ULK2_MOUSE
ID ULK2_MOUSE Reviewed; 1037 AA.
AC Q9QY01; Q80TV7; Q9WTP4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase ULK2;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase Unc51.2;
DE AltName: Full=Unc-51-like kinase 2;
GN Name=Ulk2; Synonyms=Kiaa0623;
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], AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10624947; DOI=10.1016/s0896-6273(00)81031-4;
RA Tomoda T., Bhatt R.S., Kuroyanagi H., Shirasawa T., Hatten M.E.;
RT "A mouse serine/threonine kinase homologous to C. elegans UNC51 functions
RT in parallel fiber formation of cerebellar granule neurons.";
RL Neuron 24:833-846(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND AUTOPHOSPHORYLATION.
RX PubMed=10557072; DOI=10.1038/sj.onc.1202988;
RA Yan J., Kuroyanagi H., Tomemori T., Okazaki N., Asato K., Matsuda Y.,
RA Suzuki Y., Ohshima Y., Mitani S., Masuho Y., Shirasawa T., Muramatsu M.;
RT "Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique
RT features of functional domains.";
RL Oncogene 18:5850-5859(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 SYNGAP1.
RX PubMed=15014045; DOI=10.1101/gad.1151204;
RA Tomoda T., Kim J.H., Zhan C., Hatten M.E.;
RT "Role of Unc51.1 and its binding partners in CNS axon outgrowth.";
RL Genes Dev. 18:541-558(2004).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF FRS2 AND FRS3.
RX PubMed=16887332; DOI=10.1016/j.cellsig.2006.06.003;
RA Avery A.W., Figueroa C., Vojtek A.B.;
RT "UNC-51-like kinase regulation of fibroblast growth factor receptor
RT substrate 2/3.";
RL Cell. Signal. 19:177-184(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RB1CC1, AND MUTAGENESIS OF
RP LYS-39.
RX PubMed=18443221; DOI=10.1083/jcb.200712064;
RA Hara T., Takamura A., Kishi C., Iemura S., Natsume T., Guan J.L.,
RA Mizushima N.;
RT "FIP200, a ULK-interacting protein, is required for autophagosome formation
RT in mammalian cells.";
RL J. Cell Biol. 181:497-510(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-772 AND SER-781, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF AMPK.
RX PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [12]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=21258367; DOI=10.1038/ncb2152;
RA Kim J., Kundu M., Viollet B., Guan K.L.;
RT "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1.";
RL Nat. Cell Biol. 13:132-141(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in autophagy in
CC response to starvation. Acts upstream of phosphatidylinositol 3-kinase
CC PIK3C3 to regulate the formation of autophagophores, the precursors of
CC autophagosomes. Part of regulatory feedback loops in autophagy: acts
CC both as a downstream effector and a negative regulator of mammalian
CC target of rapamycin complex 1 (mTORC1) via interaction with RPTOR.
CC Activated via phosphorylation by AMPK, also acts as a negative
CC regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1,
CC PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and
CC RPTOR; however such data need additional evidences. Not involved in
CC ammonia-induced autophagy or in autophagic response of cerebellar
CC granule neurons (CGN) to low potassium concentration. Plays a role
CC early in neuronal differentiation and is required for granule cell axon
CC formation: may govern axon formation via Ras-like GTPase signaling and
CC through regulation of the Rab5-mediated endocytic pathways within
CC developing axons. {ECO:0000269|PubMed:10624947,
CC ECO:0000269|PubMed:16887332, ECO:0000269|PubMed:18443221,
CC ECO:0000269|PubMed:21460634}.
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 -!- SUBUNIT: Component of a complex consisting of ATG13/KIAA0652, ULK1 and
CC RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652.
CC Associates with the mammalian target of rapamycin complex 1 (mTORC1)
CC through an interaction with RPTOR (By similarity). Interacts with
CC SYNGAP1. {ECO:0000250, ECO:0000269|PubMed:15014045,
CC ECO:0000269|PubMed:18443221}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:18443221}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18443221}. Note=Localizes to pre-autophagosomal
CC membrane.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10557072}.
CC -!- DOMAIN: The CTD-like region mediates membrane-binding and incorporation
CC into large protein complexes. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. In response to nutrient limitation, probably
CC phosphorylated and activated by AMPK, leading to activate autophagy.
