MCM9_MOUSE
ID MCM9_MOUSE Reviewed; 1134 AA.
AC Q2KHI9; Q3V370; Q6P6J6; Q9D344;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DNA helicase MCM9;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9NXL9};
DE AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=Mcm9; Synonyms=Mcmdc1;
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 486-1134 (ISOFORMS 1/2).
RC TISSUE=Limb;
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 PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Colon;
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 IDENTIFICATION.
RX PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
RA Lutzmann M., Maiorano D., Mechali M.;
RT "Identification of full genes and proteins of MCM9, a novel, vertebrate-
RT specific member of the MCM2-8 protein family.";
RL Gene 362:51-56(2005).
RN [5]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=15850810; DOI=10.1016/j.bbrc.2005.03.222;
RA Yoshida K.;
RT "Identification of a novel cell-cycle-induced MCM family protein MCM9.";
RL Biochem. Biophys. Res. Commun. 331:669-674(2005).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 3), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21987787; DOI=10.1073/pnas.1113524108;
RA Hartford S.A., Luo Y., Southard T.L., Min I.M., Lis J.T., Schimenti J.C.;
RT "Minichromosome maintenance helicase paralog MCM9 is dispensible for DNA
RT replication but functions in germ-line stem cells and tumor suppression.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17702-17707(2011).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22771120; DOI=10.1016/j.molcel.2012.05.048;
RA Lutzmann M., Grey C., Traver S., Ganier O., Maya-Mendoza A.,
RA Ranisavljevic N., Bernex F., Nishiyama A., Montel N., Gavois E.,
RA Forichon L., de Massy B., Mechali M.;
RT "MCM8- and MCM9-deficient mice reveal gametogenesis defects and genome
RT instability due to impaired homologous recombination.";
RL Mol. Cell 47:523-534(2012).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23401855; DOI=10.1128/mcb.01503-12;
RA Park J., Long D.T., Lee K.Y., Abbas T., Shibata E., Negishi M., Luo Y.,
RA Schimenti J.C., Gambus A., Walter J.C., Dutta A.;
RT "The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites to
RT facilitate homologous recombination.";
RL Mol. Cell. Biol. 33:1632-1644(2013).
RN [9]
RP FUNCTION.
RX PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA Latreille D., Mechali M.;
RT "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL Mol. Cell 59:831-839(2015).
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the
CC repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-
CC links (ICLs) by homologous recombination (HR) (PubMed:23401855,
CC PubMed:22771120). Required for DNA resection by the MRE11-RAD50-
CC NBN/NBS1 (MRN) complex at double-stranded DNA breaks to generate ssDNA
CC by recruiting the MRN complex to the repair site and by promoting the
CC complex nuclease activity (By similarity). Probably by regulating the
CC localization of the MNR complex, indirectly regulates the recruitment
CC of downstream effector RAD51 to DNA damage sites including DBSs and
CC ICLs (PubMed:22771120, PubMed:23401855). Acts as a helicase in DNA
CC mismatch repair (MMR) following DNA replication errors to unwind the
CC mismatch containing DNA strand (PubMed:22771120, PubMed:26300262). In
CC addition, recruits MLH1, a component of the MMR complex, to chromatin
CC (By similarity). The MCM8-MCM9 complex is dispensable for DNA
CC replication and S phase progression (PubMed:21987787). Probably by
CC regulating HR, plays a key role during gametogenesis (PubMed:21987787,
CC PubMed:22771120). {ECO:0000250|UniProtKB:Q9NXL9,
CC ECO:0000269|PubMed:21987787, ECO:0000269|PubMed:22771120,
CC ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9NXL9};
CC -!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
CC composed of MCM8 and MCM9 (PubMed:22771120). Interacts with the DNA
CC mismatch repair (MMR) complex composed at least of MSH2, MSH3, MSH6,
CC PMS1 and MLH1 (By similarity). Interacts with MLH1; the interaction
CC recruits MLH1 to chromatin (By similarity). Interacts with MSH2; the
CC interaction recruits MCM9 to chromatin (By similarity). Interacts with
CC MSH6 (By similarity). Interacts with the MRN complex composed of MRE11,
CC RAD50 and NBN/NBS1; the interaction recruits the MRN complex to DNA
CC damage sites (By similarity). Interacts with RAD51; the interaction
CC recruits RAD51 to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:Q9NXL9, ECO:0000269|PubMed:22771120}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23401855}. Chromosome
CC {ECO:0000269|PubMed:23401855}. Note=Colocalizes to nuclear foci with
CC RPA1 following DNA damage (PubMed:23401855). Localizes to double-
CC stranded DNA breaks (By similarity). Recruited to chromatin by MSH2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NXL9,
CC ECO:0000269|PubMed:23401855}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Mcm9(L) {ECO:0000303|PubMed:21987787};
CC IsoId=Q2KHI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KHI9-2; Sequence=VSP_028015;
CC Name=3; Synonyms=Mcm9(S) {ECO:0000303|PubMed:21987787};
CC IsoId=Q2KHI9-3; Sequence=VSP_028016, VSP_028017;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:21987787}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults.
