ID MMS22_HUMAN Reviewed; 1243 AA. AC Q6ZRQ5; D6R9Y8; D6RBQ4; E1P529; Q5THT2; Q68CQ6; Q68D32; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 3. DT 24-JAN-2024, entry version 141. DE RecName: Full=Protein MMS22-like {ECO:0000305}; DE AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like {ECO:0000303|PubMed:21055983, ECO:0000303|PubMed:21113133}; GN Name=MMS22L {ECO:0000303|PubMed:21055983, ECO:0000303|PubMed:21113133, GN ECO:0000312|HGNC:HGNC:21475}; GN Synonyms=C6orf167 {ECO:0000312|HGNC:HGNC:21475}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-564 AND ALA-875. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-277 AND 1043-1243. RC TISSUE=Fetal kidney, and Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MMS22L-TONSL RP COMPLEX. RX PubMed=21113133; DOI=10.1038/emboj.2010.304; RA Piwko W., Olma M.H., Held M., Bianco J.N., Pedrioli P.G., Hofmann K., RA Pasero P., Gerlich D.W., Peter M.; RT "RNAi-based screening identifies the Mms22L-Nfkbil2 complex as a novel RT regulator of DNA replication in human cells."; RL EMBO J. 29:4210-4222(2010). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MMS22L-TONSL RP COMPLEX. RX PubMed=21055983; DOI=10.1016/j.molcel.2010.10.024; RA O'Donnell L., Panier S., Wildenhain J., Tkach J.M., Al-Hakim A., RA Landry M.C., Escribano-Diaz C., Szilard R.K., Young J.T., Munro M., RA Canny M.D., Kolas N.K., Zhang W., Harding S.M., Ylanko J., Mendez M., RA Mullin M., Sun T., Habermann B., Datti A., Bristow R.G., Gingras A.C., RA Tyers M.D., Brown G.W., Durocher D.; RT "The MMS22L-TONSL complex mediates recovery from replication stress and RT homologous recombination."; RL Mol. Cell 40:619-631(2010). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MMS22L-TONSL RP COMPLEX. RX PubMed=21055984; DOI=10.1016/j.molcel.2010.10.023; RA Duro E., Lundin C., Ask K., Sanchez-Pulido L., MacArtney T.J., Toth R., RA Ponting C.P., Groth A., Helleday T., Rouse J.; RT "Identification of the MMS22L-TONSL complex that promotes homologous RT recombination."; RL Mol. Cell 40:632-644(2010). RN [8] RP FUNCTION, AND IDENTIFICATION IN THE MMS22L-TONSL COMPLEX. RX PubMed=21055985; DOI=10.1016/j.molcel.2010.10.022; RA O'Connell B.C., Adamson B., Lydeard J.R., Sowa M.E., Ciccia A., RA Bredemeyer A.L., Schlabach M., Gygi S.P., Elledge S.J., Harper J.W.; RT "A genome-wide camptothecin sensitivity screen identifies a mammalian RT MMS22L-NFKBIL2 complex required for genomic stability."; RL Mol. Cell 40:645-657(2010). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP FUNCTION. RX PubMed=26527279; DOI=10.1016/j.molcel.2015.08.005; RA Campos E.I., Smits A.H., Kang Y.H., Landry S., Escobar T.M., Nayak S., RA Ueberheide B.M., Durocher D., Vermeulen M., Hurwitz J., Reinberg D.; RT "Analysis of the histone H3.1 interactome: a suitable chaperone for the RT right event."; RL Mol. Cell 60:697-709(2015). