ALS2_MOUSE
ID ALS2_MOUSE Reviewed; 1651 AA.
AC Q920R0; G5E868; Q8JZR1; Q9CXJ3;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Alsin;
DE AltName: Full=Amyotrophic lateral sclerosis 2 protein homolog;
GN Name=Als2;
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 {ECO:0000312|EMBL:BAB69016.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11586298; DOI=10.1038/ng1001-166;
RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A.,
RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr.,
RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.;
RT "A gene encoding a putative GTPase regulator is mutated in familial
RT amyotrophic lateral sclerosis 2.";
RL Nat. Genet. 29:166-173(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH46828.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH46828.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH31479.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-1651 (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-486, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-486, AND
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-527, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May act as a GTPase regulator. Controls survival and growth
CC of spinal motoneurons. {ECO:0000250}.
CC -!- SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with ALS2CL
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q920R0-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q920R0-2; Sequence=VSP_050525, VSP_050526;
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DR EMBL; AB053307; BAB69016.1; -; mRNA.
DR EMBL; AC153652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466548; EDL00124.1; -; Genomic_DNA.
DR EMBL; BC031479; AAH31479.1; -; mRNA.
DR EMBL; BC046828; AAH46828.1; -; mRNA.
DR EMBL; AK014320; BAB29271.2; -; mRNA.
DR CCDS; CCDS35583.1; -. [Q920R0-1]
DR RefSeq; NP_001153420.2; NM_001159948.2. [Q920R0-1]
DR RefSeq; NP_082993.4; NM_028717.6. [Q920R0-1]
DR RefSeq; NP_666221.1; NM_146109.3.
DR AlphaFoldDB; Q920R0; -.
DR SMR; Q920R0; -.
DR BioGRID; 216427; 5.
DR STRING; 10090.ENSMUSP00000027178; -.
DR iPTMnet; Q920R0; -.
DR PhosphoSitePlus; Q920R0; -.
DR SwissPalm; Q920R0; -.
DR EPD; Q920R0; -.
DR jPOST; Q920R0; -.
DR MaxQB; Q920R0; -.
DR PaxDb; Q920R0; -.
DR PeptideAtlas; Q920R0; -.
DR PRIDE; Q920R0; -.
DR ProteomicsDB; 296199; -. [Q920R0-1]
DR ProteomicsDB; 296200; -. [Q920R0-2]
DR Antibodypedia; 34146; 261 antibodies from 36 providers.
DR DNASU; 74018; -.
DR Ensembl; ENSMUST00000027178; ENSMUSP00000027178; ENSMUSG00000026024. [Q920R0-1]
DR Ensembl; ENSMUST00000163058; ENSMUSP00000125753; ENSMUSG00000026024. [Q920R0-1]
DR GeneID; 74018; -.
DR KEGG; mmu:74018; -.
DR UCSC; uc007bdm.2; mouse. [Q920R0-1]
DR UCSC; uc007bdn.2; mouse. [Q920R0-2]
DR CTD; 57679; -.
DR MGI; MGI:1921268; Als2.
DR VEuPathDB; HostDB:ENSMUSG00000026024; -.
DR eggNOG; KOG0231; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000155861; -.
DR HOGENOM; CLU_003333_0_0_1; -.
DR InParanoid; Q920R0; -.
DR OMA; WFSGKPH; -.
DR OrthoDB; 37470at2759; -.
DR PhylomeDB; Q920R0; -.
DR TreeFam; TF331793; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 74018; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Als2; mouse.
DR PRO; PR:Q920R0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q920R0; protein.
DR Bgee; ENSMUSG00000026024; Expressed in retinal neural layer and 108 other tissues.
DR ExpressionAtlas; Q920R0; baseline and differential.
DR Genevisible; Q920R0; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0008219; P:cell death; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; IMP:MGI.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007041; P:lysosomal transport; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0001881; P:receptor recycling; IMP:MGI.
DR GO; GO:0051036; P:regulation of endosome size; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0016050; P:vesicle organization; IDA:MGI.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.130.10.30; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR Pfam; PF02493; MORN; 7.
