ATR_MOUSE
ID ATR_MOUSE Reviewed; 2635 AA.
AC Q9JKK8; Q3TBS8; Q3TNX3; Q3TZM6; Q3UT26; Q3V1V6; Q571L3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase ATR;
DE EC=2.7.11.1;
DE AltName: Full=Ataxia telangiectasia and Rad3-related protein;
GN Name=Atr; Synonyms=Kiaa4069;
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] OF 1-1134 AND 1578-2635.
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain, Dendritic cell, Egg, Embryo, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1684-2635.
RC TISSUE=Embryonic intestine;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2362-2635, AND FUNCTION.
RX PubMed=10801416; DOI=10.1016/s0960-9822(00)00447-4;
RA de Klein A., Muijtjens M., van Os R., Verhoeven Y., Smit B., Carr A.M.,
RA Lehmann A.R., Hoeijmakers J.H.J.;
RT "Targeted disruption of the cell-cycle checkpoint gene ATR leads to early
RT embryonic lethality in mice.";
RL Curr. Biol. 10:479-482(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8843195; DOI=10.1101/gad.10.19.2423;
RA Keegan K.S., Holtzman D.A., Plug A.W., Christenson E.R., Brainerd E.E.,
RA Flaggs G., Bentley N.J., Taylor E.M., Meyn M.S., Moss S.B., Carr A.M.,
RA Ashley T., Hoekstra M.F.;
RT "The Atr and Atm protein kinases associate with different sites along
RT meiotically pairing chromosomes.";
RL Genes Dev. 10:2423-2437(1996).
RN [6]
RP FUNCTION.
RX PubMed=10691732;
RA Brown E.J., Baltimore D.;
RT "ATR disruption leads to chromosomal fragmentation and early embryonic
RT lethality.";
RL Genes Dev. 14:397-402(2000).
RN [7]
RP FUNCTION.
RX PubMed=12629044; DOI=10.1101/gad.1067403;
RA Brown E.J., Baltimore D.;
RT "Essential and dispensable roles of ATR in cell cycle arrest and genome
RT maintenance.";
RL Genes Dev. 17:615-628(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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 INTERACTION WITH ATRIP.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=23039116; DOI=10.1111/gtc.12005;
RA Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.;
RT "HORMAD2 is essential for synapsis surveillance during meiotic prophase via
RT the recruitment of ATR activity.";
RL Genes Cells 17:897-912(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22549958; DOI=10.1101/gad.187559.112;
RA Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J.,
RA Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.;
RT "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
RT monitored by distinct HORMAD2-independent and -dependent mechanisms.";
RL Genes Dev. 26:958-973(2012).
RN [12]
RP FUNCTION.
RX PubMed=29125140; DOI=10.1038/cr.2017.139;
RA Zhao B., Zhang W., Cun Y., Li J., Liu Y., Gao J., Zhu H., Zhou H.,
RA Zhang R., Zheng P.;
RT "Mouse embryonic stem cells have increased capacity for replication fork
RT restart driven by the specific Filia-Floped protein complex.";
RL Cell Res. 28:69-89(2018).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53,
CC which collectively inhibit DNA replication and mitosis and promote DNA
CC repair, recombination and apoptosis. Phosphorylates 'Ser-139' of
CC histone variant H2AX at sites of DNA damage, thereby regulating DNA
CC damage response mechanism. Required for FANCD2 ubiquitination. Critical
CC for maintenance of fragile site stability and efficient regulation of
CC centrosome duplication (By similarity). Positively regulates the
CC restart of stalled replication forks following activation by the KHDC3-
CC OOEP scaffold complex (PubMed:29125140). Essential for preventing the
CC occurrence of DNA damage during early embryogenesis.
CC {ECO:0000250|UniProtKB:Q13535, ECO:0000269|PubMed:10691732,
CC ECO:0000269|PubMed:10801416, ECO:0000269|PubMed:12629044,
CC ECO:0000269|PubMed:29125140, ECO:0000269|PubMed:8843195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q13535};
CC -!- ACTIVITY REGULATION: Serine/threonine-protein kinase activity is
CC directly stimulated by TOPBP1. ATR kinase activity is also directly
CC activated by ETAA1, independently of TOPBP1. Activated by DNA and
CC inhibited by BCR-ABL oncogene. Slightly activated by ATRIP. Inhibited
CC by caffeine, wortmannin and LY294002. {ECO:0000250|UniProtKB:Q13535}.
CC -!- SUBUNIT: Forms a heterodimer with ATRIP (PubMed:20801936). Binds to
CC DNA, and to UV-damaged DNA with higher affinity. Interacts with RAD17,
CC MSH2 and HDAC2. Present in a complex containing ATRIP and RPA-coated
CC single-stranded DNA. Present in a complex containing CHD4 and HDAC2.
CC Interacts with EEF1E1, the interaction is enhanced by UV irradiation.
