MMS22_HUMAN
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 03-AUG-2022, entry version 133.
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}.
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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; 62.
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; Q6ZRQ5; -.
DR PeptideAtlas; Q6ZRQ5; -.
DR PRIDE; Q6ZRQ5; -.
DR ProteomicsDB; 68153; -.
DR Antibodypedia; 55212; 12 antibodies from 7 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 CTD; 253714; -.
DR DisGeNET; 253714; -.
DR GeneCards; MMS22L; -.
DR HGNC; HGNC:21475; MMS22L.
DR HPA; ENSG00000146263; Low tissue specificity.
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; GFLPSNC; -.
DR OrthoDB; 523276at2759; -.
DR PhylomeDB; Q6ZRQ5; -.
DR TreeFam; TF353832; -.
DR PathwayCommons; Q6ZRQ5; -.
DR SignaLink; Q6ZRQ5; -.
DR BioGRID-ORCS; 253714; 731 hits in 1083 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 ventricular zone and 108 other 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:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
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; PTHR28547; 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
