ARHG1_MOUSE
ID ARHG1_MOUSE Reviewed; 920 AA.
AC Q61210; O89074; Q3T9Q7; Q80YE8; Q80YE9; Q91VL3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Rho guanine nucleotide exchange factor 1;
DE AltName: Full=Lbc's second cousin;
DE AltName: Full=Lymphoid blast crisis-like 2;
GN Name=Arhgef1; Synonyms=Lbcl2, Lsc;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=8702517; DOI=10.1074/jbc.271.31.18643;
RA Whitehead I.P., Khosravi-Far R., Kirk H., Trigo-Gonzalez G., Der C.J.,
RA Kay R.;
RT "Expression cloning of lsc, a novel oncogene with structural similarities
RT to the Dbl family of guanine nucleotide exchange factors.";
RL J. Biol. Chem. 271:18643-18650(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lanson N.A. Jr., Egeland D.B., Claycomb W.C.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=NOD; TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 557-720.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 670-920 (ISOFORMS 3 AND 4), FUNCTION
RP (ISOFORMS 3 AND 4), AND SUBUNIT.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12773540; DOI=10.1074/jbc.m303277200;
RA Eisenhaure T.M., Francis S.A., Willison L.D., Coughlin S.R., Lerner D.J.;
RT "The Rho guanine exchange factor Lsc homo-oligomerizes and is negatively
RT regulated through domains in its carboxyl-terminus that are absent in novel
RT splenic isoforms.";
RL J. Biol. Chem. 278:30975-30984(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH RHOA.
RX PubMed=8910315; DOI=10.1074/jbc.271.44.27374;
RA Glaven J.A., Whitehead I.P., Nomanbhoy T., Kay R., Cerione R.A.;
RT "Lfc and Lsc oncoproteins represent two new guanine nucleotide exchange
RT factors for the Rho GTP-binding protein.";
RL J. Biol. Chem. 271:27374-27381(1996).
RN [8]
RP POSSIBLE INTERACTION WITH CCPG1.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-390; SER-412 AND
RP THR-432 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-412 AND THR-432 (ISOFORM 5), AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION AT TYR-737.
RX PubMed=20098430; DOI=10.1038/nm.2079;
RA Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M.,
RA Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M.,
RA Offermanns S., Pacaud P., Loirand G.;
RT "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on
RT vascular tone and blood pressure.";
RL Nat. Med. 16:183-190(2010).
CC -!- FUNCTION: Seems to play a role in the regulation of RhoA GTPase by
CC guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13)
CC subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13,
CC and as guanine nucleotide exchange factor (GEF) for RhoA GTPase.
CC Activated G alpha 13/GNA13 stimulates the RhoGEF activity through
CC interaction with the RGS-like domain. This GEF activity is inhibited by
CC binding to activated GNA12. Mediates angiotensin-2-induced RhoA
CC activation. Isoform 3 and isoform 4 do not homooligomerize and show an
CC enhanced RhoGEF activity. {ECO:0000269|PubMed:20098430,
CC ECO:0000269|PubMed:8910315}.
CC -!- SUBUNIT: Interacts with RHOA, GNA12 and GNA13 (By similarity).
CC Homooligomerizes through the coiled coil region. Interacts with CTNNAL1
CC (By similarity). May interact with CCPG1. {ECO:0000250,
CC ECO:0000269|PubMed:12773540, ECO:0000269|PubMed:8910315}.
CC -!- INTERACTION:
CC Q61210; Q64727: Vcl; NbExp=3; IntAct=EBI-641821, EBI-432047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Translocated to the membrane by activated GNA13 or LPA
CC stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q61210-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61210-2; Sequence=VSP_008126;
CC Name=3;
CC IsoId=Q61210-3; Sequence=VSP_008127, VSP_008128;
CC Name=4;
CC IsoId=Q61210-4; Sequence=VSP_008129, VSP_008130;
CC Name=5;
CC IsoId=Q61210-5; Sequence=VSP_008126, VSP_026131;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8702517}.