CC {ECO:0000269|PubMed:21987787}.
CC -!- INDUCTION: By E2F1 and serum stimulation.
CC {ECO:0000269|PubMed:22771120}.
CC -!- DISRUPTION PHENOTYPE: Females are viable but are sterile due to defects
CC in double-strand break repair during gametogenesis. Males are not
CC sterile and produce spermatozoa, but in much reduced quantity. Female
CC ovaries are completely devoid of oocytes, and testes show a severe
CC early proliferation defect of germ cells, causing a retarded
CC development of only a fraction of seminiferous tubules that produce
CC then apparently normal spermatozoa. {ECO:0000269|PubMed:21987787,
CC ECO:0000269|PubMed:22771120}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AC153949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062185; AAH62185.2; -; mRNA.
DR EMBL; AK018494; BAB31238.1; -; mRNA.
DR EMBL; AK046636; BAE20656.1; -; mRNA.
DR EMBL; BN000883; CAJ70649.1; -; mRNA.
DR CCDS; CCDS23846.2; -. [Q2KHI9-1]
DR RefSeq; NP_082106.2; NM_027830.2. [Q2KHI9-1]
DR RefSeq; XP_017169586.1; XM_017314097.1.
DR AlphaFoldDB; Q2KHI9; -.
DR SMR; Q2KHI9; -.
DR STRING; 10090.ENSMUSP00000074978; -.
DR iPTMnet; Q2KHI9; -.
DR PhosphoSitePlus; Q2KHI9; -.
DR EPD; Q2KHI9; -.
DR jPOST; Q2KHI9; -.
DR MaxQB; Q2KHI9; -.
DR PaxDb; Q2KHI9; -.
DR PeptideAtlas; Q2KHI9; -.
DR PRIDE; Q2KHI9; -.
DR ProteomicsDB; 292277; -. [Q2KHI9-1]
DR ProteomicsDB; 292278; -. [Q2KHI9-2]
DR ProteomicsDB; 292279; -. [Q2KHI9-3]
DR Antibodypedia; 34788; 94 antibodies from 24 providers.
DR Ensembl; ENSMUST00000075540; ENSMUSP00000074978; ENSMUSG00000058298. [Q2KHI9-2]
DR Ensembl; ENSMUST00000219838; ENSMUSP00000151639; ENSMUSG00000058298. [Q2KHI9-3]
DR Ensembl; ENSMUST00000237608; ENSMUSP00000157761; ENSMUSG00000058298. [Q2KHI9-1]
DR GeneID; 71567; -.
DR KEGG; mmu:71567; -.
DR UCSC; uc007fbq.1; mouse. [Q2KHI9-2]
DR UCSC; uc007fbs.1; mouse. [Q2KHI9-3]
DR CTD; 254394; -.
DR MGI; MGI:1918817; Mcm9.
DR VEuPathDB; HostDB:ENSMUSG00000058298; -.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01050000244972; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q2KHI9; -.
DR OMA; XHARLMF; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q2KHI9; -.
