TOPB1_MOUSE
ID TOPB1_MOUSE Reviewed; 1515 AA.
AC Q6ZQF0; Q6P6P0; Q80Y33; Q8BUI0; Q8BUK1; Q8R348; Q91VX3; Q922X8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DNA topoisomerase 2-binding protein 1;
DE AltName: Full=DNA topoisomerase II-beta-binding protein 1;
DE Short=TopBP1;
DE AltName: Full=DNA topoisomerase II-binding protein 1;
GN Name=Topbp1; Synonyms=Kiaa0259;
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 MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-1420.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Fetal limb, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-246.
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart, and Embryonic 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 [4]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15138768; DOI=10.1007/s00412-004-0277-5;
RA Reini K., Uitto L., Perera D., Moens P.B., Freire R., Syvaeoja J.E.;
RT "TopBP1 localises to centrosomes in mitosis and to chromosome cores in
RT meiosis.";
RL Chromosoma 112:323-330(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14718568; DOI=10.1091/mbc.e03-06-0444;
RA Perera D., Perez-Hidalgo L., Moens P.B., Reini K., Lakin N., Syvaeoja J.E.,
RA San-Segundo P.A., Freire R.;
RT "TopBP1 and ATR colocalization at meiotic chromosomes: role of TopBP1/Cut5
RT in the meiotic recombination checkpoint.";
RL Mol. Biol. Cell 15:1568-1579(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; SER-863 AND SER-890, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 [7]
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).
CC -!- FUNCTION: Required for DNA replication (By similarity). Plays a role in
CC the rescue of stalled replication forks and checkpoint control
CC (PubMed:14718568). Binds double-stranded DNA breaks and nicks as well
CC as single-stranded DNA (By similarity). Recruits the SWI/SNF chromatin
CC remodeling complex to E2F1-responsive promoters. Down-regulates E2F1
CC activity and inhibits E2F1-dependent apoptosis during G1/S transition
CC and after DNA damage (By similarity). Induces a large increase in the
CC kinase activity of ATR (By similarity). {ECO:0000250|UniProtKB:Q92547,
CC ECO:0000269|PubMed:14718568}.
CC -!- SUBUNIT: Interacts with POLE. Interacts with RAD9A. Interacts with
CC UBR5. Interacts with E2F1. Interacts with PML. Interacts with SMARCA2.
CC Interacts with SMARCA4. Interacts with RHNO1. May interact with TOP2B.
CC Interacts with TICRR. Interacts with HELB.
CC {ECO:0000250|UniProtKB:Q92547}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole.
CC Chromosome. Note=Has a uniform nuclear distribution during G phase.
CC Colocalizes with BRCA1 at stalled replication forks during S phase. In
CC mitotic cells it colocalizes with BRCA1 at spindle poles and
CC centrosomes during metaphase and anaphase. Detected in discrete foci
CC together with PML and numerous DNA repair enzymes after DNA damage by
CC alkylating agents, UV or gamma irradiation. Localizes to sites of DNA
CC damage in a H2AX-independent manner (By similarity). Detected on
CC unpaired autosomes in meiotic prophase cells. Detected on X and Y
CC chromosomes during later stages of prophase. Colocalizes with ATR and
CC H2AX at unsynapsed chromosome cores during prophase. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:15138768}.
CC -!- DEVELOPMENTAL STAGE: Levels increase during the first 3 weeks after
CC birth and remain high in the fourth week.
CC {ECO:0000269|PubMed:15138768}.
CC -!- PTM: Phosphorylated on serine and threonine residues in response to X-
CC ray irradiation. {ECO:0000250|UniProtKB:Q92547}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome. X-ray irradiation
CC reduces ubiquitination. {ECO:0000250|UniProtKB:Q92547}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07170.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC39345.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC97914.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129104; BAC97914.1; ALT_INIT; mRNA.
DR EMBL; BC006707; AAH06707.1; -; mRNA.
DR EMBL; BC007170; AAH07170.1; ALT_INIT; mRNA.
DR EMBL; BC026608; AAH26608.1; -; mRNA.