CC -!- DOMAIN: The RGSL domain, also known as rgRGS domain, is necessary but
CC not sufficient for full GAP activity. {ECO:0000250}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC -!- PTM: Phosphorylated by PKCA (By similarity). Angiotensin-2 induced Tyr-
CC 737 phosphorylation is mediated by JAK2. Isoform 5 is phosphorylated at
CC 'Ser-390'. {ECO:0000250, ECO:0000269|PubMed:20098430}.
CC -!- DISRUPTION PHENOTYPE: Mice have reduced response to angiotensin-2 and
CC lowered RhoA signaling pathway. {ECO:0000269|PubMed:20098430}.
CC -!- CAUTION: Ref.2 sequence was originally submitted as from rat origin.
CC {ECO:0000305}.
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DR EMBL; U58203; AAC52693.1; -; mRNA.
DR EMBL; AF314539; AAG33860.1; -; mRNA.
DR EMBL; AK157056; BAE33947.1; -; mRNA.
DR EMBL; AK172354; BAE42963.1; -; mRNA.
DR EMBL; BC012488; AAH12488.1; -; mRNA.
DR EMBL; U89421; AAC36527.1; -; mRNA.
DR EMBL; AY246272; AAO91658.1; -; mRNA.
DR EMBL; AY246273; AAO91659.1; -; mRNA.
DR CCDS; CCDS52141.1; -. [Q61210-1]
DR CCDS; CCDS52142.1; -. [Q61210-5]
DR CCDS; CCDS85239.1; -. [Q61210-2]
DR RefSeq; NP_001123622.1; NM_001130150.1. [Q61210-5]
DR RefSeq; NP_001123623.1; NM_001130151.1.
DR RefSeq; NP_001123624.1; NM_001130152.1. [Q61210-1]
DR RefSeq; NP_001123625.1; NM_001130153.1. [Q61210-1]
DR RefSeq; NP_032514.1; NM_008488.2. [Q61210-2]
DR AlphaFoldDB; Q61210; -.
DR SMR; Q61210; -.
DR BioGRID; 201115; 6.
DR IntAct; Q61210; 11.
DR STRING; 10090.ENSMUSP00000096280; -.
DR iPTMnet; Q61210; -.
DR PhosphoSitePlus; Q61210; -.
DR SwissPalm; Q61210; -.
DR EPD; Q61210; -.
DR jPOST; Q61210; -.
DR MaxQB; Q61210; -.
DR PeptideAtlas; Q61210; -.
DR PRIDE; Q61210; -.
DR ProteomicsDB; 283209; -. [Q61210-1]
DR ProteomicsDB; 283210; -. [Q61210-2]
DR ProteomicsDB; 283211; -. [Q61210-3]
DR ProteomicsDB; 283212; -. [Q61210-4]
DR ProteomicsDB; 283213; -. [Q61210-5]
DR Antibodypedia; 2765; 282 antibodies from 34 providers.
DR DNASU; 16801; -.
DR Ensembl; ENSMUST00000047873; ENSMUSP00000046469; ENSMUSG00000040940. [Q61210-1]
DR Ensembl; ENSMUST00000098683; ENSMUSP00000096280; ENSMUSG00000040940. [Q61210-5]
DR Ensembl; ENSMUST00000117419; ENSMUSP00000113366; ENSMUSG00000040940. [Q61210-1]
DR Ensembl; ENSMUST00000206508; ENSMUSP00000146314; ENSMUSG00000040940. [Q61210-2]
DR GeneID; 16801; -.
DR KEGG; mmu:16801; -.
DR UCSC; uc009fqv.2; mouse. [Q61210-2]
DR UCSC; uc009fqw.2; mouse. [Q61210-5]
DR UCSC; uc009fqy.2; mouse. [Q61210-1]
DR CTD; 9138; -.
DR MGI; MGI:1353510; Arhgef1.
DR VEuPathDB; HostDB:ENSMUSG00000040940; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000161180; -.
DR HOGENOM; CLU_003962_2_0_1; -.
DR InParanoid; Q61210; -.
DR OMA; NRGDSHC; -.
DR OrthoDB; 319635at2759; -.
DR PhylomeDB; Q61210; -.
DR TreeFam; TF106495; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 16801; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgef1; mouse.
DR PRO; PR:Q61210; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61210; protein.
DR Bgee; ENSMUSG00000040940; Expressed in granulocyte and 239 other tissues.
