ID GCN1_MOUSE Reviewed; 2671 AA. AC E9PVA8; B2RWW6; DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=Stalled ribosome sensor GCN1 {ECO:0000305}; DE AltName: Full=GCN1 eIF-2-alpha kinase activator homolog {ECO:0000250|UniProtKB:Q92616}; DE AltName: Full=GCN1-like protein 1 {ECO:0000312|MGI:MGI:2444248}; DE AltName: Full=General control of amino-acid synthesis 1-like protein 1 {ECO:0000312|MGI:MGI:2444248}; DE AltName: Full=Translational activator GCN1 {ECO:0000305}; GN Name=Gcn1 {ECO:0000303|PubMed:15937339, ECO:0000312|MGI:MGI:2444248}; GN Synonyms=Gcn1l1 {ECO:0000312|MGI:MGI:2444248}; 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]. RC 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 [3] RP FUNCTION, INTERACTION WITH IMPACT, AND TISSUE SPECIFICITY. RX PubMed=15937339; DOI=10.1074/jbc.m408571200; RA Pereira C.M., Sattlegger E., Jiang H.-Y., Longo B.M., Jaqueta C.B., RA Hinnebusch A.G., Wek R.C., Mello L.E.A.M., Castilho B.A.; RT "IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 RT and inhibits GCN2 activation."; RL J. Biol. Chem. 280:28316-28323(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC 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 [5] RP INTERACTION WITH IMPACT. RX PubMed=22404850; DOI=10.1111/j.1742-4658.2012.08553.x; RA Waller T., Lee S.J., Sattlegger E.; RT "Evidence that Yih1 resides in a complex with ribosomes."; RL FEBS J. 279:1761-1776(2012). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=23447528; DOI=10.1074/jbc.m113.461970; RA Roffe M., Hajj G.N., Azevedo H.F., Alves V.S., Castilho B.A.; RT "IMPACT is a developmentally regulated protein in neurons that opposes the RT eukaryotic initiation factor 2alpha kinase GCN2 in the modulation of RT neurite outgrowth."; RL J. Biol. Chem. 288:10860-10869(2013). RN [7] RP FUNCTION, DOMAIN, AND INTERACTION WITH EIF2AK4. RX PubMed=24333428; DOI=10.1016/j.bbrc.2013.12.021; RA Cambiaghi T.D., Pereira C.M., Shanmugam R., Bolech M., Wek R.C., RA Sattlegger E., Castilho B.A.; RT "Evolutionarily conserved IMPACT impairs various stress responses that RT require GCN1 for activating the eIF2 kinase GCN2."; RL Biochem. Biophys. Res. Commun. 443:592-597(2014). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF 2053-ASP--LEU-2471. RX PubMed=32324833; DOI=10.1371/journal.pgen.1008693; RA Yamazaki H., Kasai S., Mimura J., Ye P., Inose-Maruyama A., Tanji K., RA Wakabayashi K., Mizuno S., Sugiyama F., Takahashi S., Sato T., Ozaki T., RA Cavener D.R., Yamamoto M., Itoh K.; RT "Ribosome binding protein GCN1 regulates the cell cycle and cell RT proliferation and is essential for the embryonic development of mice."; RL PLoS Genet. 16:e1008693-e1008693(2020). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=35328622; DOI=10.3390/ijms23063201; RA Liu J., Kasai S., Tatara Y., Yamazaki H., Mimura J., Mizuno S., RA Sugiyama F., Takahashi S., Sato T., Ozaki T., Tanji K., Wakabayashi K., RA Maeda H., Mizukami H., Shinkai Y., Kumagai Y., Tomita H., Itoh K.; RT "Inducible systemic Gcn1 deletion in mice leads to transient body weight RT loss upon tamoxifen treatment associated with decrease of fat and liver RT glycogen storage."; RL Int. J. Mol. Sci. 23:0-0(2022). CC -!