DR EMBL; BC049797; AAH49797.1; -; mRNA.
DR EMBL; BC062111; AAH62111.1; -; mRNA.
DR EMBL; AK084654; BAC39241.2; -; mRNA.
DR EMBL; AK085031; BAC39345.1; ALT_FRAME; mRNA.
DR CCDS; CCDS23453.1; -.
DR RefSeq; NP_795953.2; NM_176979.5.
DR RefSeq; XP_006511770.1; XM_006511707.3.
DR PDB; 5U6K; X-ray; 2.60 A; A/B/C/D/E/F/G/H=553-746.
DR PDBsum; 5U6K; -.
DR AlphaFoldDB; Q6ZQF0; -.
DR SMR; Q6ZQF0; -.
DR BioGRID; 231681; 13.
DR ComplexPortal; CPX-4721; BRCA1-B complex.
DR IntAct; Q6ZQF0; 10.
DR MINT; Q6ZQF0; -.
DR STRING; 10090.ENSMUSP00000035164; -.
DR iPTMnet; Q6ZQF0; -.
DR PhosphoSitePlus; Q6ZQF0; -.
DR EPD; Q6ZQF0; -.
DR MaxQB; Q6ZQF0; -.
DR PaxDb; Q6ZQF0; -.
DR PeptideAtlas; Q6ZQF0; -.
DR PRIDE; Q6ZQF0; -.
DR ProteomicsDB; 259157; -.
DR Antibodypedia; 8745; 328 antibodies from 32 providers.
DR DNASU; 235559; -.
DR Ensembl; ENSMUST00000035164; ENSMUSP00000035164; ENSMUSG00000032555.
DR GeneID; 235559; -.
DR KEGG; mmu:235559; -.
DR UCSC; uc009rgl.1; mouse.
DR CTD; 11073; -.
DR MGI; MGI:1920018; Topbp1.
DR VEuPathDB; HostDB:ENSMUSG00000032555; -.
DR eggNOG; KOG1929; Eukaryota.
DR GeneTree; ENSGT00940000157001; -.
DR HOGENOM; CLU_004165_1_0_1; -.
DR InParanoid; Q6ZQF0; -.
DR OMA; WLHACAE; -.
DR OrthoDB; 557169at2759; -.
DR PhylomeDB; Q6ZQF0; -.
DR TreeFam; TF326403; -.
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-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 235559; 25 hits in 113 CRISPR screens.
DR ChiTaRS; Topbp1; mouse.
DR PRO; PR:Q6ZQF0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6ZQF0; protein.
DR Bgee; ENSMUSG00000032555; Expressed in embryonic post-anal tail and 260 other tissues.
DR ExpressionAtlas; Q6ZQF0; baseline and differential.
DR Genevisible; Q6ZQF0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070532; C:BRCA1-B complex; ISO:MGI.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISA:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; ISO:MGI.
DR CDD; cd17737; BRCT_TopBP1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 9.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR044737; TopBP1_BRCT_1.
DR Pfam; PF00533; BRCT; 4.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR SMART; SM00292; BRCT; 8.
DR SUPFAM; SSF52113; SSF52113; 7.
