ID PAK4_MOUSE Reviewed; 593 AA. AC Q8BTW9; Q6ZPX0; Q80Z97; Q9CS71; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=Serine/threonine-protein kinase PAK 4; DE EC=2.7.11.1; DE AltName: Full=p21-activated kinase 4; DE Short=PAK-4; GN Name=Pak4; Synonyms=Kiaa1142; 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], INTERACTION WITH FGFR2 AND GRB2, AND RP PHOSPHORYLATION AT TYROSINE RESIDUES. RC STRAIN=BALB/cJ; RX PubMed=12529371; DOI=10.1074/jbc.m205875200; RA Lu Y., Pan Z.-Z., Devaux Y., Ray P.; RT "p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte RT growth factor receptor and participates in keratinocyte growth factor- RT mediated inhibition of oxidant-induced cell death."; RL J. Biol. Chem. 278:10374-10380(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III. 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. 10:167-180(2003). RN [3] RP SEQUENCE REVISION. RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Embryo, and Thymus; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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 [6] RP FUNCTION IN PHOSPHORYLATION OF LIMK1. RX PubMed=11413130; DOI=10.1074/jbc.m100871200; RA Dan C., Kelly A., Bernard O., Minden A.; RT "Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are RT mediated by LIM kinase 1 and cofilin."; RL J. Biol. Chem. 276:32115-32121(2001). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=14517283; DOI=10.1128/mcb.23.20.7122-7133.2003; RA Qu J., Li X., Novitch B.G., Zheng Y., Kohn M., Xie J.M., Kozinn S., RA Bronson R., Beg A.A., Minden A.; RT "PAK4 kinase is essential for embryonic viability and for proper neuronal RT development."; RL Mol. Cell. Biol. 23:7122-7133(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and RC 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 [12] RP FUNCTION. RX PubMed=21381077; DOI=10.1002/jcb.23092; RA Nekrasova T., Minden A.; RT "PAK4 is required for regulation of the cell-cycle regulatory protein p21, RT and for control of cell-cycle progression."; RL J. Cell. Biochem. 112:1795-1806(2011). RN [13] RP DISRUPTION PHENOTYPE. RX PubMed=21382368; DOI=10.1016/j.ydbio.2011.02.026; RA Tian Y., Lei L., Minden A.; RT "A key role for Pak4 in proliferation and differentiation of neural RT progenitor cells."; RL Dev. Biol. 353:206-216(2011). CC -!- FUNCTION: Serine/threonine protein kinase that plays a role in a CC variety of different signaling pathways including cytoskeleton CC regulation, cell migration, growth, proliferation or cell survival. CC Activation by various effectors including growth factor receptors or CC active CDC42 and RAC1 results in a conformational change and a CC subsequent autophosphorylation on several serine and/or threonine CC residues. Phosphorylates and inactivates the protein phosphatase SSH1, CC leading to increased inhibitory phosphorylation of the actin CC binding/depolymerizing factor cofilin. Decreased cofilin activity may CC lead to stabilization of actin filaments. Phosphorylates LIMK1, a CC kinase that also inhibits the activity of cofilin. Phosphorylates CC integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates CC ARHGEF2 and activates the downstream target RHOA that plays a role in CC the regulation of assembly of focal adhesions and actin stress fibers. CC Stimulates cell survival by phosphorylating the BCL2 antagonist of cell CC death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 CC binding to death domain receptors in a kinase independent manner. Plays CC a role in cell-cycle progression by controlling levels of the cell- CC cycle regulatory protein CDKN1A and by phosphorylating RAN. CC {ECO:0000269|PubMed:11413130, ECO:0000269|PubMed:21381077}. 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 -!- ACTIVITY REGULATION: Inhibited by INKA1; which inhibits the CC serine/threonine-protein kinase activity by binding PAK4 in a CC substrate-like manner. {ECO:0000250|UniProtKB:O96013}. CC -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 CC and weakly with RAC1 (By similarity). Interacts with FGFR2 and GRB2 CC (PubMed:12529371). Interacts with INKA1. Interacts with SH3RF2 (By CC similarity). {ECO:0000250|UniProtKB:O96013, CC ECO:0000269|PubMed:12529371}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O96013}. CC Note=Seems to shuttle between cytoplasmic compartments depending on the CC activating effector. For example, can be found on the cell periphery CC after activation of growth-factor or integrin-mediated signaling CC pathways. {ECO:0000250|UniProtKB:O96013}. CC -!- PTM: Autophosphorylated on serine residues when activated by CDC42/p21 CC (By similarity). Phosphorylated on tyrosine residues upon stimulation CC of FGFR2 (PubMed:12529371). Methylated by SETD6. CC {ECO:0000250|UniProtKB:O96013, ECO:0000269|PubMed:12529371}. CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation. CC {ECO:0000250|UniProtKB:O96013}. CC -!