RGRF2_MOUSE
ID RGRF2_MOUSE Reviewed; 1189 AA.
AC P70392; Q3TYN3; Q9QX51;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ras-specific guanine nucleotide-releasing factor 2;
DE Short=Ras-GRF2;
DE AltName: Full=Ras guanine nucleotide exchange factor 2;
GN Name=Rasgrf2; Synonyms=Grf2;
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], FUNCTION, INTERACTION WITH RAS AND CALMODULIN,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9032266; DOI=10.1128/mcb.17.3.1396;
RA Fam N.P., Fan W.-T., Wang Z., Zhang L.-J., Chen H., Moran M.F.;
RT "Cloning and characterization of Ras-GRF2, a novel guanine nucleotide
RT exchange factor for Ras.";
RL Mol. Cell. Biol. 17:1396-1406(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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 [3]
RP PROTEIN SEQUENCE OF 464-474 AND 723-734, PHOSPHORYLATION, UBIQUITINATION,
RP AND MUTAGENESIS OF ARG-1022 AND ARG-1092.
RX PubMed=11238945; DOI=10.1128/mcb.21.6.2107-2117.2001;
RA de Hoog C.L., Koehler J.A., Goldstein M.D., Taylor P., Figeys D.,
RA Moran M.F.;
RT "Ras binding triggers ubiquitination of the Ras exchange factor Ras-GRF2.";
RL Mol. Cell. Biol. 21:2107-2117(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 922-1189, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=11909944; DOI=10.1128/mcb.22.8.2498-2504.2002;
RA Fernandez-Medarde A., Esteban L.M., Nunez A., Porteros A., Tessarollo L.,
RA Santos E.;
RT "Targeted disruption of Ras-Grf2 shows its dispensability for mouse growth
RT and development.";
RL Mol. Cell. Biol. 22:2498-2504(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH RAS AND RAC1.
RX PubMed=9707409; DOI=10.1016/s0960-9822(07)00376-4;
RA Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
RT "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent
RT mitogen-activated protein kinase pathways.";
RL Curr. Biol. 8:935-938(1998).
RN [6]
RP INTERACTION WITH RASGRF1.
RX PubMed=10373510; DOI=10.1128/mcb.19.7.4611;
RA Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E., Lowy D.R.;
RT "Ras-specific exchange factor GRF: oligomerization through its Dbl homology
RT domain and calcium-dependent activation of Raf.";
RL Mol. Cell. Biol. 19:4611-4622(1999).
RN [7]
RP FUNCTION.
RX PubMed=10733575; DOI=10.1128/mcb.20.8.2727-2733.2000;
RA de Hoog C.L., Fan W.-T., Goldstein M.D., Moran M.F., Koch C.A.;
RT "Calmodulin-independent coordination of Ras and extracellular signal-
RT regulated kinase activation by Ras-GRF2.";
RL Mol. Cell. Biol. 20:2727-2733(2000).
RN [8]
RP FUNCTION.
RX PubMed=11500499; DOI=10.1074/jbc.m104658200;
RA Gotoh T., Tian X., Feig L.A.;
RT "Prenylation of target GTPases contributes to signaling specificity of Ras-
RT guanine nucleotide exchange factors.";
RL J. Biol. Chem. 276:38029-38035(2001).
RN [9]
RP INTERACTION WITH EPB49.
RX PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
RA Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
RA Boukharov A.A., Hanada T., Chishti A.H.;
RT "Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2
RT and modulates mitogen-activated protein kinase pathways.";
RL Eur. J. Biochem. 269:638-649(2002).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15029245; DOI=10.1038/sj.emboj.7600151;
RA Tian X., Gotoh T., Tsuji K., Lo E.H., Huang S., Feig L.A.;
RT "Developmentally regulated role for Ras-GRFs in coupling NMDA glutamate
RT receptors to Ras, Erk and CREB.";
RL EMBO J. 23:1567-1575(2004).
RN [11]
RP PHOSPHORYLATION BY CDK5.
RX PubMed=15128856; DOI=10.1523/jneurosci.0690-04.2004;
RA Kesavapany S., Amin N., Zheng Y.-L., Nijhara R., Jaffe H., Sihag R.,
RA Gutkind J.S., Takahashi S., Kulkarni A., Grant P., Pant H.C.;
RT "p35/cyclin-dependent kinase 5 phosphorylation of ras guanine nucleotide
RT releasing factor 2 (RasGRF2) mediates Rac-dependent extracellular signal-
RT regulated kinase 1/2 activity, altering RasGRF2 and microtubule-associated
RT protein 1b distribution in neurons.";
RL J. Neurosci. 24:4421-4431(2004).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14749369; DOI=10.1128/mcb.24.4.1516-1530.2004;
RA Arozarena I., Matallanas D., Berciano M.T., Sanz-Moreno V., Calvo F.,
RA Munoz M.T., Egea G., Lafarga M., Crespo P.;
RT "Activation of H-Ras in the endoplasmic reticulum by the RasGRF family
RT guanine nucleotide exchange factors.";
RL Mol. Cell. Biol. 24:1516-1530(2004).