CC Interacts with CLSPN and CEP164 (By similarity). Interacts with TELO2
CC AND TTI1 (By similarity). Interacts with UHRF2; this interaction
CC promotes ATR activation (By similarity). {ECO:0000250|UniProtKB:Q13535,
CC ECO:0000269|PubMed:20801936}.
CC -!- INTERACTION:
CC Q9JKK8; Q8BMG1: Atrip; NbExp=2; IntAct=EBI-1202426, EBI-5235246;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC {ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:23039116,
CC ECO:0000269|PubMed:8843195}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is highest in testis, where
CC it is restricted to primary spermatocytes. Expression decreases as
CC spermiogenesis proceeds (at protein level).
CC {ECO:0000269|PubMed:8843195}.
CC -!- PTM: Phosphorylated; autophosphorylates in vitro.
CC {ECO:0000250|UniProtKB:Q13535}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {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; AC091531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK132223; BAE21043.1; -; mRNA.
DR EMBL; AK139834; BAE24154.1; -; mRNA.
DR EMBL; AK157754; BAE34182.1; -; mRNA.
DR EMBL; AK164916; BAE37964.1; -; mRNA.
DR EMBL; AK171072; BAE42229.1; -; mRNA.
DR EMBL; AK220176; BAD90361.1; -; mRNA.
DR EMBL; AF236887; AAF61728.1; -; mRNA.
DR AlphaFoldDB; Q9JKK8; -.
DR SMR; Q9JKK8; -.
DR ComplexPortal; CPX-3623; ATR-ATRIP DNA damage-sensing kinase complex.
DR IntAct; Q9JKK8; 2.
DR STRING; 10090.ENSMUSP00000034980; -.
DR iPTMnet; Q9JKK8; -.
DR PhosphoSitePlus; Q9JKK8; -.
DR EPD; Q9JKK8; -.
DR MaxQB; Q9JKK8; -.
DR PaxDb; Q9JKK8; -.
DR PRIDE; Q9JKK8; -.
DR ProteomicsDB; 277199; -.
DR MGI; MGI:108028; Atr.
DR eggNOG; KOG0890; Eukaryota.
DR InParanoid; Q9JKK8; -.
DR PhylomeDB; Q9JKK8; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR ChiTaRS; Atr; mouse.
DR PRO; PR:Q9JKK8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JKK8; protein.
DR GO; GO:0070310; C:ATR-ATRIP complex; IPI:ComplexPortal.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0001741; C:XY body; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032405; F:MutLalpha complex binding; ISO:MGI.
DR GO; GO:0032407; F:MutSalpha complex binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IDA:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0097694; P:establishment of RNA localization to telomere; ISO:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISO:MGI.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IC:ComplexPortal.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:1904884; P:positive regulation of telomerase catalytic core complex assembly; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding; Kinase;
KW Manganese; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2635
FT /note="Serine/threonine-protein kinase ATR"
FT /id="PRO_0000088845"
FT REPEAT 799..835
FT /note="HEAT 1"
FT REPEAT 1329..1365
FT /note="HEAT 2"
FT DOMAIN 1634..2179
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2287..2595
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2603..2635
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 423..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2299
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2463..2471
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2483..2507
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13535"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13535"
FT CONFLICT 19
FT /note="G -> A (in Ref. 2; BAE24154/BAE34182/BAE42229)"
