RAD50_MOUSE
ID RAD50_MOUSE Reviewed; 1312 AA.
AC P70388; Q6PEB0; Q8C2T7; Q9CU59;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA repair protein RAD50;
DE Short=mRad50;
DE EC=3.6.-.-;
GN Name=Rad50;
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] (ISOFORMS 1; 3 AND 4), PROTEIN SEQUENCE OF
RP 113-120; 132-140; 175-202; 230-248; 295-310; 815-832; 840-845; 1012-1026
RP AND 1079-1089, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8910585; DOI=10.1074/jbc.271.46.29255;
RA Kim K.K., Daud A.I., Wong S.C., Pajak L., Tsai S.-C., Wang H., Henzel W.J.,
RA Field L.J.;
RT "Mouse RAD50 has limited epitopic homology to p53 and is expressed in the
RT adult myocardium.";
RL J. Biol. Chem. 271:29255-29264(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-214 AND 443-743 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 1-722 (ISOFORM 2).
RC STRAIN=NMRI; 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10377422; DOI=10.1073/pnas.96.13.7376;
RA Luo G., Yao M.S., Bender C.F., Mills M., Bladl A.R., Bradley A.,
RA Petrini J.H.J.;
RT "Disruption of mRad50 causes embryonic stem cell lethality, abnormal
RT embryonic development, and sensitivity to ionizing radiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7376-7381(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF LYS-22.
RX PubMed=12208847; DOI=10.1101/gad.1007902;
RA Bender C.F., Sikes M.L., Sullivan R., Huye L.E., Le Beau M.M., Roth D.B.,
RA Mirzoeva O.K., Oltz E.M., Petrini J.H.J.;
RT "Cancer predisposition and hematopoietic failure in Rad50(S/S) mice.";
RL Genes Dev. 16:2237-2251(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [8]
RP INTERACTION WITH CYREN.
RX PubMed=30017584; DOI=10.1016/j.molcel.2018.06.018;
RA Hung P.J., Johnson B., Chen B.R., Byrum A.K., Bredemeyer A.L.,
RA Yewdell W.T., Johnson T.E., Lee B.J., Deivasigamani S., Hindi I.,
RA Amatya P., Gross M.L., Paull T.T., Pisapia D.J., Chaudhuri J.,
RA Petrini J.J.H., Mosammaparast N., Amarasinghe G.K., Zha S., Tyler J.K.,
RA Sleckman B.P.;
RT "MRI is a DNA damage response adaptor during classical non-homologous end
RT joining.";
RL Mol. Cell 71:332-342(2018).
CC -!- FUNCTION: Component of the MRN complex, which plays a central role in
CC double-strand break (DSB) repair, DNA recombination, maintenance of
CC telomere integrity and meiosis. The complex possesses single-strand
CC endonuclease activity and double-strand-specific 3'-5' exonuclease
CC activity, which are provided by MRE11. RAD50 may be required to bind
CC DNA ends and hold them in close proximity. This could facilitate
CC searches for short or long regions of sequence homology in the
CC recombining DNA templates, and may also stimulate the activity of DNA
CC ligases and/or restrict the nuclease activity of MRE11 to prevent
CC nucleolytic degradation past a given point. The complex may also be
CC required for DNA damage signaling via activation of the ATM kinase. In
CC telomeres the MRN complex may modulate t-loop formation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10377422,
CC ECO:0000269|PubMed:12208847}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC RAD50/MRE11 associated with a single NBN (By similarity). As part of
CC the MRN complex, interacts with MCM8 and MCM9; the interaction recruits
CC the complex to DNA repair sites (By similarity). Component of the BASC
CC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50,
CC MRE11 and NBN (By similarity). Found in a complex with TERF2 (By
CC similarity). Interacts with RINT1 (By similarity). Interacts with BRCA1
CC via its N-terminal domain (By similarity). Interacts with
CC DCLRE1C/Artemis (By similarity). Interacts with MRNIP (By similarity).
CC Interacts with CYREN (via XLF motif) (PubMed:30017584).
CC {ECO:0000250|UniProtKB:Q92878, ECO:0000269|PubMed:30017584}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome
CC {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci
CC after treatment with genotoxic agents. {ECO:0000250|UniProtKB:Q92878}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P70388-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70388-2; Sequence=VSP_012593;
CC Name=3; Synonyms=3.1 kb splice variant;
CC IsoId=P70388-3; Sequence=VSP_012592;
CC Name=4; Synonyms=1.6 kb splice variant;
CC IsoId=P70388-4; Sequence=VSP_012594, VSP_012595;
CC -!- TISSUE SPECIFICITY: In adult, it is expressed at very low level in most
CC tissues, except in heart, lung and aorta. Expressed at high level in
CC testis. {ECO:0000269|PubMed:8910585}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed. Expressed at higher level in
CC heart, liver and thymus from 18 dpc. By neonatal day 1.5, it decreases
CC in brain, liver, gut and skin, while it is expressed in spleen.
CC {ECO:0000269|PubMed:8910585}.
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC coil regions, contains 2 Cys residues that coordinate one molecule of
CC zinc with the help of the 2 Cys residues of the zinc-hook of another
CC RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of
CC the homodimer, which constitute the ATP-binding domain, interact with
CC the MRE11 homodimer (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Defects cause embryonic stem cell lethality,
CC abnormal embryonic development and sensitivity to ionizing radiation.
