ARMT1_HUMAN
ID ARMT1_HUMAN Reviewed; 441 AA.
AC Q9H993; Q96FC6; Q9UFY5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Damage-control phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q04371};
DE AltName: Full=Acidic residue methyltransferase 1 {ECO:0000303|PubMed:25732820};
DE AltName: Full=Protein-glutamate O-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:25732820};
DE AltName: Full=Sugar phosphate phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
GN Name=ARMT1 {ECO:0000303|PubMed:25732820, ECO:0000312|HGNC:HGNC:17872};
GN Synonyms=C6orf211 {ECO:0000312|HGNC:HGNC:17872};
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].
RC TISSUE=Teratocarcinoma;
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 MRNA], AND VARIANT ARG-77.
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238.
RC TISSUE=Fetal kidney;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND METHYLATION.
RX PubMed=25732820; DOI=10.1016/j.celrep.2015.01.054;
RA Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H.,
RA Hoelz D.J.;
RT "Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that
RT targets PCNA and is linked to the DNA damage response.";
RL Cell Rep. 10:1288-1296(2015).
RN [11]
RP CAUTION.
RX PubMed=27322068; DOI=10.1038/nchembio.2108;
RA Huang L., Khusnutdinova A., Nocek B., Brown G., Xu X., Cui H., Petit P.,
RA Flick R., Zallot R., Balmant K., Ziemak M.J., Shanklin J.,
RA de Crecy-Lagard V., Fiehn O., Gregory J.F. III, Joachimiak A.,
RA Savchenko A., Yakunin A.F., Hanson A.D.;
RT "A family of metal-dependent phosphatases implicated in metabolite damage-
RT control.";
RL Nat. Chem. Biol. 12:621-627(2016).
CC -!- FUNCTION: Metal-dependent phosphatase that shows phosphatase activity
CC against several substrates, including fructose-1-phosphate and
CC fructose-6-phosphate (By similarity). Its preference for fructose-1-
CC phosphate, a strong glycating agent that causes DNA damage rather than
CC a canonical yeast metabolite, suggests a damage-control function in
CC hexose phosphate metabolism (By similarity). Has also been shown to
CC have O-methyltransferase activity that methylates glutamate residues of
CC target proteins to form gamma-glutamyl methyl ester residues
CC (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved
CC in the DNA damage response (PubMed:25732820).
CC {ECO:0000250|UniProtKB:Q04371, ECO:0000269|PubMed:25732820}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate;
CC Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; Evidence={ECO:0000305|PubMed:25732820};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- INTERACTION:
CC Q9H993; Q08209-2: PPP3CA; NbExp=4; IntAct=EBI-1046033, EBI-11959013;
CC -!- DOMAIN: Subfamily III proteins have a conserved RTxK motif about 40-50
CC residues from the C-terminus; the threonine may be replaced by serine
CC or cysteine. {ECO:0000250|UniProtKB:Q04371}.
CC -!- PTM: Automethylated. {ECO:0000305|PubMed:25732820}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family. Sugar
CC phosphate phosphatase III subfamily. {ECO:0000305}.
CC -!- CAUTION: Has been reportedly associated with a protein carboxyl
CC methyltransferase activity, but whether this protein indeed has such an
CC activity remains to be determined (PubMed:25732820). It has been later
CC shown to belong to a family of metal-dependent phosphatases implicated
CC in metabolite damage-control (PubMed:27322068).
CC {ECO:0000269|PubMed:27322068, ECO:0000305|PubMed:25732820}.
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DR EMBL; AK022972; BAB14339.1; -; mRNA.
DR EMBL; AL590543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011348; AAH11348.1; -; mRNA.
DR EMBL; AL110241; CAB53692.2; -; mRNA.
DR CCDS; CCDS5233.1; -.
DR PIR; T14772; T14772.
DR RefSeq; NP_001273491.1; NM_001286562.1.
DR RefSeq; NP_078849.1; NM_024573.2.
DR PDB; 6UMQ; X-ray; 1.85 A; A/B=1-441.
DR PDB; 6UMR; X-ray; 2.21 A; A/B=1-441.
DR PDBsum; 6UMQ; -.
DR PDBsum; 6UMR; -.
DR AlphaFoldDB; Q9H993; -.
DR SMR; Q9H993; -.
DR BioGRID; 122754; 50.
DR IntAct; Q9H993; 16.
DR MINT; Q9H993; -.
DR STRING; 9606.ENSP00000356263; -.
DR GlyGen; Q9H993; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H993; -.
DR PhosphoSitePlus; Q9H993; -.
DR BioMuta; ARMT1; -.
DR DMDM; 74752737; -.
DR EPD; Q9H993; -.
DR jPOST; Q9H993; -.
DR MassIVE; Q9H993; -.
DR MaxQB; Q9H993; -.
DR PaxDb; Q9H993; -.
DR PeptideAtlas; Q9H993; -.
DR PRIDE; Q9H993; -.
