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   24-JAN-2024, entry version 177.
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 Mammary gland
RC   {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,
RC   Pancreas, 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   GlyGen; Q920R0; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q920R0; -.
DR   PhosphoSitePlus; Q920R0; -.
DR   SwissPalm; Q920R0; -.
DR   EPD; Q920R0; -.
DR   jPOST; Q920R0; -.
DR   MaxQB; Q920R0; -.
DR   PaxDb; 10090-ENSMUSP00000027178; -.
DR   PeptideAtlas; Q920R0; -.
DR   ProteomicsDB; 296199; -. [Q920R0-1]
DR   ProteomicsDB; 296200; -. [Q920R0-2]
DR   Pumba; Q920R0; -.
DR   Antibodypedia; 34146; 284 antibodies from 36 providers.
DR   DNASU; 74018; -.
DR   Ensembl; ENSMUST00000027178.13; ENSMUSP00000027178.7; ENSMUSG00000026024.15. [Q920R0-1]
DR   Ensembl; ENSMUST00000163058.2; ENSMUSP00000125753.2; ENSMUSG00000026024.15. [Q920R0-1]
DR   GeneID; 74018; -.
DR   KEGG; mmu:74018; -.
DR   UCSC; uc007bdm.2; mouse. [Q920R0-1]
DR   UCSC; uc007bdn.2; mouse. [Q920R0-2]
DR   AGR; MGI:1921268; -.
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; 3740287at2759; -.
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 77 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 110 other cell types or tissues.
DR   ExpressionAtlas; Q920R0; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; 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; ISO:MGI.
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:0016197; P:endosomal transport; IMP:MGI.
DR   GO; GO:0007032; P:endosome organization; ISO:MGI.
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: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   CDD; cd13269; PH_alsin; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 1.20.1050.80; VPS9 domain; 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   PANTHER; PTHR46089:SF3; ALSIN; 1.
DR   PANTHER; PTHR46089; ALSIN HOMOLOG; 1.
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; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR   SUPFAM; SSF109993; VPS9 domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00626; RCC1_2; 2.
DR   PROSITE; PS50012; RCC1_3; 4.
DR   PROSITE; PS51205; VPS9; 1.
DR   Genevisible; Q920R0; MM.
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
//