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   27-MAR-2024, entry version 172.
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; 11.
DR   DIP; DIP-60901N; -.
DR   IntAct; Q9QY01; 10.
DR   MINT; Q9QY01; -.
DR   STRING; 10090.ENSMUSP00000004920; -.
DR   GlyGen; Q9QY01; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9QY01; -.
DR   PhosphoSitePlus; Q9QY01; -.
DR   MaxQB; Q9QY01; -.
DR   PaxDb; 10090-ENSMUSP00000004920; -.
DR   ProteomicsDB; 298125; -.
DR   Antibodypedia; 2063; 589 antibodies from 32 providers.
DR   DNASU; 29869; -.
DR   Ensembl; ENSMUST00000004920.4; ENSMUSP00000004920.4; ENSMUSG00000004798.15.
DR   GeneID; 29869; -.
DR   KEGG; mmu:29869; -.
DR   UCSC; uc007jih.2; mouse.
DR   AGR; MGI:1352758; -.
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; SFFSHPF; -.
DR   OrthoDB; 8335at2759; -.
DR   PhylomeDB; Q9QY01; -.
DR   TreeFam; TF324551; -.
DR   BioGRID-ORCS; 29869; 5 hits in 80 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 258 other cell types or tissues.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
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:0048675; P:axon extension; IMP:MGI.
DR   GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:MGI.
DR   GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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: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   CDD; cd14201; STKc_ULK2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR048941; ATG1-like_MIT2.
DR   InterPro; IPR022708; Atg1-like_tMIT.
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   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   PANTHER; PTHR24348:SF18; SERINE_THREONINE-PROTEIN KINASE ULK2; 1.
DR   Pfam; PF12063; ATG1-like_MIT1; 1.
DR   Pfam; PF21127; ATG1-like_MIT2; 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; 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; Q9QY01; MM.
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
//