- FUNCTION: Ribosome collision sensor that plays a key role in the RNF14- CC RNF25 translation quality control pathway, a pathway that takes place CC when a ribosome has stalled during translation, and which promotes CC ubiquitination and degradation of translation factors on stalled CC ribosomes (By similarity). Directly binds to the ribosome and acts as a CC sentinel for colliding ribosomes: activated following ribosome stalling CC and promotes recruitment of RNF14, which directly ubiquitinates CC EEF1A1/eEF1A, leading to its degradation (By similarity). In addition CC to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway CC mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal CC protein (By similarity). GCN1 also acts as a positive activator of the CC integrated stress response (ISR) by mediating activation of CC EIF2AK4/GCN2 in response to amino acid starvation (PubMed:15937339, CC PubMed:24333428, PubMed:32324833). Interaction with EIF2AK4/GCN2 on CC translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading CC to phosphorylation of eukaryotic translation initiation factor 2 (eIF- CC 2-alpha/EIF2S1) (PubMed:24333428, PubMed:32324833). EIF2S1/eIF-2-alpha CC phosphorylation converts EIF2S1/eIF-2-alpha into a global protein CC synthesis inhibitor, leading to a global attenuation of cap-dependent CC translation, and thus to a reduced overall utilization of amino acids, CC while concomitantly initiating the preferential translation of ISR- CC specific mRNAs, such as the transcriptional activator ATF4, and hence CC allowing ATF4-mediated reprogramming of amino acid biosynthetic gene CC expression to alleviate nutrient depletion (PubMed:24333428, CC PubMed:32324833). {ECO:0000250|UniProtKB:Q92616, CC ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:24333428, CC ECO:0000269|PubMed:32324833}. CC -!- SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction stimulates the CC EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety CC of stress conditions, such as amino acid depletion, UV-C irradiation, CC proteasome inhibitor treatment and glucose deprivation CC (PubMed:24333428). Interacts with IMPACT; this prevents the interaction CC of GCN1 with EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity CC (PubMed:15937339, PubMed:22404850). Interacts with RNF14; interaction CC takes place following ribosome stalling and promotes recruitment of CC RNF14 (By similarity). {ECO:0000250|UniProtKB:Q92616, CC ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:22404850, CC ECO:0000269|PubMed:24333428}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32324833, CC ECO:0000305|PubMed:23447528}. Note=Associates with ribosomes in CC undifferentiated neuroblastoma cells and increases after neuronal CC differentiation (PubMed:23447528). {ECO:0000269|PubMed:23447528}. CC -!- TISSUE SPECIFICITY: Expressed in the hypothalamus, cortex and CC hippocampus (PubMed:15937339). {ECO:0000269|PubMed:15937339}. CC -!- DOMAIN: The RWDBD (RWD-binding domain) region mediates binding to RWD CC domain-containing proteins, such as EIF2AK4/GCN2, IMPACT and RNF14. CC {ECO:0000269|PubMed:24333428, ECO:0000269|PubMed:32324833}. CC -!- DISRUPTION PHENOTYPE: Perinatal lethality; mice die at the intermediate CC stage of embryonic development because of severe growth retardation CC (PubMed:32324833). Tamoxifen-inducible deletion in adult mice leads to CC transient body weight loss associated with decrease of fat and liver CC glycogen storage (PubMed:35328622). {ECO:0000269|PubMed:32324833, CC ECO:0000269|PubMed:35328622}. CC -!