DR PROSITE; PS50172; BRCT; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1515
FT /note="DNA topoisomerase 2-binding protein 1"
FT /id="PRO_0000072632"
FT DOMAIN 101..189
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 195..284
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 353..443
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 551..636
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 644..741
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 902..993
FT /note="BRCT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1255..1347
FT /note="BRCT 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 799..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1510..1513
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1033..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92547"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92547"
FT MOD_RES 851
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92547"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92547"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92547"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VARIANT 1420
FT /note="S -> P (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 324
FT /note="V -> I (in Ref. 2; AAH07170)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="T -> I (in Ref. 2; AAH07170)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="R -> L (in Ref. 2; AAH07170)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="D -> E (in Ref. 2; AAH07170)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="L -> P (in Ref. 2; AAH62111)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="M -> I (in Ref. 2; AAH07170)"
FT /evidence="ECO:0000305"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 568..579
FT /evidence="ECO:0007829|PDB:5U6K"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 616..625
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:5U6K"
FT TURN 648..651
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 661..673
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:5U6K"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 706..713
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 721..730
FT /evidence="ECO:0007829|PDB:5U6K"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5U6K"
SQ SEQUENCE 1515 AA; 168860 MW; E2E729D2E57B6F2F CRC64;
MSRNDQEPFL VKFLKSSDNS ECFFKALESI KELQSEDYLQ IITDEEALKI RENDKSLYIC
DRFSGTVFDH LKQLGCRIVG PQVVTFCMRH QQCVPRAEHP VYNMIMSDVT VSCTSLDKDK
REEVHKYVQM MGGRVYRDLN VSVTHLIAGE VGSKKYLVAA NLKKPILLPS WIKTLWEKSQ
EKKITKYTDV NMEDFKCPIF LGCIICVTGL NGIHRKTVQQ LTAKHGGQYM GQLKMNECTH
LIVQEPKGQK YECARRWNVH CVTLQWFHDS IEKGFCQDES IYKAETRVEA KMVPDTSTPT
AQSNAESHTL ADVSHISNIN GSCVNETMFG STTSKLECSL ENLENLDISM FQAPEDLLDG
CRIYLCGFSG RKLDKLRRLI NSGGGVRFNQ LNEDVTHVIV GDYDDDVRQF WSKSSHRPHV
VGAKWLLECF TKGYILPEES YIHTNYQPAG IAVSDQPGNQ TAVLDKSGSF SKSALVPAER
LQQADEDLLA QYGNDDSTMV EAKLSEALEP EVGPCPGSAH REPCDDSTHI SVQEENKSSV
SHCILDDSTV REEGLFSQKS FLVLGFSVEN KCNIVDIIRE HAGKIVSLPS RIVADYAVVP
LLGCEVDVTV GEVVTNTWLV TCIDNQTLVD PKSNPLFTPV SVMSGVTPLE DCVISFSQCV
GAERDSLVFL ANHLGASVQE FFVRKANAKK GMLASTHLIV KEPTGSKYEA AKKWSLPAVN
ISWLLETARI GKRADENHFL VDNAPKQEQV LETKIPNGVS SNPDLPAHPD AHLEIHRKKA
VTPLDMNRFQ SRAFRAVISQ QRGQDPTFPP VRQPLTKEPS LHLDTPSKFL SKDKLFKPSF
DVTDALAALE TPNAASQKRK LSSPLSEVIV RNLTVALANS SRNTDSHSAS PQLKGAHLEE
EETRKPLDSV VVCVSKKLSK KQSELNGVAA SLGAEYRWSF DETVTHFIYQ GRANDSNREY
KSAKERGVHI VSEHWLLECA QEYKHLPESL YPHTYNPKMS LDINTVQDGR LCNSRAPLAV
SASKDDGPDH LSVEGNETNT MGTNDKESPL LNGSGRDDCK GALTQALEMR ENFQKQLQEI
MSATCIVKTP AQKTCMSRSS CNSASSTPDS ARSVRSGRSR VLEALRQSRQ AVPDVNTEPS
QNEQIIWDDP TAREERARLA SNLQWPSDPT QHSELQVEIK MPDDSPSRKP VYHSEIAEQA
SCVTQAPGHP GSEEPEPPVA ERPLIPEPQA PAVASPLAKP PVAPQPADKI ETQEETHRKV
KKQYVFQMSS LNSQERIDYC RLIKDLGGSV IEKQCSDPSC THMVVGYPLR NEKYLASMAA
GKWVLHRSYL DACKTAGRFV QEEDYEWGSS SILDALPDVT EHQQKLALAA MRWRKRIQQS
QESGIVEGAF SGWKAILRVD RPREAGFKRL LQAGGAKVLS GHPEPLLKDA THLFCDFNKL
KPDDCRVFIA EATAQNMVCL KTEYIADYLM LESPPCADNY RVSEAALFHN KKGGPGLPQK
RKTPAENVVK RPRVH