RN [13]
RP INTERACTION WITH MICROTUBULES.
RX PubMed=16649990; DOI=10.1111/j.1742-4658.2006.05226.x;
RA Forlani G., Baldassa S., Lavagni P., Sturani E., Zippel R.;
RT "The guanine nucleotide exchange factor RasGRF1 directly binds microtubules
RT via DHPH2-mediated interaction.";
RL FEBS J. 273:2127-2138(2006).
RN [14]
RP FUNCTION, AND INTERACTION WITH GRIA1.
RX PubMed=16407208; DOI=10.1074/jbc.m512060200;
RA Tian X., Feig L.A.;
RT "Age-dependent participation of Ras-GRF proteins in coupling calcium-
RT permeable AMPA glutamate receptors to Ras/Erk signaling in cortical
RT neurons.";
RL J. Biol. Chem. 281:7578-7582(2006).
RN [15]
RP FUNCTION.
RX PubMed=16467520; DOI=10.1523/jneurosci.3990-05.2006;
RA Li S., Tian X., Hartley D.M., Feig L.A.;
RT "Distinct roles for Ras-guanine nucleotide-releasing factor 1 (Ras-GRF1)
RT and Ras-GRF2 in the induction of long-term potentiation and long-term
RT depression.";
RL J. Neurosci. 26:1721-1729(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725; SER-726; SER-745;
RP SER-749; SER-801; SER-805 AND SER-924, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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).
CC -!- FUNCTION: Functions as a calcium-regulated nucleotide exchange factor
CC activating both Ras and RAC1 through the exchange of bound GDP for GTP.
CC Preferentially activates HRAS in vivo compared to RRAS based on their
CC different types of prenylation. Functions in synaptic plasticity by
CC contributing to the induction of long term potentiation.
CC {ECO:0000269|PubMed:10733575, ECO:0000269|PubMed:11500499,
CC ECO:0000269|PubMed:14749369, ECO:0000269|PubMed:15029245,
CC ECO:0000269|PubMed:16407208, ECO:0000269|PubMed:16467520,
CC ECO:0000269|PubMed:9032266, ECO:0000269|PubMed:9707409}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with RASGRF1. Interacts with
CC Ras and RAC1. Interacts in a calcium-dependent manner with calmodulin.
CC Interacts with EPB49 and probably CDK5R1. Interacts with the AMPA
CC receptor through GRIA1. Interacts with microtubules.
CC {ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11856323,
CC ECO:0000269|PubMed:16407208, ECO:0000269|PubMed:16649990,
CC ECO:0000269|PubMed:9032266, ECO:0000269|PubMed:9707409}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
CC Note=Translocates to membranes when activated. Found both at cell
CC periphery and along the axon of neurons (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain in the nucleus of the solitary
CC tract. Not observed in the hippocampus (at protein level).
CC {ECO:0000269|PubMed:11909944}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in the cortex from birth to
CC adulthood. {ECO:0000269|PubMed:15029245}.
CC -!- DOMAIN: The Ras-GEF domain and the N-terminal Ras-GEF domain form a
CC Ras-binding site and mediate Ras activation. {ECO:0000250}.
CC -!- DOMAIN: The IQ domain mediates the calcium-dependent interaction with
CC calmodulin but is dispensable for the Ras-GEF activity.
CC -!- DOMAIN: The DH (DBL-homology) domain mediates interaction with RASGRF1
CC and probably EPB49 and is required for RAC1 activation.
CC -!- PTM: Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1
CC activation. {ECO:0000269|PubMed:11238945, ECO:0000269|PubMed:15128856}.
CC -!- PTM: Ubiquitinated upon interaction with Ras. Ubiquitination leads to
CC degradation through the 26S proteasome. {ECO:0000269|PubMed:11238945}.
CC -!- DISRUPTION PHENOTYPE: Mice do not display overt phenotype.
CC {ECO:0000269|PubMed:11909944, ECO:0000269|PubMed:15029245}.
CC -!- MISCELLANEOUS: Preferentially activates HRAS in vivo compared to R-RAS
CC based on their different types of prenylation.
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DR EMBL; U67326; AAC53058.2; -; mRNA.
DR EMBL; AK158472; BAE34529.1; -; mRNA.
DR EMBL; AH008805; AAF18297.1; -; Genomic_DNA.
DR PIR; T42726; T42726.
DR RefSeq; NP_033053.2; NM_009027.3.
DR AlphaFoldDB; P70392; -.
DR SMR; P70392; -.
DR BioGRID; 202601; 1.
DR IntAct; P70392; 4.
DR STRING; 10090.ENSMUSP00000096930; -.
DR iPTMnet; P70392; -.
DR PhosphoSitePlus; P70392; -.
DR SwissPalm; P70392; -.
DR MaxQB; P70392; -.
DR PeptideAtlas; P70392; -.
DR PRIDE; P70392; -.
DR ProteomicsDB; 255191; -.
DR Antibodypedia; 12760; 40 antibodies from 13 providers.
DR DNASU; 19418; -.