- SIMILARITY: Belongs to the GCN1 family. {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; AC159539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC150735; AAI50736.1; -; mRNA. DR CCDS; CCDS19595.1; -. DR RefSeq; NP_766307.2; NM_172719.2. DR AlphaFoldDB; E9PVA8; -. DR IntAct; E9PVA8; 5. DR MINT; E9PVA8; -. DR STRING; 10090.ENSMUSP00000069432; -. DR GlyGen; E9PVA8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; E9PVA8; -. DR PhosphoSitePlus; E9PVA8; -. DR SwissPalm; E9PVA8; -. DR jPOST; E9PVA8; -. DR MaxQB; E9PVA8; -. DR PaxDb; 10090-ENSMUSP00000069432; -. DR PeptideAtlas; E9PVA8; -. DR ProteomicsDB; 267424; -. DR Pumba; E9PVA8; -. DR Antibodypedia; 9618; 88 antibodies from 15 providers. DR Ensembl; ENSMUST00000064454.12; ENSMUSP00000069432.8; ENSMUSG00000041638.19. DR GeneID; 231659; -. DR KEGG; mmu:231659; -. DR UCSC; uc008zeg.1; mouse. DR AGR; MGI:2444248; -. DR CTD; 10985; -. DR MGI; MGI:2444248; Gcn1. DR VEuPathDB; HostDB:ENSMUSG00000041638; -. DR eggNOG; KOG1242; Eukaryota. DR GeneTree; ENSGT00940000153612; -. DR HOGENOM; CLU_000504_2_2_1; -. DR InParanoid; E9PVA8; -. DR OMA; KYATQRG; -. DR OrthoDB; 6844at2759; -. DR PhylomeDB; E9PVA8; -. DR TreeFam; TF105398; -. DR BioGRID-ORCS; 231659; 21 hits in 82 CRISPR screens. DR ChiTaRS; Gcn1l1; mouse. DR PRO; PR:E9PVA8; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; E9PVA8; Protein. DR Bgee; ENSMUSG00000041638; Expressed in retinal neural layer and 157 other cell types or tissues. DR Genevisible; E9PVA8; MM. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI. DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB. DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB. DR GO; GO:0170011; F:stalled ribosome sensor activity; ISO:MGI. DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB. DR GO; GO:0140469; P:GCN2-mediated signaling; IDA:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central. DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 6. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR021133; HEAT_type_2. DR InterPro; IPR034085; TOG. DR PANTHER; PTHR23346:SF7; EIF-2-ALPHA KINASE ACTIVATOR GCN1; 1. DR PANTHER; PTHR23346; TRANSLATIONAL ACTIVATOR GCN1-RELATED; 1. DR SMART; SM00185; ARM; 5. DR SMART; SM01349; TOG; 1. DR SUPFAM; SSF48371; ARM repeat; 4. DR PROSITE; PS50077; HEAT_REPEAT; 3. PE 1: Evidence at protein level; KW Acetylation; Activator; Coiled coil; Cytoplasm; Phosphoprotein; KW Reference proteome; Repeat; Stress response; Translation regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q92616" FT CHAIN 2..2671 FT /note="Stalled ribosome sensor GCN1" FT /id="PRO_0000435424" FT REPEAT 140..178 FT /note="HEAT 1" FT /evidence="ECO:0000255" FT REPEAT 257..293 FT /note="HEAT 2" FT /evidence="ECO:0000255" FT REPEAT 294..331 FT /note="HEAT 3" FT /evidence="ECO:0000255" FT REPEAT 385..423 FT /note="HEAT 4" FT /evidence="ECO:0000255" FT REPEAT 425..459 FT /note="HEAT 5" FT /evidence="ECO:0000255" FT REPEAT 460..500 FT /note="HEAT 6" FT /evidence="ECO:0000255" FT REPEAT 560..597 FT /note="HEAT 7" FT /evidence="ECO:0000255" FT REPEAT 599..636 FT /note="HEAT 8" FT /evidence="ECO:0000255" FT REPEAT 