PEAK1_MOUSE
ID PEAK1_MOUSE Reviewed; 1735 AA.
AC Q69Z38; E9QKY2; Q8BX56; Q8R365;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Inactive tyrosine-protein kinase PEAK1 {ECO:0000305};
DE AltName: Full=Pseudopodium-enriched atypical kinase 1 {ECO:0000303|PubMed:20534451};
DE AltName: Full=Sugen kinase 269;
DE AltName: Full=Tyrosine-protein kinase SgK269;
GN Name=Peak1; Synonyms=Kiaa2002, Sgk269;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-991.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1026-1735.
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1534-1735.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632 AND TYR-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824; SER-825 AND THR-1141,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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 [9]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CSK.
RX PubMed=20534451; DOI=10.1073/pnas.0914776107;
RA Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA Yates J.R. III, Klemke R.L.;
RT "Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and
RT cancer progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
RN [10]
RP ERRATUM OF PUBMED:20534451.
RA Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA Yates J.R. III, Klemke R.L.;
RL Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
CC -!- FUNCTION: Probable catalytically inactive kinase. Scaffolding protein
CC that regulates the cytoskeleton to control cell spreading and migration
CC by modulating focal adhesion dynamics. Acts as a scaffold for mediating
CC EGFR signaling. {ECO:0000250|UniProtKB:Q9H792}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BCAR1 and CRK (By
CC similarity). Interacts with PRAG1 (By similarity). Interacts (when
CC phosphorylated at Tyr-1177) with SHC1 (via PID domain) (By similarity).
CC Found in a complex with PPP1CA, PPP1CC and SHC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H792}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20534451}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:20534451}. Note=Colocalizes with actin
CC (PubMed:20534451).
CC -!- DOMAIN: The dimerization region encompasses helices both from the
CC N- and C-terminal of the protein kinase domain.
CC {ECO:0000250|UniProtKB:Q9H792}.
CC -!- PTM: Phosphorylated on tyrosine in a CSK-dependent manner in response
CC to adhesion to fibronectin and to EGF stimulation (PubMed:20534451).
CC Phosphorylation at Tyr-662 by a Src family kinase controls subcellular
CC localization to focal adhesion and focal adhesion dynamics.
CC Phosphorylation at Tyr-1177 is essential for binding to SHC1.
CC {ECO:0000250|UniProtKB:Q9H792, ECO:0000269|PubMed:20534451}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Has been the subject of controversy surrounding its catalytic
CC capabilities. Early characterization of PEAK1 gave a weak in vitro
CC tyrosine kinase activity. The crystal structure indicates that the
CC kinase-domain contains a closed nucleotide-binding cleft that in this
CC conformation may deleteriously affect nucleotide bindin. Furthermore
CC PEAK1 is devoid of nucleotide binding activity, as detected by a
CC thermal-shift assay. So it seems probable that PEAK1 is an inactive
CC kinase. {ECO:0000250|UniProtKB:Q9H792}.
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DR EMBL; AC157474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK048912; BAC33490.1; -; mRNA.
DR EMBL; AK173328; BAD32606.1; -; mRNA.
DR EMBL; BC026466; AAH26466.1; -; mRNA.
DR CCDS; CCDS52804.1; -.
DR RefSeq; NP_766512.2; NM_172924.3.
DR RefSeq; XP_006511230.1; XM_006511167.3.
DR RefSeq; XP_006511231.1; XM_006511168.3.
DR AlphaFoldDB; Q69Z38; -.
DR SMR; Q69Z38; -.
DR BioGRID; 232703; 6.
DR IntAct; Q69Z38; 3.
DR STRING; 10090.ENSMUSP00000109901; -.
DR iPTMnet; Q69Z38; -.
DR PhosphoSitePlus; Q69Z38; -.
DR SwissPalm; Q69Z38; -.
DR EPD; Q69Z38; -.
DR jPOST; Q69Z38; -.
DR MaxQB; Q69Z38; -.
DR PaxDb; Q69Z38; -.
DR PeptideAtlas; Q69Z38; -.
DR PRIDE; Q69Z38; -.
DR ProteomicsDB; 287911; -.
DR Antibodypedia; 7598; 218 antibodies from 29 providers.
DR DNASU; 244895; -.
DR Ensembl; ENSMUST00000061552; ENSMUSP00000109901; ENSMUSG00000074305.
DR GeneID; 244895; -.
DR KEGG; mmu:244895; -.
DR UCSC; uc009psz.2; mouse.
DR CTD; 79834; -.
DR MGI; MGI:2442366; Peak1.
DR VEuPathDB; HostDB:ENSMUSG00000074305; -.
DR eggNOG; ENOG502QVUZ; Eukaryota.
DR GeneTree; ENSGT00940000157591; -.
DR HOGENOM; CLU_002882_0_0_1; -.
DR InParanoid; Q69Z38; -.
DR OMA; MGWNRNR; -.
DR OrthoDB; 49921at2759; -.
DR TreeFam; TF333340; -.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 244895; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Peak1; mouse.
DR PRO; PR:Q69Z38; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q69Z38; protein.
DR Bgee; ENSMUSG00000074305; Expressed in animal zygote and 214 other tissues.