FT /evidence="ECO:0000305"
FT CONFLICT 2208
FT /note="D -> E (in Ref. 2; BAE37964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2347
FT /note="R -> C (in Ref. 2; BAE37964)"
FT /evidence="ECO:0000305"
FT CONFLICT 2556
FT /note="G -> W (in Ref. 2; BAE21043 and 3; BAD90361)"
FT /evidence="ECO:0000305"
FT CONFLICT 2563
FT /note="H -> R (in Ref. 2; BAE21043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2635 AA; 300224 MW; C126413D15ACB8DC CRC64;
MGDHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV VALELVKKTD
AQPTSVMLLD FIQHIMKSSP LMFVNVNGSQ GQNEAKDSCI EFSHWIITRL LRIAATPSCH
MLHKKICEVI CSLLFLFKSK NPAIFGVLTR ELLYLFEDLI YLHKRNAVGE VMEWPVVVSR
FLSRLDEHMG CLQPAPLQFM NVQNVEFIEV TLLMVLIHIV PTVFFRRQEL LLWQIGCALL
EHGSPKIRSL AISLLTELFE LGGLPAQPAS TFFSLFLELL QHLVGMDADQ LKLYEEPLSK
LLKTLFPFEA EAYRNIEPVY LNVLLEKLSV MFEDRVLMRL KSDLLKAALC HLLQYFLTFV
PAGYESALQV RKVYVTNICR ALVDALGVQK HVGYLLGPFY AALKMESKEI IERIQCQAQQ
ENLSGNNDEV SPKRRKLSSS LSSYKKPSRQ PEEIIHVDMD KKSILWNVLK QKAESLQISL
ECGTLKNSVA EALEGITVVL QLTALCTVHC SHQDMDGHNV KDHQHKYKKK PPVVVTWMSL
DFYTKVLKSC RSLLESVQKL ELELVIDSMV RICDALMYMQ VKSSFKDHVL EELCGMLSLP
WIYSYSDDNS LKMTTFATNL LPLSQRVWDS YSPQAQSKCV FLLTLFPRRI FLEWRTAVYN
WALKSSHEVI RASCVKGFFI LLHQQNSCNQ IPKMLVDRVK DDSDMVKKEF ASVLGQLVCT
LHGMFYLSSS VEPCFEHMDL FSKNLKATSQ HECSSSQVKA STCKPFLFLL TKNTPSPVKL
AFIDNLHHLC KHLDFQEDER EVKAVLGTLL NLMEDPDKDV RIAFSGNIKY ILESLNSEDG
FVKELFVLRM KEAYTHAQIA RNNELKDTLI LTTGDIGRAA KGDLIPFALL HLLHCLLSKS
ASVSGAAYTE IRALVAAKSV KLQNFFSQYK KPICQFLVES LHSSQMTALP SAPCQSSEIR
KQDVAHHREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP DLAAKASPAA SALIRTLGKQ
LNVSRREILI NNFKYIFSHL VCSCSKDELE RALHYLKNET EIELGSLLRQ DFQGLHNELL
LRIGEHYQQV FNGLSILASF ASSDDPYQGP RDITSPELMA DYLQPKLLGI LAFFNMQLLS
SSVGIEDKKM ALTSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV
RCLDHAYLGP LLSHVIVALL PLIHMQPKET AAIFHYLIIE NRDAVQDFLH EIYFLPDHPE
LEKIKAVLQE YRKETSETTD LQTTLQLSMK AIQHENVDVR IHALTSLKET LYKNQEKLIK
YATDSETVEP VISQLVTVIL KGCQDANSQA RLLCGECLGE LGAIDPGRLD FSTTETQGKD
FTFVTGVEDL SFAYGLLMEL TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMQSNGPGY
QLWKRFPEHV REILEPHLNT RYKSSQKSTD WSGVTKPIYL SKLGNNFAEW SSSWAGYLIT
KVRDNLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA EIMAVLKHDE
QHAISTQDSA SDLCQLSTQT VFSVLDHLTQ WARHKFQALN AEKLAQNKPK GVSNVNFEDY
QSVTRFLDLI PQDTLAVASF RSKAYTRAVM HFESFITEKK QNIQKHLGFL QKLYAAMHEP
DGVAGVSAIR KAEPSLKEQI LEHESIGLLR DATACYDRAI QLEPDQIIHY HGVVKSMLGL
GQLSTVITQV NGVHANRSEW TDELNTYRVE AAWKLSQWDL VENYLAADGK STTWSVRLGQ
LLLSAKKRDT TTFYDTLKLV RAEQIVPLSA ASFERGSYQR GYEFIVRLHM LCELEHSLKP
LFRKSPGDSC NEDSLNWGAR LEMTQNSYRA KEPILALRRA LLSLNKRPDY NEMVGECWLQ
SARVARKAGH HQTAYNALLN AGESRLAELY VERAKWLWSK GDVHQALIVL QKGVELCFPE
NKSPSESKHM LIHGRATLLV GRFMEETANF ESNAVMKKYK DVTLFLPEWE DGHFYLAKYY
DKLMPMVTDN KMEKQGDLIR YIVLHFGRSL QYGNQFIYQS MPRMLSLWLD FGAKAYEWEK
GGRSDRLQMR NDLAKINSVL TEHTNRLAPY QFLTAFSQLI SRICHSHDEV FVVLMEIIAK
VFLAYPQQAM WMMTAVSKSS YPMRVNRCKE ILTKAIHMKK SLEKFVGDAT RLTDKLLELC
NKSVDGSNST LSMSTHFKML KRLVEDPTFS EILIPLQSVM IPTLPSVLGA HANHDPFPGH
WAYLAGFDDV VEILSSLQKP KKISLKGSDG KFYIMMCKPK DDLRKDCRLM EFNSLINKSL
RKDAESRRRE LHIRTYAVIP LNDECGIIEW VNNTAGLRPI LTKIYKEKGV YMTGKELRQC
MLPKSAALSE KLKVFQELLL PRHPPVFHEW FLRTFPDPTS WYSSRSAYCR STAVMSMVGY
ILGLGDRHGE NILFDSFTGE CVHVDFNCLF NKGETFEVPE IVPFRLTHNM VNGMGPMGTE
GLFRRACEVT LRLMRDQREP LMSVLKTFLH DPLVEGSKPV KGHSKAPLNE TGEVVNEKAK
THVLDIEQRL QGVIKTRNRV TGLPLSIEGH VHYLIQEATD ENLLCQMYLG WTPYM
