrate of Nek2, suggesting specific
RT roles of Nek2 in Golgi.";
RL Exp. Cell Res. 292:393-402(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH HMGA2.
RX PubMed=14668482; DOI=10.1091/mbc.e03-09-0638;
RA Di Agostino S., Fedele M., Chieffi P., Fusco A., Rossi P., Geremia R.,
RA Sette C.;
RT "Phosphorylation of high-mobility group protein A2 by Nek2 kinase during
RT the first meiotic division in mouse spermatocytes.";
RL Mol. Biol. Cell 15:1224-1232(2004).
CC -!- FUNCTION: Protein kinase which is involved in the control of centrosome
CC separation and bipolar spindle formation in mitotic cells and chromatin
CC condensation in meiotic cells. Regulates centrosome separation
CC (essential for the formation of bipolar spindles and high-fidelity
CC chromosome separation) by phosphorylating centrosomal proteins such as
CC CROCC, CEP250 and NINL, resulting in their displacement from the
CC centrosomes. Regulates kinetochore microtubule attachment stability in
CC mitosis via phosphorylation of NDC80. Involved in regulation of mitotic
CC checkpoint protein complex via phosphorylation of CDC20 and MAD2L1.
CC Plays an active role in chromatin condensation during the first meiotic
CC division through phosphorylation of HMGA2. Phosphorylates: PPP1CC;
CC SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to
CC kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68
CC and CNTLN directly or indirectly (By similarity). NEK2-mediated
CC phosphorylation of CEP68 promotes CEP68 dissociation from the
CC centrosome and its degradation at the onset of mitosis (By similarity).
CC Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in
CC the regulation of centrosome disjunction (By similarity).
CC {ECO:0000250|UniProtKB:P51955, ECO:0000269|PubMed:14668482,
CC ECO:0000269|PubMed:14697346}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Its catalytic activity is inhibited by the
CC inhibitor CCT241950. In the presence of this inhibitor, displays an
CC autoinhibited conformation: Tyr-70 side chain points into the active
CC site, interacts with the activation loop, and blocks the alphaC helix.
CC {ECO:0000250|UniProtKB:P51955}.
CC -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with CDC20,
CC CTNB1, MAD1L1, MAD2L1, MAPK, NEK11, NPM1, NDC80, PCNT, PPP1CA, PPP1CC
CC and SGO1. Interacts with STK3/MST2 (via SARAH domain) and SAV1 (via
CC SARAH domain) (By similarity). Interacts with NECAB3 and HMGA2
CC (PubMed:14697346, PubMed:14668482). Interacts with CEP68; the
CC interaction leads to phosphorylation of CEP68. Interacts with CNTLN;
CC the interaction leads to phosphorylation of CNTLN. Interacts with CEP85
CC (By similarity). {ECO:0000250|UniProtKB:P51955,
CC ECO:0000269|PubMed:14668482, ECO:0000269|PubMed:14697346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9187143}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P51955}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P51955}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC Chromosome, centromere {ECO:0000269|PubMed:9187143}. Note=STK3/MST2 and
CC SAV1 are required for its targeting to the centrosome. Colocalizes with
CC SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in
CC the interphase but becomes associated with it upon the breakdown of the
CC nuclear envelope. Has a nucleolar targeting/ retention activity via a
CC coiled-coil domain at the C-terminal end (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in testis. Low levels
CC found in mid-gestation embryo, ovary, placenta, intestine, thymus and
CC skin. Within the testis, expression restricted to germ cells with
CC highest levels detected in spermatocytes at pachytene and diplotene
CC stages. Also expressed in meiotic pachytene oocytes.
CC {ECO:0000269|PubMed:9187143, ECO:0000269|PubMed:9434622}.
CC -!- DOMAIN: The leucine-zipper domain is required for its dimerization and
CC activation. {ECO:0000250|UniProtKB:P51955}.
CC -!- PTM: Activated by autophosphorylation. Protein phosphatase 1 represses
CC autophosphorylation and activation of isoform 1 by dephosphorylation.
CC Phosphorylation by STK3/MST2 is necessary for its localization to the
CC centrosome. {ECO:0000250|UniProtKB:P51955}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; U95610; AAB67973.1; -; mRNA.
DR EMBL; AF013166; AAC35393.1; -; mRNA.
DR EMBL; AF007247; AAB70470.1; -; mRNA.
DR EMBL; AK147072; BAE27653.1; -; mRNA.