CC {ECO:0000269|PubMed:10377422}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR EMBL; U66887; AAC52894.1; -; mRNA.
DR EMBL; AK018001; BAB31030.1; -; mRNA.
DR EMBL; AK087982; BAC40074.1; -; mRNA.
DR EMBL; BC058180; AAH58180.1; -; mRNA.
DR CCDS; CCDS24684.1; -. [P70388-1]
DR PIR; T30845; T30845.
DR AlphaFoldDB; P70388; -.
DR SMR; P70388; -.
DR ComplexPortal; CPX-4703; MRN complex.
DR DIP; DIP-46805N; -.
DR IntAct; P70388; 4.
DR STRING; 10090.ENSMUSP00000020649; -.
DR iPTMnet; P70388; -.
DR PhosphoSitePlus; P70388; -.
DR EPD; P70388; -.
DR MaxQB; P70388; -.
DR PaxDb; P70388; -.
DR PeptideAtlas; P70388; -.
DR PRIDE; P70388; -.
DR ProteomicsDB; 300229; -. [P70388-1]
DR ProteomicsDB; 300230; -. [P70388-2]
DR ProteomicsDB; 300231; -. [P70388-3]
DR ProteomicsDB; 300232; -. [P70388-4]
DR UCSC; uc011xus.1; mouse. [P70388-2]
DR MGI; MGI:109292; Rad50.
DR eggNOG; KOG0962; Eukaryota.
DR InParanoid; P70388; -.
DR PhylomeDB; P70388; -.
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR ChiTaRS; Rad50; mouse.
DR PRO; PR:P70388; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70388; protein.
DR GO; GO:0070533; C:BRCA1-C complex; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0098687; C:chromosomal region; IC:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0030870; C:Mre11 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
DR GO; GO:0000729; P:DNA double-strand break processing; IC:ComplexPortal.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IC:ComplexPortal.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IC:ComplexPortal.
DR GO; GO:1904354; P:negative regulation of telomere capping; ISO:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:0000019; P:regulation of mitotic recombination; ISO:MGI.
DR GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0031860; P:telomeric 3' overhang formation; ISO:MGI.
DR CDD; cd03240; ABC_Rad50; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Chromosome;
KW Coiled coil; Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
KW Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Zinc.
FT CHAIN 1..1312
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000138642"
FT DOMAIN 635..734
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT COILED 200..532
FT /evidence="ECO:0000255"
FT COILED 635..673
FT /evidence="ECO:0000255"
FT COILED 706..734
FT /evidence="ECO:0000255"
FT COILED 776..942
FT /evidence="ECO:0000255"
FT COILED 1043..1075
FT /evidence="ECO:0000255"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 959
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92878"
FT VAR_SEQ 1..886
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8910585"
FT /id="VSP_012592"
FT VAR_SEQ 485..545
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012593"
FT VAR_SEQ 485..496
FT /note="ERELSKAEKNSS -> IYFLELVRWLSG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8910585"
FT /id="VSP_012594"
FT VAR_SEQ 497..1312
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8910585"
FT /id="VSP_012595"
FT MUTAGEN 22
FT /note="K->M: In Rad50S; hypomorphic allele that induces
FT growth defects and cancer predisposition. Homozygous
FT individuals die with complete bone marrow depletion as a
FT result of progressive hematopoietic stem cell failure."
FT /evidence="ECO:0000269|PubMed:12208847"
FT CONFLICT 97
FT /note="H -> Q (in Ref. 2; BAB31030)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> V (in Ref. 3; AAH58180)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="I -> V (in Ref. 2; BAC40074)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="E -> A (in Ref. 2; BAC40074)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="L -> K (in Ref. 3; AAH58180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1312 AA; 153488 MW; 4AF9AF9AD9E1D7A2 CRC64;
MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVAVHRSM LCSQKNKKTE FKTLEGVITR
MKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLASSQEI
VRSYEDELEP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT
DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKEARLLN QEKAELLVEQ GRLQLQADRH
QEHIRARDSL IQSLATHLEL DGFERGPFSE RQIKNFHELV KERQEREAKT ASQLLSDLTD
KEALKQRQLD ELRDRKSGLG RTIELKTEIL TKKQSELRHV RSELQQLEGS SDRILELDQE
LTKAERELSK AEKNSSIETL KAEVMSLQNE KADLDRSLRK LDQEMEQLNH HTTTRTQMEM
LTKDKTDKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
LASAEQNKNH INNELKKKEE QLSSYEDKLF DVCGSQDLES DLGRLKEEIE KSSKQRAMLA
GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
KKERRRDEML GLVPVRQSII DLKEKEIPEL RNRLQSVNRD IQRLKNDIEE QETLLGTIMP
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGVD LDRTVQQVNQ EKQEKQHRLD
TVTSKIELNR KLIQDQQEQI QHLKSKTNEL KSEKLQIATN LQRRQQMEEQ SVELSTEVQS
LNREIKDAKE QISPLETALE KLQQEKEELI HRKHTSNKMA QDKINDIKEK VKNIHGYMKD
IENYIQDGKD DYKKQKETEL NGVAVQLNEC EKHREKINKD MGTMRQDIDT QKIQERWLQD
NLTLRKRRDE LKEVEEEPKQ HLKEMGQMQV LQMKNEHQKL EENIDTIKRN HSLALGRQKG
YEDEILHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVEKFYRVK KNMDQCSEIV KCSISSLGSY VH