DR TreeFam; TF329421; -.
DR BioGRID-ORCS; 71567; 24 hits in 109 CRISPR screens.
DR ChiTaRS; Mcm9; mouse.
DR PRO; PR:Q2KHI9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q2KHI9; protein.
DR Bgee; ENSMUSG00000058298; Expressed in animal zygote and 161 other tissues.
DR ExpressionAtlas; Q2KHI9; baseline and differential.
DR Genevisible; Q2KHI9; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0032406; F:MutLbeta complex binding; ISO:MGI.
DR GO; GO:0032407; F:MutSalpha complex binding; ISO:MGI.
DR GO; GO:0032408; F:MutSbeta complex binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; ISO:MGI.
DR GO; GO:0036298; P:recombinational interstrand cross-link repair; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1134
FT /note="DNA helicase MCM9"
FT /id="PRO_0000304144"
FT DOMAIN 300..505
FT /note="MCM"
FT REGION 659..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXL9"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXL9"
FT VAR_SEQ 1
FT /note="M -> MDQRTTRNGKYCDVEPVSRSNPAPCLRDPPLRRLVRPKPRLQLPESR
FT LSPCSRLPLADSSVRPGARPPASAPGRSPSGRKVEAVRGSGSAGSSSPSEAEREQREEA
FT CAPPRKAAPSSGRAHAPPPPTPRGSGWGDHGRSAVPATKTVRVEPYPPFKM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_028015"
FT VAR_SEQ 385..386
FT /note="LT -> TV (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_028016"
FT VAR_SEQ 387..1134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_028017"
FT CONFLICT 137
FT /note="K -> R (in Ref. 3; BAB31238)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="S -> T (in Ref. 2; AAH62185)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="S -> P (in Ref. 2; AAH62185)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063..1065
FT /note="Missing (in Ref. 2; AAH62185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1134 AA; 125814 MW; 92E748317EB14832 CRC64;
MNSEQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMSLFET NMEIGDYFTV
FPNEVLTVFD SALRRSALAI LQSLPETEGL SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KHVFMVEADF EQYYTFSRPS SCPSLASCDS
SKFSCLSDLS SSPARCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGVVMQRWKP FQRDVRCEVE IVLKANYVQV NNEQSSGMVM DEDTRKEFED FWEHYKSDPF
AGRNEILASL CPQVFGMYLV KLAVAMVLAG GIQRTDAAGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPKESVS VNIALGSPLL
SRFDLVLVLL DTRNEDWDRI ISSFILENKG YPSKSENLWS MEKMKTYFCL IRNLHPTLSE
VSNQVLLRYY QMQRQSDSRN AARTTIRLLE SLIRLAEAHA RLMFRSAVTL EDAVTAVSVM
ESSMQGGALL GGVNALHTSF PENPRAQYQR QCELILEKLE LQGLLQEELR RLERLQNESV
HQCQSHSLEE EVAPGSCRND PRDKPRLRTS TQQEQSCSWS STERSGADSP PGPGLNRPTS
CNNSAENRDG RGDGLDWLDP TSSPEIAPES TIVSPNVKTT EKNVNLKISN NKSQGKEKHG
PQQRSKLLEA GHLPSSGAMN APLRSHGVKR TKASQAVVVS EAGRGDEEDS VPRRLPKLLK
EGSQNVCRST TRVRPLPPTV PLSLSIPSPG SGKRSGTPKR KRRKSAQVEE PEPEGMETPT
VKLAKFTFKQ KTKLTHSPEG QGPIPPSASE IAVDSSKIPQ QRTRREAAVP VVAPGKSTST
SGDRCSDQLH GKTKELSRQP PDSNPPREER EQGPKRRVIQ PKPELGNQAG HSHLACEKDR
KEGVSCGNKS SKVHAGTIAR LASFSFTSPS ESKSESLPPE RKDSRDSRDS RDSRDRCHSP
PATTAPVLGQ QRQTFQLQQP TERANLSTLS LFTLSELDDE ALDFDWEEEM RKKP