DR ExpressionAtlas; Q61210; baseline and differential.
DR Genevisible; Q61210; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR CDD; cd08755; RGS_p115RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR037887; p115RhoGEF_RGS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..920
FT /note="Rho guanine nucleotide exchange factor 1"
FT /id="PRO_0000080907"
FT DOMAIN 39..230
FT /note="RGSL"
FT DOMAIN 415..604
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 646..759
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 231..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 865..894
FT /evidence="ECO:0000255"
FT COMPBIAS 231..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 694
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 737
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000269|PubMed:20098430"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 291
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8702517, ECO:0000303|Ref.2"
FT /id="VSP_008126"
FT VAR_SEQ 372..373
FT /note="ES -> ERRWKRLSGRLGRSESLRVSDRRRPSRGSLGAKGRGGGRSRSDVDM
FT DPGSATAVLGPTRRAT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026131"
FT VAR_SEQ 780..791
FT /note="REPLLSSSENGT -> SHPRGLEQREIG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12773540"
FT /id="VSP_008127"
FT VAR_SEQ 792..920
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12773540"
FT /id="VSP_008128"
FT VAR_SEQ 830..856
FT /note="VLSLKQILLSTEEDSGAGPPRDGDGVP -> GVGRGILSPKTPPVPAWGDSV
FT PQPGCT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12773540"
FT /id="VSP_008129"
FT VAR_SEQ 857..920
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12773540"
FT /id="VSP_008130"
FT CONFLICT 574
FT /note="I -> M (in Ref. 5; AAC36527)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="I -> T (in Ref. 5; AAC36527)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="H -> Y (in Ref. 6; AAO91659)"
FT /evidence="ECO:0000305"
FT MOD_RES Q61210-5:386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES Q61210-5:390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES Q61210-5:412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q61210-5:432
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 920 AA; 102805 MW; 913A819972CBACC8 CRC64;
MGEVAGGAAP GPPRSGLVSI IIGAEDEDFE NELEANSEDQ NSQFQSLEQV KRRPAHLMAL
LQHVALQFEP GPLLCCLHAD MLSSLGPKEA KKAFLDFYHS FLEKTAVLRV PVPPSVAFEL
DRTRPDLISE DVQRRFIQEV VQSQQAAVSR QLEDFRSKRL MGMTPWEQEL SLLEPWIGKD
RGNYEARERH VAERLLSHLE ETQHTISTDE EKSAAVVTAI SLYMRHLGVR TKSGDKKSGR
NFFRKKVMGN RRSDEPPKTK KGLSSILDPA RWNRGEPSAP DCRHLKVEAD AEKPGPADRK
GGLGMSSRDR TVGTPGQDNP GVSLHPLSTD SVDSREPGVD TPQEPGDTPP QGPTSLEPLA
PPESTEDNGE TESPEPGDDG EPGRSGLELE PEEPPGWREL VPPDTLLSLP KSQVKRQEVI
SELLVTEAAH VRMLRVLHDL FYQPMADGGF FPLDELQNIF PSLDELIEVH SLFLDRLMKR
RQESGYLIEE IGDVLLARFD GAEGSWFQKI SSRFCSRQSF ALEQLKAKQR KEPRFCAFVQ
EAESRPRCRR LQLKDMIPTE MQRLTKYPLL LQSIGQNTEE STERGKVELA AECCREILHH
VNQAVRDMED LLRLKDYQRR LDLTHLRQSS DPMLSEFKNL DITKKKLVHE GPLTWRVTKD
KAIEVHVLLL DDLLLLLQRQ DERLLLKSHS RTLTPTPDGK TMLRPVLRLT SAMTREVATD
HKAFYVIFTW DQEAQIYELV AQTSSERKNW CNLITETAGS LKVPAPASRL KPRPSPSSIR
EPLLSSSENG TGGAEMAPAD ARTERLLNDL LPFCRPGPEG QLAATALQKV LSLKQILLST
EEDSGAGPPR DGDGVPGGRA PGPVHTQEIE ENLLSLEVAI RQLEELEEEF CRLRPLLSQL
GGTLSPNLAA PERSAQTGLS