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE MMS22L-TONSL, RP INTERACTION WITH RAD51, AND MUTAGENESIS OF 29-PHE--ALA-32; RP 595-PHE--ALA-598; 1034-PHE--ALA-1037 AND PHE-1034. RX PubMed=27797818; DOI=10.15252/embj.201593132; RA Piwko W., Mlejnkova L.J., Mutreja K., Ranjha L., Stafa D., Smirnov A., RA Brodersen M.M., Zellweger R., Sturzenegger A., Janscak P., Lopes M., RA Peter M., Cejka P.; RT "The MMS22L-TONSL heterodimer directly promotes RAD51-dependent RT recombination upon replication stress."; RL EMBO J. 35:2584-2601(2016). RN [12] RP FUNCTION, AND IDENTIFICATION IN THE MMS22L-TONSL. RX PubMed=27338793; DOI=10.1038/nature18312; RA Saredi G., Huang H., Hammond C.M., Alabert C., Bekker-Jensen S., Forne I., RA Reveron-Gomez N., Foster B.M., Mlejnkova L., Bartke T., Cejka P., RA Mailand N., Imhof A., Patel D.J., Groth A.; RT "H4K20me0 marks post-replicative chromatin and recruits the TONSL-MMS22L RT DNA repair complex."; RL Nature 534:714-718(2016). RN [13] RP FUNCTION. RX PubMed=29478807; DOI=10.1016/j.molcel.2018.01.031; RA Huang T.H., Fowler F., Chen C.C., Shen Z.J., Sleckman B., Tyler J.K.; RT "The histone chaperones ASF1 and CAF-1 promote MMS22L-TONSL-mediated Rad51 RT loading onto ssDNA during homologous recombination in human cells."; RL Mol. Cell 69:879-892(2018). CC -!- FUNCTION: Component of the MMS22L-TONSL complex, a complex that CC promotes homologous recombination-mediated repair of double-strand CC breaks (DSBs) at stalled or collapsed replication forks CC (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:21113133, CC PubMed:26527279, PubMed:27338793, PubMed:29478807). The MMS22L-TONSL CC complex is required to maintain genome integrity during DNA replication CC (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:27797818). CC It mediates the assembly of RAD51 filaments on single-stranded DNA CC (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following CC histone replacement by histone chaperones and eviction of the CC replication protein A complex (RPA/RP-A) from DSBs (PubMed:21055983, CC PubMed:21055984, PubMed:21055985, PubMed:29478807). Following CC recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of CC RAD51 filaments and subsequent homologous recombination CC (PubMed:27797818, PubMed:29478807). Within the complex, MMS22L acts by CC binding ssDNA (PubMed:27797818). {ECO:0000269|PubMed:21055983, CC ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21055985, CC ECO:0000269|PubMed:21113133, ECO:0000269|PubMed:26527279, CC ECO:0000269|PubMed:27338793, ECO:0000269|PubMed:27797818, CC ECO:0000269|PubMed:29478807}. CC -!- SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least CC composed of MMS22L and TONSL/NFKBIL2 (PubMed:21055983, PubMed:21055984, CC PubMed:21055985, PubMed:21113133, PubMed:27797818). Interacts with CC RAD51; interaction is direct (PubMed:27797818). CC {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, CC ECO:0000269|PubMed:21055985, ECO:0000269|PubMed:21113133, CC ECO:0000269|PubMed:27797818}. CC -!