ANM1_RAT
ID ANM1_RAT Reviewed; 353 AA.
AC Q63009;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein arginine N-methyltransferase 1;
DE EC=2.1.1.319 {ECO:0000269|PubMed:19405910};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1;
GN Name=Prmt1; Synonyms=Hrmt1l2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BTG1; BTG2 AND IFNAR1.
RX PubMed=8663146; DOI=10.1074/jbc.271.25.15034;
RA Lin W.-J., Gary J.D., Yang M.C., Clarke S., Herschman H.R.;
RT "The mammalian immediate-early TIS21 protein and the leukemia-associated
RT BTG1 protein interact with a protein-arginine N-methyltransferase.";
RL J. Biol. Chem. 271:15034-15044(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15837430; DOI=10.1016/j.bbagen.2005.02.015;
RA Lim Y., Kwon Y.H., Won N.H., Min B.H., Park I.S., Paik W.K., Kim S.;
RT "Multimerization of expressed protein-arginine methyltransferases during
RT the growth and differentiation of rat liver.";
RL Biochim. Biophys. Acta 1723:240-247(2005).
RN [4]
RP FUNCTION.
RX PubMed=18492485; DOI=10.1016/j.bbrc.2008.05.051;
RA Iwasaki H.;
RT "Involvement of PRMT1 in hnRNPQ activation and internalization of insulin
RT receptor.";
RL Biochem. Biophys. Res. Commun. 372:314-319(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19405910; DOI=10.1042/bj20090268;
RA Lakowski T.M., Frankel A.;
RT "Kinetic analysis of human protein arginine N-methyltransferase 2:
RT formation of monomethyl- and asymmetric dimethyl-arginine residues on
RT histone H4.";
RL Biochem. J. 421:253-261(2009).
RN [6]
RP FUNCTION, INTERACTION WITH MAP3K5, AND MUTAGENESIS OF GLY-80.
RX PubMed=22095282; DOI=10.1038/cdd.2011.168;
RA Cho J.H., Lee M.K., Yoon K.W., Lee J., Cho S.G., Choi E.J.;
RT "Arginine methylation-dependent regulation of ASK1 signaling by PRMT1.";
RL Cell Death Differ. 19:859-870(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND PEPTIDE SUBSTRATE, SUBUNIT, FUNCTION, ACTIVE
RP SITE, AND MUTAGENESIS OF GLU-144 AND GLU-153.
RX PubMed=12737817; DOI=10.1016/s0969-2126(03)00071-6;
RA Zhang X., Cheng X.;
RT "Structure of the predominant protein arginine methyltransferase PRMT1 and
RT analysis of its binding to substrate peptides.";
RL Structure 11:509-520(2003).
CC -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1,
CC HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1,
CC CHTOP and MAP3K5/ASK1 (PubMed:12737817, PubMed:15837430,
CC PubMed:18492485, PubMed:22095282, PubMed:19405910). Constitutes the
CC main enzyme that mediates monomethylation and asymmetric dimethylation
CC of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific
CC tag for epigenetic transcriptional activation (By similarity). May be
CC involved in the regulation of TAF15 transcriptional activity, act as an
CC activator of estrogen receptor (ER)-mediated transactivation, play a
CC key role in neurite outgrowth and act as a negative regulator of
CC megakaryocytic differentiation, by modulating p38 MAPK pathway (By
CC similarity). Methylates RBM15, promoting ubiquitination and degradation
CC of RBM15 (By similarity). Methylates FOXO1 and retains it in the
CC nucleus increasing its transcriptional activity (By similarity).
CC Methylates CHTOP and this methylation is critical for its 5-
CC hydroxymethylcytosine (5hmC)-binding activity (By similarity).