- DISRUPTION PHENOTYPE: Mice die at embryonic day 11.5 probably due to a CC defect in the fetal heart. They show strong defects in neuronal CC development and axonal outgrowth. Spinal cord motor neurons and CC interneurons failed to differentiate and migrate to their proper CC position. Nervous system-specific conditional PAK4 deletion mice CC display growth retardation and die prematurely. CC {ECO:0000269|PubMed:14517283, ECO:0000269|PubMed:21382368}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC98108.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY217016; AAO61496.1; -; mRNA. DR EMBL; AK129298; BAC98108.2; ALT_INIT; mRNA. DR EMBL; AK017713; BAB30889.1; -; mRNA. DR EMBL; AK088512; BAC40396.1; -; mRNA. DR EMBL; BC048238; AAH48238.1; -; mRNA. DR CCDS; CCDS21049.1; -. DR RefSeq; NP_081746.1; NM_027470.3. DR RefSeq; XP_017167785.1; XM_017312296.1. DR RefSeq; XP_017167786.1; XM_017312297.1. DR AlphaFoldDB; Q8BTW9; -. DR SMR; Q8BTW9; -. DR BioGRID; 214149; 4. DR STRING; 10090.ENSMUSP00000103918; -. DR iPTMnet; Q8BTW9; -. DR PhosphoSitePlus; Q8BTW9; -. DR EPD; Q8BTW9; -. DR jPOST; Q8BTW9; -. DR MaxQB; Q8BTW9; -. DR PeptideAtlas; Q8BTW9; -. DR ProteomicsDB; 294376; -. DR Pumba; Q8BTW9; -. DR Antibodypedia; 16732; 708 antibodies from 43 providers. DR DNASU; 70584; -. DR Ensembl; ENSMUST00000032823.5; ENSMUSP00000032823.5; ENSMUSG00000030602.14. DR Ensembl; ENSMUST00000108283.8; ENSMUSP00000103918.2; ENSMUSG00000030602.14. DR GeneID; 70584; -. DR KEGG; mmu:70584; -. DR UCSC; uc009fzh.1; mouse. DR AGR; MGI:1917834; -. DR CTD; 10298; -. DR MGI; MGI:1917834; Pak4. DR VEuPathDB; HostDB:ENSMUSG00000030602; -. DR GeneTree; ENSGT00940000159792; -. DR HOGENOM; CLU_000288_26_6_1; -. DR InParanoid; Q8BTW9; -. DR OMA; QENGDPQ; -. DR OrthoDB; 460351at2759; -. DR PhylomeDB; Q8BTW9; -. DR TreeFam; TF105352; -. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013404; RAC2 GTPase cycle. DR Reactome; R-MMU-9013406; RHOQ GTPase cycle. DR Reactome; R-MMU-9013407; RHOH GTPase cycle. DR Reactome; R-MMU-9013408; RHOG GTPase cycle. DR Reactome; R-MMU-9013420; RHOU GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-9013424; RHOV GTPase cycle. DR BioGRID-ORCS; 70584; 1 hit in 78 CRISPR screens. DR ChiTaRS; Pak4; mouse. DR PRO; PR:Q8BTW9; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q8BTW9; Protein. DR Bgee; ENSMUSG00000030602; Expressed in animal zygote and 221 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI. DR GO; GO:0060996; P:dendritic spine development; IGI:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI. DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central. DR CDD; cd01093; CRIB_PAK_like; 1. DR Gene3D; 3.90.810.10; CRIB domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000095; CRIB_dom. DR InterPro; IPR036936; CRIB_dom_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR033923; PAK_BD. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1. DR PANTHER; PTHR48015:SF17; SERINE_THREONINE-PROTEIN KINASE PAK 4; 1. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00285; PBD; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50108; CRIB; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q8BTW9; MM. PE 1: Evidence at protein level; KW Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Kinase; Methylation; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..593 FT /note="Serine/threonine-protein kinase PAK 4" FT /id="PRO_0000086475" FT DOMAIN 11..24 FT /note="CRIB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057" FT DOMAIN 323..574 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 25..322 FT /note="Linker" FT REGION 95..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 146..165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 185..201 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 277..295 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 442 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 329..337 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 41 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 78 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 187 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 195 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 207 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 293 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O96013" FT MOD_RES 476 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079" FT CONFLICT 5 FT /note="K -> R (in Ref. 1; AAO61496)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="P -> L (in Ref. 1; AAO61496)" FT /evidence="ECO:0000305" FT CONFLICT 564 FT /note="T -> P (in Ref. 4; BAB30889)" FT /evidence="ECO:0000305" SQ SEQUENCE 593 AA; 64623 MW; 4AFA91DD73D4C6D5 CRC64; MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRESPPPPAR AHQENGMLEE RAAPARMAPD KAGSRARATG HSEAGSGSGD RRRVGPEKRP KSSRDGPGGP QEASRDKRPL SGPDVSTPQP GSLTSGTKLA AGRPFNTYPR ADTDHPPRGA QGEPHTMAPN GPSATGLAAP QSSSSSRPPT RARGAPSPGV LGPHASEPQL APPARALAAP AVPPAPGPPG PRSPQREPQR VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGIVCIA TVRSSGKLVA VKKMDLRKQQ RRELLFNEVV IMRDYRHENV VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA AVCLAVLQAL AVLHAQGVIH RDIKSDSILL THDGRVKLSD FGFCAQVSKE VPRRKSLVGT PYWMAPELIS RLPYGPEVDI WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL HKASPSLKGF LDRLLVRDPA QRATAAELLK HPFLTKAGPP ASIVPLMRQH RTR //