DR ExpressionAtlas; Q69Z38; baseline and differential.
DR Genevisible; Q69Z38; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_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; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..1735
FT /note="Inactive tyrosine-protein kinase PEAK1"
FT /id="PRO_0000250590"
FT DOMAIN 1302..1664
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 26..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1300
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT REGION 1394..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1732
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 632
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 638
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 662
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 1141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H792"
FT CONFLICT 560
FT /note="K -> R (in Ref. 2; BAC33490)"
FT /evidence="ECO:0000305"
FT CONFLICT 965..991
FT /note="PPVQRHHWFTEAKGEASEKPAIVFMYR -> SSPAPSLVHRGQRRGQREACY
FT SLHVQV (in Ref. 2; BAC33490)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026..1039
FT /note="SSYLPSQIPDKACS -> GDPVKMSLNGELCD (in Ref. 3;
FT BAD32606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="L -> S (in Ref. 3; BAD32606)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534..1536
FT /note="LAC -> PTR (in Ref. 4; AAH26466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1735 AA; 191097 MW; 99A629E9061A0BF0 CRC64;
MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDSEKTPITH GSGKTNANHS NNHRVRSTGN
FRPPVAKKPT IAVKPTMMVA DGQSVCGELS IQEHCENKPV ILGWNQNKTS LSQKPLNNNS
EGDAEGFGSD PQQCANNDSA QKISNNNNGL TEVLKEIAGL EATPPVRGNE TNARETFLGR
INDCYKRSLE RKIPPSCMTG SMKDSQGKHV ILSGSAEVIS NEGGRFCYPE FSSGEESEED
VLFSNMEEEH ESWDESDEEL LAMEIRMRGQ PRFANFRANT LSPVRFFVSK KWNTIPLRNK
SLQRICAVDY DDSYDEILNG YEENSGVSYG QGSVQSTISS DCTSPGSSFT EESRSETASS
LSQKVCNGGI SPGNPGNSKD IAETESNFES PPGNNEEKDE SLTSKSSVKV PETHKAVLAL
RLQEKDGKIA VHTEKPESKA STDIAGQAVT ISLVPVEEQT KPYRVVNLEQ PLCKPYTVVD
VSAAMASEHL GRPKIKGSSS TPNSPVTSPA LTPGQINAHL KKSSAIRYQE VWTSSTSPRQ
KIPKIELSTG GPGPNVPPRK NCHKSAPTSP TATNISSKTI PVKSPNLSEI KFNSYNNAGM
PPFPIIIHDE PSYARSSKNA IKVPIVINPN AYDNLAIYKS FLGTSGELSV KEKTTSVISH
TYEEIETESK VSDSTPSKLT DCPQAKGFSN STERKRGSVA QKVQEFNNCL NRGQSSPQRS
YSSTHSSPAK IQRPTQEPAG KTEGAQGSQV PGSSSNSTRE KASAVLCQIV ASIQPPQTPP
EAPQSSPKAC SVEELYAVPP DADTTKSIPK NPPVRPKSLF TSQSSGEGEA HQTTESPTAK
IQKDPSTKPV TSPPSKLVTS AQSEPPPPFP PPRSTSSPYH ASNLLQRHFT NWTKPTSPTR
STEAESILHS EGSRRAADAK PKRWISFKSF FRRRKTDEEE EKEKEREKGK LVGLDGTVIH
MLPPPPVQRH HWFTEAKGEA SEKPAIVFMY RCDPDQGHLS VDQSKAGAEK GRAEEVLLRN
SEEKKSSYLP SQIPDKACSR VTHEVAGELS PRDPRTPAGK QDGTSVTPTL PPPDLEREEE
KDDTLDPTDV SPCSATYSNL GQSRAAMIPP KHPRHPKGAV DDAIAFGEKT DQEGLNASQP
TPPPLPKKMI RANTEPISKD LQKAMESSLC VMANPTYDID PNWDASSAGS SISYELKGLD
VESYESLERP LHKERPVPSA ANSISSLATL SVKDRFSNSM ESLSSRRGLS YRQTRSIQKP
QRQALYRGLD NREEVVGKLR SLHTDALKRL AVKCEDLFMA GQKDQLRFGV DSWSDFRLTS
DKPCCEAGDA VYYTASYAKD PLSNYAVKIC KSKAKESQQY YHSLAVRQSL PVHFNIQQDC
GHFLAEVPSR LLPWEDPDAP EKAEDGTEDS EEEGKAETLG GNPEPCSETE PSQKENQRVT
NRKQRSHVVV ITREVPHLTV ADFVRDSLAH HGNSPDLYER QVCLLLLQLC SGLEHLKPYH
VTHCDLRLEN LLLVQHQPGG AAQGPSPADP CPTLACPTRL IVSNFSQAKQ KSHLVDPQIL
RDQSRLAPEI ITATQYKKCD EFQTGILIYE MLHLPNPFDE NPELKEKEYT RTDLPRIPLR
SPYSWGLQQL ASCLLNPNPS ERILISDAKG ILQCLLWGPR EDLFQIFTTS ATLAQKNALL
QNWLDIKRTL LMIKFAEKSL DREGGISLED WLCAQYLAFA TTDSLSYIVK ILQYR