CC Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes
CC association of MAP3K5 with thioredoxin and negatively regulates MAP3K5
CC association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-
CC induced activation of JNK (PubMed:22095282). Methylates H4R3 in genes
CC involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent
CC manner (By similarity). Plays a role in regulating alternative splicing
CC in the heart (By similarity). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:12737817,
CC ECO:0000269|PubMed:15837430, ECO:0000269|PubMed:18492485,
CC ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:22095282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000269|PubMed:19405910};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for AdoMet {ECO:0000269|PubMed:19405910};
CC KM=4.2 uM for histone H4 {ECO:0000269|PubMed:19405910};
CC Vmax=1.2 nmol/min/mg enzyme toward AdoMet
CC {ECO:0000269|PubMed:19405910};
CC Vmax=1.24 nmol/min/mg enzyme toward histone H4
CC {ECO:0000269|PubMed:19405910};
CC -!- SUBUNIT: Homodimer and heterodimer with PRMT8. Homooctamer; individual
CC homodimers associates to form a homooctamer. Interacts with NFATC2IP.
CC Interacts with ILF3 and SUPT5H. Individual homodimers can associate to
CC form a homohexamer. Interacts with FOXO1; the interaction methylates
CC FOXO1, retaining it in the nucleus and increasing its transcriptional
CC activity. Methylation of FOXO1 is increased with oxidative stress.
CC Interacts with CHTOP; the interaction methylates CHTOP, enabling its
CC interaction with the 5FMC complex (By similarity). Interacts with BTG1,
CC BTG2 and IFNAR1. Interacts with and probably methylates ATXN2L (By
CC similarity). Component of the methylosome, a 20S complex containing at
CC least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (By
CC similarity). Interacts with DHX9 (via RGG region) (By similarity).
CC Interacts (via N-terminus) with HABP4 (By similarity). Interacts with
CC MAP3K5/ASK1; the interaction results in MAP3K5 methylation by PRMT1
CC which inhibits MAP3K5 activation (PubMed:22095282). Interacts with
CC TRIM48; the interaction results in ubiquitination of PRMT1 by TRIM48,
CC leading to PRMT1 proteasomal degradation and activation of MAP3K5 (By
CC similarity). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000269|PubMed:12737817, ECO:0000269|PubMed:22095282,
CC ECO:0000269|PubMed:8663146}.
CC -!- INTERACTION:
CC Q63009; Q9JIL3: Ilf3; NbExp=2; IntAct=EBI-78708, EBI-78714;
CC Q63009; Q63009: Prmt1; NbExp=2; IntAct=EBI-78708, EBI-78708;
CC Q63009; P62633: CNBP; Xeno; NbExp=2; IntAct=EBI-78708, EBI-1047529;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15837430}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm.
CC Colocalizes with CHTOP within the nucleus. Low levels detected also in
CC the chromatin fraction (By similarity). {ECO:0000250|UniProtKB:Q9JIF0}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Polyubiquitinated at Lys-127 by the SCF(FBXL17) complex, leading
CC to its subsequent degradation (By similarity). Ubiquitination is
CC regulated by acetylation at Lys-210 and Lys-215 (By similarity).
CC Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to
CC suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation
CC (By similarity). {ECO:0000250|UniProtKB:Q99873,
CC ECO:0000250|UniProtKB:Q9JIF0}.
CC -!- PTM: Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the
CC SCF(FBXL17) complex. Acetylated at Lys-215 by p300/EP300. Deacetylated
CC at Lys-210 and Lys-215 by SIRT1. {ECO:0000250|UniProtKB:Q9JIF0}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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; U60882; AAC52622.1; -; mRNA.
DR EMBL; BC078815; AAH78815.1; -; mRNA.
DR RefSeq; NP_077339.1; NM_024363.1.
DR PDB; 1OR8; X-ray; 2.35 A; A=14-353.
DR PDB; 1ORH; X-ray; 2.64 A; A=1-353.
DR PDB; 1ORI; X-ray; 2.50 A; A=11-353.
DR PDB; 3Q7E; X-ray; 2.20 A; A=14-353.
DR PDBsum; 1OR8; -.
DR PDBsum; 1ORH; -.
DR PDBsum; 1ORI; -.
DR PDBsum; 3Q7E; -.
DR AlphaFoldDB; Q63009; -.
DR SMR; Q63009; -.
DR BioGRID; 248825; 3.
DR IntAct; Q63009; 6.
DR MINT; Q63009; -.
DR STRING; 10116.ENSRNOP00000063624; -.