- INTERACTION: CC Q6ZRQ5; Q96HA7: TONSL; NbExp=5; IntAct=EBI-718662, EBI-1052467; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21055983, CC ECO:0000269|PubMed:21055984, ECO:0000269|PubMed:21113133}. Chromosome CC {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, CC ECO:0000269|PubMed:21113133, ECO:0000269|PubMed:27338793, CC ECO:0000269|PubMed:27797818}. Note=Localizes to DNA damage sites, CC accumulates at stressed replication forks (PubMed:21055983, CC PubMed:21055984, PubMed:27797818). Recruited to stalled or collapsed CC replication forks; directly binds replication protein A complex CC (RPA/RP-A)-coated single-stranded DNA (ssDNA) (PubMed:27797818). CC {ECO:0000269|PubMed:21055983, ECO:0000269|PubMed:21055984, CC ECO:0000269|PubMed:27797818}. CC -!- PTM: Degraded by the ubiquitin-proteasome system upon replication CC stress. {ECO:0000269|PubMed:21113133}. CC -!- SIMILARITY: Belongs to the MMS22 family. MMS22L 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; AK128060; BAC87254.1; -; mRNA. DR EMBL; AL023656; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353679; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590484; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48494.1; -; Genomic_DNA. DR EMBL; CH471051; EAW48496.1; -; Genomic_DNA. DR EMBL; CR749603; CAH18398.1; -; mRNA. DR EMBL; CR749822; CAH18682.1; -; mRNA. DR CCDS; CCDS5039.1; -. DR RefSeq; NP_940870.2; NM_198468.2. DR RefSeq; XP_006715493.1; XM_006715430.1. DR AlphaFoldDB; Q6ZRQ5; -. DR BioGRID; 128982; 66. DR IntAct; Q6ZRQ5; 16. DR MINT; Q6ZRQ5; -. DR STRING; 9606.ENSP00000275053; -. DR iPTMnet; Q6ZRQ5; -. DR PhosphoSitePlus; Q6ZRQ5; -. DR BioMuta; MMS22L; -. DR DMDM; 281185507; -. DR EPD; Q6ZRQ5; -. DR jPOST; Q6ZRQ5; -. DR MassIVE; Q6ZRQ5; -. DR MaxQB; Q6ZRQ5; -. DR PaxDb; 9606-ENSP00000275053; -. DR PeptideAtlas; Q6ZRQ5; -. DR ProteomicsDB; 68153; -. DR Pumba; Q6ZRQ5; -. DR Antibodypedia; 55212; 24 antibodies from 8 providers. DR DNASU; 253714; -. DR Ensembl; ENST00000275053.8; ENSP00000275053.4; ENSG00000146263.12. DR Ensembl; ENST00000683635.1; ENSP00000508046.1; ENSG00000146263.12. DR GeneID; 253714; -. DR KEGG; hsa:253714; -. DR MANE-Select; ENST00000683635.1; ENSP00000508046.1; NM_001350599.2; NP_001337528.1. DR UCSC; uc003ppb.3; human. DR AGR; HGNC:21475; -. DR CTD; 253714; -. DR DisGeNET; 253714; -. DR GeneCards; MMS22L; -. DR HGNC; HGNC:21475; MMS22L. DR HPA; ENSG00000146263; Tissue enhanced (bone). DR MIM; 615614; gene. DR neXtProt; NX_Q6ZRQ5; -. DR OpenTargets; ENSG00000146263; -. DR PharmGKB; PA134878007; -. DR VEuPathDB; HostDB:ENSG00000146263; -. DR eggNOG; ENOG502QQCR; Eukaryota. DR GeneTree; ENSGT00390000011769; -. DR HOGENOM; CLU_007143_0_0_1; -. DR InParanoid; Q6ZRQ5; -. DR OMA; RVYLCLL; -. DR OrthoDB; 3109168at2759; -. DR PhylomeDB; Q6ZRQ5; -. DR TreeFam; TF353832; -. DR PathwayCommons; Q6ZRQ5; -. DR SignaLink; Q6ZRQ5; -. DR BioGRID-ORCS; 253714; 761 hits in 1159 CRISPR screens. DR ChiTaRS; MMS22L; human. DR GeneWiki; MMS22L; -. DR GenomeRNAi; 253714; -. DR Pharos; Q6ZRQ5; Tbio. DR PRO; PR:Q6ZRQ5; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q6ZRQ5; Protein. DR Bgee; ENSG00000146263; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 109 other cell types or tissues. DR ExpressionAtlas; Q6ZRQ5; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProt. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0071168; P:protein localization to chromatin; IDA:UniProt. DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB. DR InterPro; IPR042320; MMS22-like. DR InterPro; IPR029424; MMS22L_C. DR InterPro; IPR029425; MMS22L_N. DR PANTHER; PTHR28547; PROTEIN MMS22-LIKE; 1. DR PANTHER; PTHR28547:SF1; PROTEIN MMS22-LIKE; 1. DR Pfam; PF14911; MMS22L_C; 1. DR Pfam; PF14910; MMS22L_N; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Chromosome; DNA damage; DNA repair; DNA-binding; KW Nucleus; Reference proteome. FT CHAIN 1..1243 FT /note="Protein MMS22-like" FT /id="PRO_0000260216" FT VARIANT 419 FT /note="N -> D (in dbSNP:rs9374435)" FT /id="VAR_029013" FT VARIANT 564 FT /note="T -> M (in dbSNP:rs9481410)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_029014" FT VARIANT 875 FT /note="V -> A (in dbSNP:rs1737145)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_029015" FT VARIANT 1015 FT /note="P -> L (in dbSNP:rs10484830)" FT /id="VAR_029016" FT MUTAGEN 29..32 FT /note="FSCA->ASCD: Does not affect interaction with RAD51." FT /evidence="ECO:0000269|PubMed:27797818" FT MUTAGEN 595..598 FT /note="FSCA->ASCD: Does not affect interaction with RAD51." FT /evidence="ECO:0000269|PubMed:27797818" FT MUTAGEN 1034..1037 FT /note="FLPA->ALPD: Abolished interaction with RAD51." FT /evidence="ECO:0000269|PubMed:27797818" FT MUTAGEN 1034 FT /note="F->A: Abolished interaction with RAD51." FT /evidence="ECO:0000269|PubMed:27797818" FT CONFLICT 292 FT /note="C -> R (in Ref. 1; BAC87254)" FT /evidence="ECO:0000305" SQ SEQUENCE 1243 AA; 142321 MW; B63CE3030701CD71 CRC64; MENCSAASTF LTDSLELELG TEWCKPPYFS CAVDNRGGGK HFSGESYLCS GALKRLILNL DPLPTNFEED TLEIFGIQWV TETALVNSSR ELFHLFRQQL YNLETLLQSS CDFGKVSTLH CKADNIRQQC VLFLHYVKVF IFRYLKVQNA ESHVPVHPYE ALEAQLPSVL IDELHGLLLY IGHLSELPSV NIGAFVNQNQ IKLFPPSWHL LHLHLDIHWL VLEILYMLGE KLKQVVYGHQ FMNLASDNLT NISLFEEHCE TLLCDLISLS LNRYDKVRSS ESLMSDQCPC LCIKELWVLL IHLLDHRSKW FVSESFWNWL NKLLKTLLEK SSDRRRSSMP VIQSRDPLGF SWWIITHVAS FYKFDRHGVP DEMRKVESNW NFVEELLKKS ISVQGVILEE QLRMYLHCCL TLCDFWEPNI AIVTILWEYY SKNLNSSFSI SWLPFKGLAN TMKSPLSMLE MVKTCCCDKQ DQELYKSSSS YTIFLCILAK VVKKAMKSNG PHPWKQVKGR IYSKFHQKRM EELTEVGLQN FFSLFLLLAA VAEVEDVASH VLDLLNFLKP AFVTSQRALI WKGHMAFLLM YAQKNLDIGV LAEKFSCAFR EKAKEFLVSK NEEMVQRQTI WTLLSIYIDG VQEVFETSYC LYPSHEKLLN DGFSMLLRAC RESELRTVLS FLQAVLARIR SMHQQLCQEL QRDNVDLFVQ SSLSAKERHL AAVASALWRH FFSFLKSQRM SQVVPFSQLA DAAADFTLLA MDMPSTAPSD FQPQPVISII QLFGWDDIIC PQVVARYLSH VLQNSTLCEA LSHSGYVSFQ ALTVRSWIRC VLQMYIKNLS GPDDLLIDKN LEEAVEKEYM KQLVKLTRLL FNLSEVKSIF SKAQVEYLSI SEDPKKALVR FFEAVGVTYG NVQTLSDKSA MVTKSLEYLG EVLKYIKPYL GKKVFSAGLQ LTYGMMGILV KSWAQIFATS KAQKLLFRII DCLLLPHAVL QQEKELPAPM LSAIQKSLPL YLQGMCIVCC QSQNPNAYLN QLLGNVIEQY IGRFLPASPY VSDLGQHPVL LALRNTATIP PISSLKKCIV QVIRKSYLEY KGSSPPPRLA SILAFILQLF KETNTDIYEV ELLLPGILKC LVLVSEPQVK RLATENLQYM VKACQVGSEE EPSSQLTSVF RQFIQDYGMR YYYQVYSILE TVATLDQQVV IHLISTLTQS LKDSEQKWGL GRNIAQREAY SKLLSHLGQM GQDEMQRLEN DNT //