DR EMBL; AK164467; BAE37799.1; -; mRNA.
DR CCDS; CCDS15623.1; -.
DR RefSeq; NP_035022.2; NM_010892.3.
DR AlphaFoldDB; O35942; -.
DR SMR; O35942; -.
DR BioGRID; 201728; 38.
DR IntAct; O35942; 37.
DR STRING; 10090.ENSMUSP00000027931; -.
DR iPTMnet; O35942; -.
DR PhosphoSitePlus; O35942; -.
DR MaxQB; O35942; -.
DR PaxDb; O35942; -.
DR PRIDE; O35942; -.
DR ProteomicsDB; 252945; -.
DR Antibodypedia; 4308; 464 antibodies from 38 providers.
DR DNASU; 18005; -.
DR Ensembl; ENSMUST00000027931; ENSMUSP00000027931; ENSMUSG00000026622.
DR GeneID; 18005; -.
DR KEGG; mmu:18005; -.
DR UCSC; uc007ecx.2; mouse.
DR CTD; 4751; -.
DR MGI; MGI:109359; Nek2.
DR VEuPathDB; HostDB:ENSMUSG00000026622; -.
DR eggNOG; KOG1826; Eukaryota.
DR GeneTree; ENSGT00940000156989; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O35942; -.
DR OMA; PSRPEDY; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; O35942; -.
DR TreeFam; TF101184; -.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 18005; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Nek2; mouse.
DR PRO; PR:O35942; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35942; protein.
DR Bgee; ENSMUSG00000026622; Expressed in spermatocyte and 62 other tissues.
DR Genevisible; O35942; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
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:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051299; P:centrosome separation; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:MGI.
DR GO; GO:1903126; P:negative regulation of centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinase;
KW Kinetochore; Magnesium; Meiosis; Metal-binding; Microtubule; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..443
FT /note="Serine/threonine-protein kinase Nek2"
FT /id="PRO_0000086422"
FT DOMAIN 8..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 264..443
FT /note="Interaction with PCNT"
FT /evidence="ECO:0000250"
FT REGION 282..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..443
FT /note="Interaction with CEP85"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT REGION 306..334
FT /note="Leucine-zipper"
FT REGION 329..443
FT /note="Necessary for interaction with MAD1L1"
FT /evidence="ECO:0000250"
FT REGION 333..370
FT /note="Required for microtubule binding and for
FT localization to the centrosomes"
FT /evidence="ECO:0000250"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..437
FT /note="Interaction with SAV1 and STK3/MST2"
FT /evidence="ECO:0000250"
FT COILED 303..361
FT /evidence="ECO:0000255"
FT COILED 403..427
FT /evidence="ECO:0000255"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 170
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 171
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 179
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 241
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 356
FT /note="Phosphoserine; by STK3/MST2"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT MOD_RES 436
FT /note="Phosphoserine; by STK3/MST2"
FT /evidence="ECO:0000250|UniProtKB:P51955"
FT CONFLICT 69
FT /note="S -> R (in Ref. 1; AAB67973, 2; AAC35393 and 3;
FT AAB70470)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="G -> A (in Ref. 1; AAB67973)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="N -> F (in Ref. 1; AAB67973)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="L -> M (in Ref. 1; AAB67973, 2; AAC35393 and 3;
FT AAB70470)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> S (in Ref. 1; AAB67973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51243 MW; 1EF2CA320F60FB5C CRC64;
MPSRVEDYEV LHSIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEVEKQ MLVSEVNLLR
ELKHPNIVSY YDRIIDRTNT TLYIVMEYCE GGDLASVISK GTKDRQYLEE EFVLRVMTQL
TLALKECHRR SDGGHTVLHR DLKPANVFLD SKHNVKLGDF GLARILNHDT SFAKTFVGTP
YYMSPEQMSC LSYNEKSDIW SLGCLLYELC ALMPPFTAFN QKELAGKIRE GRFRRIPYRY
SDGLNDLITR MLNLKDYHRP SVEEILESPL IADLVAEEQR RNLERRGRRS GEPSKLPDSS
PVLSELKLKE RQLQDREQAL RAREDILEQK ERELCIRERL AEDKLARAES LMKNYSLLKE
HRLLCLAGGP ELDLPSSAMK KKVHFHGESK ENTARSENSE SYLAKSKCRD LKKRLHAAQL
RAQALADIEK NYQLKSRQIL GMR
