CARME_HUMAN
ID CARME_HUMAN Reviewed; 409 AA.
AC Q8N4J0; Q7Z383; Q8N7C5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Carnosine N-methyltransferase {ECO:0000303|PubMed:26001783, ECO:0000312|HGNC:HGNC:23435};
DE EC=2.1.1.22 {ECO:0000269|PubMed:26001783};
GN Name=CARNMT1 {ECO:0000312|HGNC:HGNC:23435};
GN Synonyms=C9orf41 {ECO:0000312|HGNC:HGNC:23435};
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 99-409.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-409.
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26001783; DOI=10.1074/jbc.m115.640037;
RA Drozak J., Piecuch M., Poleszak O., Kozlowski P., Chrobok L., Baelde H.J.,
RA de Heer E.;
RT "UPF0586 protein C9orf41 homolog is anserine-producing methyltransferase.";
RL J. Biol. Chem. 290:17190-17205(2015).
RN [7] {ECO:0007744|PDB:5YF0, ECO:0007744|PDB:5YF1, ECO:0007744|PDB:5YF2}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 53-409 IN COMPLEXES WITH
RP CARNOSINE AND S-ADENOSYL-L-METHIONINE, DOMAIN, SUBUNIT, TOPOLOGY, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF PHE-313; ASP-316; PRO-343; LEU-345; HIS-347;
RP TYR-386; TYR-396 AND TYR-398.
RX PubMed=29463897; DOI=10.1038/s41422-018-0003-0;
RA Cao R., Zhang X., Liu X., Li Y., Li H.;
RT "Molecular basis for histidine N1 position-specific methylation by
RT CARNMT1.";
RL Cell Res. 28:494-496(2018).
CC -!- FUNCTION: N-methyltransferase that catalyzes the formation of anserine
CC (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a
CC methylated derivative of carnosine (beta-alanyl-L-histidine), is an
CC abundant constituent of vertebrate skeletal muscles. Also methylates
CC other L-histidine-containing di- and tripeptides such as Gly-Gly-His,
CC Gly-His and homocarnosine (GABA-His). {ECO:0000269|PubMed:26001783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:14205, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57485, ChEBI:CHEBI:57856, ChEBI:CHEBI:58445,
CC ChEBI:CHEBI:59789; EC=2.1.1.22;
CC Evidence={ECO:0000269|PubMed:26001783, ECO:0000269|PubMed:29463897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14206;
CC Evidence={ECO:0000305|PubMed:29463897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.959 mM for carnosine {ECO:0000269|PubMed:26001783};
CC KM=0.053 mM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:26001783};
CC Vmax=1.77 nmol/min/mg enzyme with carnosine as substrate
CC {ECO:0000269|PubMed:26001783};
CC Note=kcat is 0.09 min(-1) for carnosine. kcat is 3.57 min(-1) for S-
CC adenosyl-L-methionine. {ECO:0000269|PubMed:26001783};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:26001783};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:26001783};
CC -!- SUBUNIT: Homodimer. Each monomer accommodates one molecule of carnosine
CC in its active pocket (residues 313-398), precisely anchoring the
CC histidine imidazole ring such that only N1 is exposed and deprotonated
CC for methylation. {ECO:0000269|PubMed:29463897}.
CC -!- INTERACTION:
CC Q8N4J0; Q01081: U2AF1; NbExp=6; IntAct=EBI-11963218, EBI-632461;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26001783}.
CC Nucleus {ECO:0000269|PubMed:26001783}.
CC -!- TISSUE SPECIFICITY: Expressed at higher level in kidney. Expressed at
CC lower level in brain and skeletal muscle.
CC {ECO:0000269|PubMed:26001783}.
CC -!- DOMAIN: The Gly-Xaa-Gly-Xaa-Gly (GXGXG) motif binds the adenosyl part
CC of S-adenosyl-L-methionine. {ECO:0000305|PubMed:29463897}.
CC -!- DOMAIN: The carnosine-binding region forms hydrophobic and hydrogen
CC bonds with carnosine, defining a flipping orientation of the imidazole
CC ring so that N1 is present next to S-adenosyl-L-methionine for
CC methylation. {ECO:0000305|PubMed:29463897}.
CC -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05369.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL158825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034033; AAH34033.1; -; mRNA.
DR EMBL; BX538061; CAD97992.1; -; mRNA.
DR EMBL; AK098661; BAC05369.1; ALT_INIT; mRNA.
DR CCDS; CCDS6649.1; -.
DR RefSeq; NP_001307426.1; NM_001320497.1.
DR RefSeq; NP_689633.1; NM_152420.2.
DR PDB; 5YF0; X-ray; 2.25 A; A/B=53-409.
DR PDB; 5YF1; X-ray; 2.40 A; A/B=53-409.
DR PDB; 5YF2; X-ray; 2.80 A; A/B=53-409.
DR PDBsum; 5YF0; -.
DR PDBsum; 5YF1; -.
DR PDBsum; 5YF2; -.
DR AlphaFoldDB; Q8N4J0; -.
DR SMR; Q8N4J0; -.
DR BioGRID; 126504; 53.
DR IntAct; Q8N4J0; 38.
DR STRING; 9606.ENSP00000366030; -.
DR GlyGen; Q8N4J0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N4J0; -.
DR PhosphoSitePlus; Q8N4J0; -.