CC {ECO:0000269|PubMed:21258367}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65613.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF145922; AAF18325.1; -; mRNA.
DR EMBL; AB019577; BAA77341.1; -; mRNA.
DR EMBL; AK146620; BAE27309.1; -; mRNA.
DR EMBL; AK122331; BAC65613.2; ALT_INIT; mRNA.
DR EMBL; BC046778; AAH46778.1; -; mRNA.
DR EMBL; BC053029; AAH53029.1; -; mRNA.
DR CCDS; CCDS24820.1; -.
DR RefSeq; NP_038909.3; NM_013881.4.
DR AlphaFoldDB; Q9QY01; -.
DR SMR; Q9QY01; -.
DR BioGRID; 205934; 10.
DR DIP; DIP-60901N; -.
DR IntAct; Q9QY01; 10.
DR MINT; Q9QY01; -.
DR STRING; 10090.ENSMUSP00000004920; -.
DR iPTMnet; Q9QY01; -.
DR PhosphoSitePlus; Q9QY01; -.
DR MaxQB; Q9QY01; -.
DR PaxDb; Q9QY01; -.
DR PRIDE; Q9QY01; -.
DR ProteomicsDB; 298125; -.
DR Antibodypedia; 2063; 570 antibodies from 32 providers.
DR DNASU; 29869; -.
DR Ensembl; ENSMUST00000004920; ENSMUSP00000004920; ENSMUSG00000004798.
DR GeneID; 29869; -.
DR KEGG; mmu:29869; -.
DR UCSC; uc007jih.2; mouse.
DR CTD; 9706; -.
DR MGI; MGI:1352758; Ulk2.
DR VEuPathDB; HostDB:ENSMUSG00000004798; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000157588; -.
DR HOGENOM; CLU_011264_0_0_1; -.
DR InParanoid; Q9QY01; -.
DR OMA; RIKIVCE; -.
DR OrthoDB; 1084750at2759; -.
DR PhylomeDB; Q9QY01; -.
DR TreeFam; TF324551; -.
DR BioGRID-ORCS; 29869; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Ulk2; mouse.
DR PRO; PR:Q9QY01; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QY01; protein.
DR Bgee; ENSMUSG00000004798; Expressed in triceps brachii and 255 other tissues.
DR Genevisible; Q9QY01; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016237; Ser/Thr_kin_STPK_Ulk-1/2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR022708; Ser/Thr_kinase_C.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF12063; DUF3543; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000580; Ser/Thr_PK_STPK_ULK-1/2; 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; Autophagy; Cytoplasmic vesicle; Kinase; Membrane;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1037
FT /note="Serine/threonine-protein kinase ULK2"
FT /id="PRO_0000086783"
FT DOMAIN 9..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..1037
FT /note="CTD-like region"
FT /evidence="ECO:0000250"
FT COMPBIAS 455..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 39
FT /note="K->T: Decreased kinase activity."
FT /evidence="ECO:0000269|PubMed:18443221"
FT CONFLICT 998
FT /note="L -> V (in Ref. 2; BAA77341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1037 AA; 112877 MW; 2E7DC3B0B87E9607 CRC64;
MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ ILLGKEIKIL
KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK GTLSEDTIRV FLHQIAAAMR
ILHSKGIIHR DLKPQNILLS YANRRKSNVS GIRIKIADFG FARYLHSNTM AATLCGSPMY
MAPEVIMSQH YDAKADLWSI GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET
SPYLANLLLG LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP
SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT DDFVLVPHNI
SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP IPVPTQVRNY QRIEQNLIST
ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL
VGTIPEQFSQ CCCGHPQGHE ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ
KLRKQHSDPV CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS
PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG SERHRSEQQQ
SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD VAPAGACGVM LALPAGTAAS
ARAVLFTVGS PPHSATAPTC THMVLRTRTT SVGSSSSGGS LCSASGRVCV GSPPGPGLGS
SPPGAEGAPS LRYVPYGASP PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC
VLDLTAVRGG NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL
HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK QRFIDEINSV
TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL EGLSKILQDP TDVENVHKYK
CSIERRLSAL CCSTATV