DR BindingDB; Q63009; -.
DR ChEMBL; CHEMBL1275220; -.
DR iPTMnet; Q63009; -.
DR PhosphoSitePlus; Q63009; -.
DR jPOST; Q63009; -.
DR PaxDb; Q63009; -.
DR PRIDE; Q63009; -.
DR GeneID; 60421; -.
DR KEGG; rno:60421; -.
DR UCSC; RGD:62020; rat.
DR CTD; 3276; -.
DR RGD; 62020; Prmt1.
DR VEuPathDB; HostDB:ENSRNOG00000026109; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; Q63009; -.
DR OMA; TTDRMEV; -.
DR OrthoDB; 840669at2759; -.
DR BRENDA; 2.1.1.319; 5301.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; Q63009; -.
DR PRO; PR:Q63009; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000026109; Expressed in ovary and 19 other tissues.
DR Genevisible; Q63009; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016275; F:[cytochrome c]-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042054; F:histone methyltransferase activity; ISO:RGD.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:RGD.
DR GO; GO:0008170; F:N-methyltransferase activity; ISO:RGD.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:RGD.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:MGI.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:MGI.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
DR GO; GO:0030519; F:snoRNP binding; IDA:RGD.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:UniProtKB.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:RGD.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:MGI.
DR GO; GO:0035247; P:peptidyl-arginine omega-N-methylation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IDA:BHF-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:BHF-UCL.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Methyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation.
FT CHAIN 1..353
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000212323"
FT DOMAIN 32..353
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 144
FT /evidence="ECO:0000269|PubMed:12737817"
FT ACT_SITE 153
FT /evidence="ECO:0000269|PubMed:12737817"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12737817"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12737817"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12737817"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12737817"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12737817"
FT MOD_RES 116
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99873"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99873"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MUTAGEN 80
FT /note="G->R: Abolishes catalytic activity. Disrupts
FT interaction of MAP3K5/ASK1 with thioredoxin. Abolishes
FT inhibition of MAP3K5 and activation of JNK1. No effect on
FT interaction with MAP3K5."
FT /evidence="ECO:0000269|PubMed:22095282"
FT MUTAGEN 144
FT /note="E->D: Reduces catalytic activity 10-fold, and causes
FT higher order oligomers of the protein."
FT /evidence="ECO:0000269|PubMed:12737817"
FT MUTAGEN 144
FT /note="E->Q: Reduces catalytic activity 3000-fold, and
FT causes higher order oligomers of the protein."
FT /evidence="ECO:0000269|PubMed:12737817"
FT MUTAGEN 153
FT /note="E->D: Reduces catalytic activity to 0.03%, but does
FT not affect oligomerization."
FT /evidence="ECO:0000269|PubMed:12737817"
FT MUTAGEN 153
FT /note="E->Q: Completely abolishes catalytic activity, but
FT does not affect oligomerization."
FT /evidence="ECO:0000269|PubMed:12737817"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1ORH"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:3Q7E"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3Q7E"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:3Q7E"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:3Q7E"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 259..273
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 296..307
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1ORI"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:3Q7E"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:3Q7E"
SQ SEQUENCE 353 AA; 40522 MW; EDBB0587784C527E CRC64;
MAAAEAANCI MEVSCGQAES SEKPNAEDMT SKDYYFDSYA HFGIHEEMLK DEVRTLTYRN
SMFHNRHLFK DKVVLDVGSG TGILCMFAAK AGARKVIGIE CSSISDYAVK IVKANKLDHV
VTIIKGKVEE VELPVEKVDI IISEWMGYCL FYESMLNTVL HARDKWLAPD GLIFPDRATL
YVTAIEDRQY KDYKIHWWEN VYGFDMSCIK DVAIKEPLVD VVDPKQLVTN ACLIKEVDIY
TVKVEDLTFT SPFCLQVKRN DYVHALVAYF NIEFTRCHKR TGFSTSPESP YTHWKQTVFY
MEDYLTVKTG EEIFGTIGMR PNAKNNRDLD FTIDLDFKGQ LCELSCSTDY RMR