DR ProteomicsDB; 81298; -.
DR Antibodypedia; 1089; 160 antibodies from 24 providers.
DR DNASU; 79624; -.
DR Ensembl; ENST00000367294.4; ENSP00000356263.3; ENSG00000146476.11.
DR GeneID; 79624; -.
DR KEGG; hsa:79624; -.
DR MANE-Select; ENST00000367294.4; ENSP00000356263.3; NM_024573.3; NP_078849.1.
DR UCSC; uc003qok.3; human.
DR CTD; 79624; -.
DR DisGeNET; 79624; -.
DR GeneCards; ARMT1; -.
DR HGNC; HGNC:17872; ARMT1.
DR HPA; ENSG00000146476; Low tissue specificity.
DR MIM; 616332; gene.
DR neXtProt; NX_Q9H993; -.
DR OpenTargets; ENSG00000146476; -.
DR PharmGKB; PA134870747; -.
DR VEuPathDB; HostDB:ENSG00000146476; -.
DR eggNOG; KOG3870; Eukaryota.
DR GeneTree; ENSGT00530000064023; -.
DR HOGENOM; CLU_030117_0_0_1; -.
DR InParanoid; Q9H993; -.
DR OMA; GFRPTNI; -.
DR OrthoDB; 856818at2759; -.
DR PhylomeDB; Q9H993; -.
DR TreeFam; TF314853; -.
DR PathwayCommons; Q9H993; -.
DR SignaLink; Q9H993; -.
DR BioGRID-ORCS; 79624; 26 hits in 1051 CRISPR screens.
DR ChiTaRS; ARMT1; human.
DR GenomeRNAi; 79624; -.
DR Pharos; Q9H993; Tbio.
DR PRO; PR:Q9H993; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H993; protein.
DR Bgee; ENSG00000146476; Expressed in cartilage tissue and 203 other tissues.
DR ExpressionAtlas; Q9H993; baseline and differential.
DR Genevisible; Q9H993; HS.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0103026; F:fructose-1-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0051998; F:protein carboxyl O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:UniProtKB.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR039763; ARMT1.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR PANTHER; PTHR12260; PTHR12260; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA damage; Hydrolase; Manganese; Metal-binding;
KW Methylation; Methyltransferase; Nickel; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..441
FT /note="Damage-control phosphatase ARMT1"
FT /id="PRO_0000230795"
FT MOTIF 401..404
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:25732820"
FT BINDING 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:25732820"
FT BINDING 367..371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 73
FT /note="K -> N (in dbSNP:rs35036943)"
FT /id="VAR_053090"
FT VARIANT 77
FT /note="P -> R (in dbSNP:rs17850732)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025791"
FT VARIANT 150
FT /note="G -> E (in dbSNP:rs35734927)"
FT /id="VAR_053091"
FT VARIANT 154
FT /note="S -> A (in dbSNP:rs34437617)"
FT /id="VAR_053092"
FT VARIANT 161
FT /note="H -> P (in dbSNP:rs36037706)"
FT /id="VAR_053093"
FT VARIANT 264
FT /note="I -> V (in dbSNP:rs35989216)"
FT /id="VAR_053094"
FT VARIANT 317
FT /note="A -> T (in dbSNP:rs35972078)"
FT /id="VAR_053095"
FT CONFLICT 120..121
FT /note="MY -> ID (in Ref. 3; AAH11348)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="F -> S (in Ref. 4; CAB53692)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="D -> Y (in Ref. 3; AAH11348)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="F -> Y (in Ref. 4; CAB53692)"
FT /evidence="ECO:0000305"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 49..70
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6UMQ"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:6UMQ"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6UMQ"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:6UMQ"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:6UMQ"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:6UMQ"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6UMQ"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:6UMQ"
SQ SEQUENCE 441 AA; 51172 MW; 3BE4D15528FDFC4E CRC64;
MAVVPASLSG QDVGSFAYLT IKDRIPQILT KVIDTLHRHK SEFFEKHGEE GVEAEKKAIS
LLSKLRNELQ TDKPFIPLVE KFVDTDIWNQ YLEYQQSLLN ESDGKSRWFY SPWLLVECYM
YRRIHEAIIQ SPPIDYFDVF KESKEQNFYG SQESIIALCT HLQQLIRTIE DLDENQLKDE
FFKLLQISLW GNKCDLSLSG GESSSQNTNV LNSLEDLKPF ILLNDMEHLW SLLSNCKKTR
EKASATRVYI VLDNSGFELV TDLILADFLL SSELATEVHF YGKTIPWFVS DTTIHDFNWL
IEQVKHSNHK WMSKCGADWE EYIKMGKWVY HNHIFWTLPH EYCAMPQVAP DLYAELQKAH
LILFKGDLNY RKLTGDRKWE FSVPFHQALN GFHPAPLCTI RTLKAEIQVG LQPGQGEQLL
ASEPSWWTTG KYGIFQYDGP L