700..732 FT /note="HEAT 9" FT /evidence="ECO:0000255" FT REPEAT 733..772 FT /note="HEAT 10" FT /evidence="ECO:0000255" FT REPEAT 879..918 FT /note="HEAT 11" FT /evidence="ECO:0000255" FT REPEAT 979..1016 FT /note="HEAT 12" FT /evidence="ECO:0000255" FT REPEAT 1035..1072 FT /note="HEAT 13" FT /evidence="ECO:0000255" FT REPEAT 1078..1115 FT /note="HEAT 14" FT /evidence="ECO:0000255" FT REPEAT 1155..1192 FT /note="HEAT 15" FT /evidence="ECO:0000255" FT REPEAT 1210..1250 FT /note="HEAT 16" FT /evidence="ECO:0000255" FT REPEAT 1251..1289 FT /note="HEAT 17" FT /evidence="ECO:0000255" FT REPEAT 1290..1332 FT /note="HEAT 18" FT /evidence="ECO:0000255" FT REPEAT 1335..1372 FT /note="HEAT 19" FT /evidence="ECO:0000255" FT REPEAT 1374..1410 FT /note="HEAT 20" FT /evidence="ECO:0000255" FT REPEAT 1413..1451 FT /note="HEAT 21" FT /evidence="ECO:0000255" FT REPEAT 1455..1492 FT /note="HEAT 22" FT /evidence="ECO:0000255" FT REPEAT 1493..1530 FT /note="HEAT 23" FT /evidence="ECO:0000255" FT REPEAT 1534..1571 FT /note="HEAT 24" FT /evidence="ECO:0000255" FT REPEAT 1573..1609 FT /note="HEAT 25" FT /evidence="ECO:0000255" FT REPEAT 1611..1648 FT /note="HEAT 26" FT /evidence="ECO:0000255" FT REPEAT 1653..1690 FT /note="HEAT 27" FT /evidence="ECO:0000255" FT REPEAT 1692..1729 FT /note="HEAT 28" FT /evidence="ECO:0000255" FT REPEAT 1731..1769 FT /note="HEAT 29" FT /evidence="ECO:0000255" FT REPEAT 1773..1810 FT /note="HEAT 30" FT /evidence="ECO:0000255" FT REPEAT 1812..1848 FT /note="HEAT 31" FT /evidence="ECO:0000255" FT REPEAT 1921..1958 FT /note="HEAT 32" FT /evidence="ECO:0000255" FT REPEAT 1959..1996 FT /note="HEAT 33" FT /evidence="ECO:0000255" FT REPEAT 2001..2038 FT /note="HEAT 34" FT /evidence="ECO:0000255" FT REPEAT 2039..2074 FT /note="HEAT 35" FT /evidence="ECO:0000255" FT REPEAT 2076..2108 FT /note="HEAT 36" FT /evidence="ECO:0000255" FT REPEAT 2111..2146 FT /note="HEAT 37" FT /evidence="ECO:0000255" FT REPEAT 2147..2184 FT /note="HEAT 38" FT /evidence="ECO:0000255" FT REPEAT 2188..2225 FT /note="HEAT 39" FT /evidence="ECO:0000255" FT REPEAT 2259..2296 FT /note="HEAT 40" FT /evidence="ECO:0000255" FT REPEAT 2301..2338 FT /note="HEAT 41" FT /evidence="ECO:0000255" FT REPEAT 2339..2380 FT /note="HEAT 42" FT /evidence="ECO:0000255" FT REPEAT 2382..2417 FT /note="HEAT 43" FT /evidence="ECO:0000255" FT REPEAT 2422..2459 FT /note="HEAT 44" FT /evidence="ECO:0000255" FT REPEAT 2546..2583 FT /note="HEAT 45" FT /evidence="ECO:0000255" FT REPEAT 2588..2625 FT /note="HEAT 46" FT /evidence="ECO:0000255" FT REPEAT 2627..2661 FT /note="HEAT 47" FT /evidence="ECO:0000255" FT REGION 2260..2408 FT /note="RWDBD region" FT /evidence="ECO:0000250|UniProtKB:P33892" FT COILED 804..865 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q92616" FT MOD_RES 729 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92616" FT MOD_RES 786 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92616" FT MOD_RES 2276 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92616" FT MUTAGEN 2053..2471 FT /note="Missing: In Gcn1(DeltaRWDBD) mice; mild growth FT retardation, leading to death soon after birth, most likely FT due to respiratory failure." FT /evidence="ECO:0000269|PubMed:32324833" FT CONFLICT 466 FT /note="L -> V (in Ref. 2; AAI50736)" FT /evidence="ECO:0000305" FT CONFLICT 537 FT /note="D -> E (in Ref. 2; AAI50736)" FT /evidence="ECO:0000305" FT CONFLICT 1477 FT /note="E -> K (in Ref. 2; AAI50736)" FT /evidence="ECO:0000305" FT CONFLICT 2544 FT /note="S -> G (in Ref. 2; AAI50736)" FT /evidence="ECO:0000305" FT CONFLICT 2583 FT /note="P -> H (in Ref. 2; AAI50736)" FT /evidence="ECO:0000305" SQ SEQUENCE 2671 AA; 293021 MW; 77B317C0797DC5A7 CRC64; MAADTQVSET LKRFAVKVTT ASVKERREIL SELGRCIAGK DLPEGAVKGL CKLFCLTLHR YRDAASRRAL QAAIQQLAEA QPEATAKNLL HSLQSSGVGS KACVPSKSSG SAALLALTWT CLLVRIVFPL KAKRQGDIWN KLVEVQCLLL LEVLGGSHKH AVDGAVKKLT KLWKENPGLV EQYFSAILSL EPSQNYAAML GLLVQFCTNH KEMDAVSQHK STLLEFYVKN ILMSKAKPPK YLLDNCAPLL RFMSHSEFKD LILPTIQKSL LRSPENVIET ISSLLASVTL DLSQYALDIV KGLANQLKSN SPRLMDEAVL ALRNLARQCS DSSATEALTK HLFAILGGSE GKLTIIAQKM SVLSGIGSLS HHVVSGPSGQ VLNGCVAELF IPFLQQEVHE GTLVHAVSIL ALWCNRFTTE VPKKLTDWFK KVFSLKTSTS AVRHAYLQCM LASFRGDTLL QALDFLPLLM QTVEKAASQG TQVPTVTEGV AAALLLSKLS VADAQAEAKL SGFWQLVVDE KRQTFTSEKF LLLASEDALC TVLRLTERLF LDHPHRLTNS KVQQYYRVLV AVLLSRTWHV RRQAQQTVRK LLSSLGGVKL ANGLLDELKT VLNSHKVLPL EALVTDAGEV TEMGKTYVPP RVLQEALCVI SGVPGLKGDI PSTEQLAQEM LIISHHPSLV AVQSGLWPAL LTRMKIDPDA FITRHLDQII PRITTQSPLN QSSMNAMGSL SVLSPDRVLP QLISTITASV QNPALCLVTR EEFSIMQTPA GELFDKSIIQ SAQQDSIKKA NMKRENKAYS FKEQIIEMEL KEEIKKKKGI KEEVQLTSKQ KEMLQAQMDK EAQIRRRLQE LDGELEAALG LLDAIMARNP CGLIQYIPVL VDAFLPLLKS PLAAPRVKGP FLSLAACVMP PRLKTLGTLV SHVTLRLLKP ECALDKSWCQ EELPVAVRRA VSLLHTHTIP SRVGKGEPDA APLSAPAFSL VFPMLKMVLT EMPYHSEEEE EQMAQILQIL TVHAQLRASP DTPPERVDEN GPELLPRVAM LRLLTWVIGT GSPRLQVLAS DTLTALCASS SGEDGCAFAE QEEVDVLLAA LQSPCASVRE TALRGLMELR LVLPSPDTDE KSGLSLLRRL WVIKFDKEDE IRKLAERLWS TMGLDLQSDL CSLLIDDVIY HEAAVRQAGA EALSQAVARY QRQAAEVMGR LMEIYQEKLY RPPPVLDALG RVISESPPDQ WEARCGLALA LNKLSQYLDS SQVKPLFQFF VPDALNDRNP DVRKCMLDAA LATLNAHGKE NVNSLLPVFE EFLKDAPNDA SYDAVRQSVV VLMGSLAKHL DKSDPKVKPI VAKLIAALST PSQQVQESVA SCLPPLVPAV KEDAGGMIQR LMQQLLESDK YAERKGAAYG LAGLVKGLGI LSLKQQEMMA ALTDAIQDKK NFRRREGALF AFEMLCTMLG KLFEPYVVHV LPHLLLCFGD GNQYVREAAD DCAKAVMSNL SAHGVKLVLP SLLAALEEES WRTKAGSVEL LGAMAYCAPK QLSSCLPNIV PKLTEVLTDS HVKVQKAGQQ ALRQIGSVIR NPEILAIAPV LLDALTDPSR KTQKCLQTLL DTKFVHFIDA PSLALIMPIV QRAFQDRSTD TRKMAAQIIG NMYSLTDQKD LAPYLPSVTP GLKASLLDPV PEVRTVSAKA LGAMVKGMGE SCFEDLLPWL METLTYEQSS VDRSGAAQGL AEVMAGLGVE KLEKLMPEIV ATASKVDIAP HVRDGYIMMF NYLPITFGDK FTPYVGPIIP CILKALADEN EFVRDTALRA GQRVISMYAE TAIALLLPQL EQGLFDDLWR IRFSSVQLLG DLLFHISGVT GKMTTETASE DDNFGTAQSN KAIITALGVD RRNRVLAGLY MGRSDTQLVV RQASLHVWKI VVSNTPRTLR EILPTLFGLL LGFLASTCAD KRTIAARTLG DLVRKLGEKI LPEIIPILEE GLRSQKSDER QGVCIGLSEI MKSTSRDAVL FFSESLVPTA RKALCDPLEE VREAAAKTFE QLHSTIGHQA LEDILPFLLK QLDDEEVSEF ALDGLKQVMA VKSRVVLPYL VPKLTTPPVN TRVLAFLSSV AGDALTRHLG VILPAVMLAL KEKLGTPDEQ LEMANCQAVI LSVEDDTGHR IIIEDLLEAT RSPEVGMRQA AAIILNMYCS RSKADYSSHL RSLVSGLIRL FNDSSPVVLE ESWDALNAIT KKLDAGNQLA LIEELHKEIR FIGNECKGEH VPGFCLPKRG VTSILPVLRE GVLTGSPEQK EEAAKGLGLV IRLTSADALR PSVVSITGPL IRILGDRFNW TVKAALLETL SLLLGKVGIA LKPFLPQLQT TFTKALQDSN RGVRLKAADA LGKLISIHVK VDPLFTELLN GIRAVEDPGI RDTMLQALRF VIQGAGSKVD AAIRKNLVSL LLSMLGHDED NTRISTAGCL GELCAFLTDE ELNTVLQQCL LADVSGIDWM VRHGRSLALS VAVNVAPSRL CAGRYSNEVQ DMILSNAVAD RIPIAMSGIR GMGFLMKYHI ETGSGQLPPR LSSLLIKCLQ NPCSDIRLVA EKMIWWANKE PRPPLEPQTI KPILKALLDN TKDKNTVVRA YSDQAIVNLL KMRRGEELLQ SLSKILDVAS LEALNECSRR SLRKLACQAD SVEQVDDTIL T //