DR BioMuta; CARNMT1; -.
DR DMDM; 68565210; -.
DR EPD; Q8N4J0; -.
DR jPOST; Q8N4J0; -.
DR MassIVE; Q8N4J0; -.
DR MaxQB; Q8N4J0; -.
DR PaxDb; Q8N4J0; -.
DR PeptideAtlas; Q8N4J0; -.
DR PRIDE; Q8N4J0; -.
DR ProteomicsDB; 71936; -.
DR Antibodypedia; 12742; 172 antibodies from 20 providers.
DR DNASU; 138199; -.
DR Ensembl; ENST00000376834.8; ENSP00000366030.3; ENSG00000156017.13.
DR GeneID; 138199; -.
DR KEGG; hsa:138199; -.
DR MANE-Select; ENST00000376834.8; ENSP00000366030.3; NM_152420.3; NP_689633.1.
DR UCSC; uc004ajq.4; human.
DR CTD; 138199; -.
DR GeneCards; CARNMT1; -.
DR HGNC; HGNC:23435; CARNMT1.
DR HPA; ENSG00000156017; Low tissue specificity.
DR MIM; 616552; gene.
DR neXtProt; NX_Q8N4J0; -.
DR OpenTargets; ENSG00000156017; -.
DR PharmGKB; PA134929393; -.
DR VEuPathDB; HostDB:ENSG00000156017; -.
DR eggNOG; KOG2798; Eukaryota.
DR GeneTree; ENSGT00390000005323; -.
DR HOGENOM; CLU_030612_0_0_1; -.
DR InParanoid; Q8N4J0; -.
DR OMA; PNGLWIN; -.
DR OrthoDB; 1437030at2759; -.
DR PhylomeDB; Q8N4J0; -.
DR TreeFam; TF313564; -.
DR BRENDA; 2.1.1.22; 2681.
DR PathwayCommons; Q8N4J0; -.
DR Reactome; R-HSA-70921; Histidine catabolism.
DR SABIO-RK; Q8N4J0; -.
DR SignaLink; Q8N4J0; -.
DR BioGRID-ORCS; 138199; 48 hits in 1063 CRISPR screens.
DR ChiTaRS; CARNMT1; human.
DR GenomeRNAi; 138199; -.
DR Pharos; Q8N4J0; Tbio.
DR PRO; PR:Q8N4J0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N4J0; protein.
DR Bgee; ENSG00000156017; Expressed in epithelial cell of pancreas and 178 other tissues.
DR ExpressionAtlas; Q8N4J0; baseline and differential.
DR Genevisible; Q8N4J0; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030735; F:carnosine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035498; P:carnosine metabolic process; IDA:UniProtKB.
DR GO; GO:0006548; P:histidine catabolic process; TAS:Reactome.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR012901; CARME.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12303; PTHR12303; 1.
DR Pfam; PF07942; N2227; 1.
DR SMART; SM01296; N2227; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..409
FT /note="Carnosine N-methyltransferase"
FT /id="PRO_0000089685"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 312
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 316
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF1"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF0"
FT BINDING 347
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF1"
FT BINDING 398
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000269|PubMed:29463897,
FT ECO:0007744|PDB:5YF1"
FT MUTAGEN 313
FT /note="F->A: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 316
FT /note="D->A,E,N: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 343
FT /note="P->A: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 345
FT /note="L->A: Significantly reduces N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 347
FT /note="H->A,F: Impairs binding to S-adenosyl-L-methionine.
FT Significantly reduces N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 386
FT /note="Y->A: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 386
FT /note="Y->F,W: Reduces N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 396
FT /note="Y->A: Reduces N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 396
FT /note="Y->D: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT MUTAGEN 398
FT /note="Y->A,F: Impairs N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29463897"
FT CONFLICT 333
FT /note="K -> R (in Ref. 3; CAD97992)"
FT /evidence="ECO:0000305"
FT HELIX 61..93
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 105..128
FT /evidence="ECO:0007829|PDB:5YF0"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5YF1"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 174..191
FT /evidence="ECO:0007829|PDB:5YF0"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5YF0"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:5YF0"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:5YF0"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:5YF0"
FT STRAND 392..406
FT /evidence="ECO:0007829|PDB:5YF0"
SQ SEQUENCE 409 AA; 47186 MW; 458584B41E1794EF CRC64;
MQRRRRPPPP TSRLPEGCGG GGGGSEEVEV QFSAGRWGSA AAVSAAAAAA TRSTEEEEER
LEREHFWKII NAFRYYGTSM HERVNRTERQ FRSLPANQQK LLPQFLLHLD KIRKCIDHNQ
EILLTIVNDC IHMFENKEYG EDGNGKIMPA STFDMDKLKS TLKQFVRDWS ETGKAERDAC
YQPIIKEILK NFPKERWDPS KVNILVPGAG LGRLAWEIAM LGYACQGNEW SFFMLFSSNF
VLNRCSEINK YKLYPWIHQF SNNRRSADQI RPIFFPDVDP HSLPPGSNFS MTAGDFQEIY
SECNTWDCIA TCFFIDTAHN VIDYIDTIWK ILKPGGIWIN LGPLLYHFEN LANELSIELS
YEDIKNVVLQ YGFKVEVEKE SVLSTYTVND LSMMKYYYEC VLFVVRKPQ