DR Ensembl; ENSMUST00000151408; ENSMUSP00000116892; ENSMUSG00000021708.
DR GeneID; 19418; -.
DR KEGG; mmu:19418; -.
DR UCSC; uc029sco.1; mouse.
DR CTD; 5924; -.
DR MGI; MGI:109137; Rasgrf2.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000155679; -.
DR InParanoid; P70392; -.
DR OMA; WMKVDKM; -.
DR OrthoDB; 70788at2759; -.
DR PhylomeDB; P70392; -.
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-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 19418; 2 hits in 52 CRISPR screens.
DR PRO; PR:P70392; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P70392; protein.
DR Bgee; ENSMUSG00000021708; Expressed in subparaventricular zone and 140 other tissues.
DR ExpressionAtlas; P70392; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IGI:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR030744; RasGRF2.
DR PANTHER; PTHR23113; PTHR23113; 2.
DR PANTHER; PTHR23113:SF187; PTHR23113:SF187; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Calcium; Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1189
FT /note="Ras-specific guanine nucleotide-releasing factor 2"
FT /id="PRO_0000312864"
FT DOMAIN 22..133
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 205..234
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 243..429
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 470..588
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 635..755
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 954..1186
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 713..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..751
FT /note="Regulates proteasomal degradation"
FT REGION 757..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1080
FT /note="Responsible of the affinity for farnesylated versus
FT geranylgeranylated Ras"
FT COILED 158..193
FT /evidence="ECO:0000255"
FT COMPBIAS 757..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O14827"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 1022
FT /note="R->E: Loss of interaction with Ras. Loss of Ras
FT activation. Loss of ubiquitination."
FT /evidence="ECO:0000269|PubMed:11238945"
FT MUTAGEN 1092
FT /note="R->E: Partial loss of interaction with Ras. Partial
FT loss of Ras activation. Partial loss of ubiquitination."
FT /evidence="ECO:0000269|PubMed:11238945"
FT CONFLICT 1023
FT /note="A -> P (in Ref. 4; AAF18297)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="A -> P (in Ref. 4; AAF18297)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="K -> R (in Ref. 2; BAE34529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="D -> N (in Ref. 2; BAE34529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1189 AA; 135668 MW; 42E346B623F18E59 CRC64;
MQKSVRYNEG HALYLAMLAR KEGTKRGFLS KKAAEASRWH EKWFALYQNV LFYFEGEQSG
RPAGMYLLEG CSCERTPAPP RTNAGPAGAR DALDKQYYFT VLFGHDGQKP LELRCEEEQA
GKEWMEAIHQ ASYADILIER EVLMQKYIHL VQIVETEKIA TNQLRHQLED QDTEIERLKS
EIVALNKTKE RMRPYHVHQE EEDPDIKKIK KVQSFMRGWL CRRKWKTIVQ DYICSPHAES
MRKRNQIVFT MVEAETEYVH QLYILVNGFL RPLRMAASSK KPPINHDDVS SIFLNSETIM
FLHEIFHQGL KARLANWPTL VLADLFDILL PMLNIYQEFV RNHQYSLQVL ANCKQNRDFD
KLLKQYEANP ACEGRMLETF LTYPMFQIPR YIITLHELLA HTPHEHVERK SLEFAKSKLE
ELSRVMHDEV SDTENIRKNL AIERMIVEGC DILLDTSQTF IRQGSLIQVP SVERGKLSKV
RLGSLSLKKE GERQCFLFTK HFLICTRSSG GKLHLLKTGG VLSLIQCTLI EEPDGSDDDP
KGSGHMFGHL DFKIVVEPPD AASFTVVLLA PSRQEKAAWM SDISQCVDNI RCNGLMTIVF
EENSKVTVPH MIKSDARLHK DDTDICFSKT LNSCKVPQIR YASVERLLER LTDLRFLSID
FLNTFLHTYR IFTTATVVLA KLSDIYKRPF TSIPVRSLEL FFATSQNNRE HLVDGKSPRL
CRKFSSPPPL AVSRTSSPVR ARKLSLTSSL NSRIGALDLT NSSSSSSPTT TTHSPAASPP
PHTAVLESAP ADKAGDSADM SPCRSPTTPR HLRYRQPGGQ VADSAHCSVS PASAFAIATA
AAGHGSPPGF NNERTCDKEF IIRRTATNRV LNVLRHWVSK HAQDFELNNE LKMNVLNLLE
EVLRDPDLLP QERKATANIL RALSQDDQDD IHLKLEDIIQ MTDCPKAECF ETLSAMELAE
QITLLDHIVF RSIPYEEFLG QGWMKLDKNE RTPYIMKTSQ HFNEMSNLVA SQIMNYADIS
SRANAIEKWV AVADICRCLH NYNGVLEITS ALNRSAIYRL KKTWAKVSKQ TKALMDKLQK
TVSSEGRFKN LRETLKNCNP PAVPYLGMYL TDLAFIEEGT PNFTEEGLVN FSKMRMISHI
IREIRQFQQT AYRIDQQPKV IQYLLDKALV IDEDSLYELS LKIEPRLPA