DR Pfam; PF00415; RCC1; 4.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF02204; VPS9; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00698; MORN; 8.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50985; SSF50985; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 4.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1651
FT /note="Alsin"
FT /id="PRO_0000080904"
FT REPEAT 59..108
FT /note="RCC1 1"
FT /evidence="ECO:0000305"
FT REPEAT 109..167
FT /note="RCC1 2"
FT /evidence="ECO:0000305"
FT REPEAT 169..218
FT /note="RCC1 3"
FT /evidence="ECO:0000305"
FT REPEAT 519..570
FT /note="RCC1 4"
FT /evidence="ECO:0000305"
FT REPEAT 572..621
FT /note="RCC1 5"
FT /evidence="ECO:0000305"
FT DOMAIN 684..879
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 895..1001
FT /note="PH"
FT /evidence="ECO:0000305"
FT REPEAT 1043..1065
FT /note="MORN 1"
FT REPEAT 1066..1088
FT /note="MORN 2"
FT REPEAT 1094..1116
FT /note="MORN 3"
FT REPEAT 1117..1139
FT /note="MORN 4"
FT REPEAT 1145..1167
FT /note="MORN 5"
FT REPEAT 1169..1191
FT /note="MORN 6"
FT REPEAT 1192..1214
FT /note="MORN 7"
FT REPEAT 1215..1238
FT /note="MORN 8"
FT DOMAIN 1507..1651
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 425..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q42"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C5Y8"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C5Y8"
FT VAR_SEQ 855..928
FT /note="TSPEYQKLQDSSSCYESLALHLGKKRKEAEYTLSFWKTFPGKMTDSLRKPER
FT RLLCESSNRALSLQHAGRFSVN -> VGFVCAPPNTREAKSQSSLFALSLLKMLGPGAG
FT EMAQWVRAPDCSSEGLEFKSQQPHGGSQPPVMRSDALFWSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050525"
FT VAR_SEQ 929..1651
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050526"
FT CONFLICT 318
FT /note="V -> I (in Ref. 1; BAB69016 and 4; AAH31479)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="L -> S (in Ref. 1; BAB69016 and 4; AAH31479)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="V -> F (in Ref. 4; AAH46828)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="V -> L (in Ref. 5; BAB29271)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296
FT /note="R -> H (in Ref. 1; BAB69016)"
FT /evidence="ECO:0000305"
FT CONFLICT 1452
FT /note="S -> L (in Ref. 1; BAB69016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1651 AA; 182566 MW; F9A9DBCA1ED423B2 CRC64;
MDSKKKSSTE AEGSKERGLV HVWQAGSFSL TPERLPGWGG KTVLQAALGV RHGVLLTEDG
EVYSFGTLPW KSESAEICPS SPLLESALVG HHVITVATGS FHSGAVTESG VVYMWGENAA
GQCAVANQQY VPEPSPVSIS DSETSPSLAV RILQLACGEE HTLALSLSRE IWAWGTGCQL
GLITTTFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PPQDLKPVPE RCNQCSQLLI
TMTDKEDHVI ISDSHCCPLG VTLSESQAEK HASPAPSPHP EALDEQGEVF ENTVVEAELN
MGSSQTTSGS AISTQQNVVG TAEVSSARTA PSYPDTHAVT AYLQKLSEHS MRENHEPGEK
PPQVQPLVEE AVPDLHSPPT TSTSALNSLV VSCASAVGVR VAATYEAGAL SLKKVMNFYS
TAPCETAAQS GSASTGPESL KDLREEQVKQ ESLQGKKSSS LMDIREEELE GGSRRLSLPG
LLSQVSPRLL RKAARVKTRT VVLTPTYSGE ADALLPSLRT EVWTWGKGKE GQLGHGDVLP
RLQPLCVKCL DGKEVIHLEA GGSHSLALTA KSQVYSWGSN TFGQLGHSEF PTTVPRLSKV
SSENGVWSVA AGQDYSLFLV DTEDFQPGLY YSGRQDRAEG DTLPENPSGT KTPVLLSCSK
LGYISRVTAG KDSYLALVDK NIMGYIASLH ELASTERRFY SKLSEIKSQI LRPLLSLENL
GTVTTVQLLQ EVASRFSKLC YLIGQHGASL SSYLQGMKEA SSLVIMKHSS LFLDSYTEYC
TSVSNFLVMG GFQLLAKPAI DFLNKNQELL QDLSEVNDEN TQLMEILNML FFLPIRRLHN
YAKVLLKLAT CFEVTSPEYQ KLQDSSSCYE SLALHLGKKR KEAEYTLSFW KTFPGKMTDS
LRKPERRLLC ESSNRALSLQ HAGRFSVNWF ILFNDALVHA QFSTHHVFPL ATLWAEPLSE
EAGSVNGLKI TTPEEQFTLI SSTPQEKTKW LRAISQAVDQ ALRGTSDFPL YGGGSSVQRQ
EPPISRSAKY TFYKDTRLKD ATYDGRWLSG KPHGRGVLKW PDGKMYSGMF RNGLEDGYGE
YRIPNKALNK EDHYVGHWKE GKMCGQGVYS YASGEVFEGC FQDNMRHGHG LLRSGKLTSS
SPSMFIGQWV MDKKAGYGVF DDITRGEKYM GMWQDDVCQG NGVVVTQFGL YYEGNFHLNK
MMGNGVLLSE DDTIYEGEFS DDWTLSGKGT LTMPHGDYIE GYFSGEWGSG IKITGTYFKP
SLYESDKDKP KAFRKLGNLA VAADEKWRAV FEECWRQLGC ESPGQGEVWK AWDNIAVALT
TNRRQHKDSP EILSRSQTQT LESLEYIPQH IGAFSVEKYD DIKKYLIKAC DTPLHPLGRL
VETLVAVYRM TYVGVGANRR LLQEAVKEIK SYLKRIFQLV RFLFPELPEE GSTIPLSAPL
PTGRRSFCTG KSDSRSESPE PGYVVTSSGL LLPVLLPRLY PPLFMLYALD NDREEDIYWE
CVLRLNKQPD IALLGFLGVQ KKFWPATLSI LGESKKVLST TKDACFASAV ECLQQISTTF
TPSDKLKVIQ QTFEEISQSV LASLQEDFLW SMDDLFPVFL YVVLRARIRN LGSEVHLIED
LMDPFLQHGE QGIMFTTLKA CYFQIQREKL N
