GAK_MOUSE
ID GAK_MOUSE Reviewed; 1305 AA.
AC Q99KY4; Q6P1I8; Q6P9S5; Q8BM74; Q8K0Q4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cyclin-G-associated kinase;
DE EC=2.7.11.1;
GN Name=Gak;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, and Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824 AND SER-827, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin
CC homolog that is involved in the uncoating of clathrin-coated vesicles
CC by Hsc70 in non-neuronal cells. Expression oscillates slightly during
CC the cell cycle, peaking at G1 (By similarity). {ECO:0000250}.
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 -!- INTERACTION:
CC Q99KY4; P97378: Il12rb2; NbExp=7; IntAct=EBI-7652906, EBI-6253448;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250}. Cell junction,
CC focal adhesion {ECO:0000250}. Note=Localizes to the perinuclear area
CC and to the trans-Golgi network. Also seen on the plasma membrane,
CC probably at focal adhesions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99KY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KY4-2; Sequence=VSP_015821;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK034637; BAC28779.1; -; mRNA.
DR EMBL; AK166682; BAE38941.1; -; mRNA.
DR EMBL; BC003958; AAH03958.1; -; mRNA.
DR EMBL; BC030859; AAH30859.1; -; mRNA.
DR EMBL; BC060622; AAH60622.1; -; mRNA.
DR EMBL; BC065052; AAH65052.1; -; mRNA.
DR CCDS; CCDS19513.1; -. [Q99KY4-1]
DR RefSeq; NP_001268980.1; NM_001282051.1.
DR RefSeq; NP_001268981.1; NM_001282052.1.
DR RefSeq; NP_705797.1; NM_153569.2.
DR AlphaFoldDB; Q99KY4; -.
DR SMR; Q99KY4; -.
DR BioGRID; 231137; 17.
DR IntAct; Q99KY4; 2.
DR MINT; Q99KY4; -.
DR STRING; 10090.ENSMUSP00000036705; -.
DR GlyConnect; 2244; 1 N-Linked glycan (1 site).
DR GlyGen; Q99KY4; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q99KY4; -.
DR PhosphoSitePlus; Q99KY4; -.
DR SwissPalm; Q99KY4; -.
DR EPD; Q99KY4; -.
DR jPOST; Q99KY4; -.
DR MaxQB; Q99KY4; -.
DR PaxDb; Q99KY4; -.
DR PRIDE; Q99KY4; -.
DR ProteomicsDB; 273024; -. [Q99KY4-1]
DR ProteomicsDB; 273025; -. [Q99KY4-2]
DR DNASU; 231580; -.
DR GeneID; 231580; -.
DR KEGG; mmu:231580; -.
DR UCSC; uc008yoh.2; mouse. [Q99KY4-1]
DR CTD; 2580; -.
DR MGI; MGI:2442153; Gak.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; Q99KY4; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; Q99KY4; -.
DR TreeFam; TF105165; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 231580; 19 hits in 79 CRISPR screens.
DR ChiTaRS; Gak; mouse.
DR PRO; PR:Q99KY4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99KY4; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0072318; P:clathrin coat disassembly; IGI:MGI.
DR GO; GO:1905224; P:clathrin-coated pit assembly; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:MGI.
DR GO; GO:0002064; P:epithelial cell development; IMP:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:MGI.
DR GO; GO:0048853; P:forebrain morphogenesis; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
DR GO; GO:0035622; P:intrahepatic bile duct development; IMP:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell junction;
KW Cytoplasm; Golgi apparatus; Kinase; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT CHAIN 2..1305
FT /note="Cyclin-G-associated kinase"
FT /id="PRO_0000085959"
FT DOMAIN 40..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 397..564
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 570..708
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1241..1305
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 707..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97874"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 792
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97874"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT MOD_RES 1122
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14976"
FT VAR_SEQ 748..796
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015821"
FT CONFLICT 301
FT /note="V -> E (in Ref. 1; BAE38941 and 2; AAH65052)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="D -> G (in Ref. 1; BAC28779)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="A -> V (in Ref. 2; AAH03958/AAH30859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1305 AA; 143641 MW; 4FC416FE52650ED2 CRC64;
MSLLQSALDF LAGPGSLGGA AGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDL
GSGREYALKR LLSNEEEKNR AIIQEVCFLK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
LLTELCKGQL VEFLKRVECK GPLSCDSILK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
LSNQGTIKLC DFGSATTISH YPDYSWSAQK RAMVEEEITR NTTPMYRTPE IVDLYSNFPI
GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPV NDTRYTVFHD LIRAMLKVNP
VERLSIAEVV RQLQEIAAAR NVNPKAPITE LLEQNGGYGN SGPSRAQPPC GGTVNSSGVL
ALAEYDQPYG GFLDILRGGT ERLFTNLKDT SSKVIQSVAN YAKGDLDISY ITSRIAVMSF
PAEGVESAIK NNIEDVRMFL DAKHPGHYAV YNLSPRIYRA SKFHNRVTEC GWAVRRAPHL
HSLYTLCRSM HAWLREDHRN VCVVHCMDGR AASAVAVCAF LCFCRLFSTA EAAVYMFSMK
RCPPGIWPSH KRYIEYVCDM VAEEPITPHS KPMLVKSVVM TPVPLFSKQR NGCRPFCEVY
VGEERVTTTS QEYDRMKEFK IEDGKAVIPL GVTVQGDVLI IIYHARATLG GRLQAKMASM
KMFQIQFHTG FVPRNATTVK FAKYDLDACD IQEKYPDLFQ VNLEVEVEPR DRPSREAPPW
ENTSLRGLNP KILFSNREEQ QDILSKFGKP ELPRQPGSTA QYDAEAGSPE AEITESDSPQ
SSSTDTNHFL HTLDWQEEKE PETGLDNTSP KESQSVLIAD GDGSEVSDEE EASFPSEERK
PGAGEDTPRL AAGTKQQDLI FDVGMLAAPQ EPVQPEEGVD LLGLHSEGDL RPAAPLQACG
VPSSNTDLLS CLLEPSDAAQ VGPPGDLLGG EAPLLLASPV SPLGLQNNLQ GKVPDTVDPF
DQFLLSSNSD TQPCSKPDLF GEFLNSDSVA SSTAFPSTHS APPPSCSTAF LHLGDLPAEP
SKVIASSSHP DLLGGWDTWA DTATPGPASI PVPEGTLFSS AGHPAPPGPN PSQTKSQNLD
PFADLSDLSS SLQGLPAGLP AGGFVGAPAP TQKSNSPWQA NRPTAPGTSW TPQAKPAPRA
SEQLRSHFSV IGAREERGVR VPSFAQKPKV SENDFEDLLP NQGFSKSDKK GPKTMAEMRK
QELARDTDPL KLKLLDWIEG KERNIRALLS TLHTVLWDGE SRWTPVSMAD LVTPEQVKKQ
YRRAVLVVHP DKATGQPYEQ YAKMIFMELN DAWSEFENQG SRPLF
