KAD1_HUMAN
ID KAD1_HUMAN Reviewed; 194 AA.
AC P00568; Q9BVK9; Q9UQC7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN Name=AK1 {ECO:0000255|HAMAP-Rule:MF_03171};
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 PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Skeletal muscle;
RX PubMed=183954; DOI=10.1111/j.1432-1033.1976.tb10787.x;
RA von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H.,
RA Pai E.F.;
RT "Primary and tertiary structure of the principal human adenylate kinase.";
RL Eur. J. Biochem. 68:281-290(1976).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HAAKD TRP-128.
RX PubMed=2542324; DOI=10.1016/s0021-9258(18)81779-3;
RA Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F., Kajii T.,
RA Fujii H., Miwa S., Sakurai M., Nakazawa A.;
RT "Human adenylate kinase deficiency associated with hemolytic anemia. A
RT single base substitution affecting solubility and catalytic activity of the
RT cytosolic adenylate kinase.";
RL J. Biol. Chem. 264:10148-10155(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Noma T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [6]
RP PROTEIN SEQUENCE OF 10-21; 32-44; 64-77; 89-97; 108-128; 156-166 AND
RP 172-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23416111; DOI=10.1016/j.biocel.2013.02.004;
RA Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.;
RT "The human adenylate kinase 9 is a nucleoside mono- and diphosphate
RT kinase.";
RL Int. J. Biochem. Cell Biol. 45:925-931(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP5A.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human AK1A in complex with AP5A.";
RL Submitted (MAR-2007) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP4A.
RG Structural genomics consortium (SGC);
RT "Structure of adenylate kinase 1 in complex with P1, P4-
RT di(adenosine)tetraphosphate.";
RL Submitted (DEC-2005) to the PDB data bank.
RN [13]
RP VARIANT HAAKD CYS-164.
RX PubMed=9432020; DOI=10.1046/j.1365-2141.1997.4953299.x;
RA Qualtieri A., Pedace V., Bisconte M.G., Bria M., Gulino B., Andreoli V.,
RA Brancati C.;
RT "Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G
RT substitution at codon 164 of human AK1 gene associated with chronic
RT haemolytic anaemia.";
RL Br. J. Haematol. 99:770-776(1997).
RN [14]
RP VARIANTS HAAKD ARG-40; ARG-64 AND ASP-140 DEL.
RX PubMed=12649162; DOI=10.1182/blood-2002-07-2288;
RA Corrons J.-L., Garcia E., Tusell J.J., Varughese K.I., West C., Beutler E.;
RT "Red cell adenylate kinase deficiency: molecular study of 3 new mutations
RT (118G>A, 190G>A, and GAC deletion) associated with hereditary
RT nonspherocytic hemolytic anemia.";
RL Blood 102:353-356(2003).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Also displays broad nucleoside diphosphate
CC kinase activity. Plays an important role in cellular energy homeostasis
CC and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_03171,
CC ECO:0000269|PubMed:23416111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171,
CC ECO:0000269|PubMed:23416111};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03171, ECO:0000269|PubMed:23416111};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171,
CC ECO:0000269|PubMed:23416111};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|Ref.11,
CC ECO:0000269|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000305|Ref.11,
CC ECO:0000305|Ref.12}.
CC -!- POLYMORPHISM: This enzyme represents the most common of at least five
CC alleles. {ECO:0000305|PubMed:183954}.
CC -!- DISEASE: Hemolytic anemia due to adenylate kinase deficiency (HAAKD)
CC [MIM:612631]: A disease characterized by hemolytic anemia and
CC undetectable erythrocyte adenylate kinase activity.
CC {ECO:0000269|PubMed:12649162, ECO:0000269|PubMed:2542324,
CC ECO:0000269|PubMed:9432020}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Adenylate kinase entry;
CC URL="https://en.wikipedia.org/wiki/Adenylate_kinase";
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DR EMBL; J04809; AAA51686.1; -; Genomic_DNA.
DR EMBL; AB021871; BAA78534.1; -; mRNA.
DR EMBL; BT019580; AAV38387.1; -; mRNA.
DR EMBL; BC001116; AAH01116.1; -; mRNA.
DR CCDS; CCDS6881.1; -.
DR PIR; A33508; KIHUA.
DR RefSeq; NP_000467.1; NM_000476.2.
DR RefSeq; NP_001305050.1; NM_001318121.1.
DR RefSeq; XP_016869916.1; XM_017014427.1.
DR RefSeq; XP_016869917.1; XM_017014428.1.
DR PDB; 1Z83; X-ray; 1.90 A; A/B/C=1-193.
DR PDB; 2C95; X-ray; 1.71 A; A/B=1-193.
DR PDB; 7DE3; X-ray; 2.20 A; A=1-194.
DR PDBsum; 1Z83; -.
DR PDBsum; 2C95; -.
DR PDBsum; 7DE3; -.
DR AlphaFoldDB; P00568; -.
DR BMRB; P00568; -.
DR SMR; P00568; -.
DR BioGRID; 106706; 49.
DR IntAct; P00568; 24.
DR STRING; 9606.ENSP00000362271; -.
DR ChEMBL; CHEMBL4925; -.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR DrugBank; DB14126; Tenofovir.
DR DrugBank; DB09299; Tenofovir alafenamide.
DR iPTMnet; P00568; -.
DR MetOSite; P00568; -.
DR PhosphoSitePlus; P00568; -.
DR SwissPalm; P00568; -.
DR BioMuta; AK1; -.
DR DMDM; 20178288; -.
DR OGP; P00568; -.
DR REPRODUCTION-2DPAGE; IPI00018342; -.
DR UCD-2DPAGE; P00568; -.
DR EPD; P00568; -.
DR jPOST; P00568; -.
DR MassIVE; P00568; -.
DR PaxDb; P00568; -.
DR PeptideAtlas; P00568; -.
DR PRIDE; P00568; -.
DR ProteomicsDB; 51267; -.
DR TopDownProteomics; P00568; -.
DR Antibodypedia; 1017; 643 antibodies from 36 providers.
DR DNASU; 203; -.
DR Ensembl; ENST00000373156.5; ENSP00000362249.1; ENSG00000106992.19.
DR Ensembl; ENST00000644144.2; ENSP00000494600.1; ENSG00000106992.19.
DR GeneID; 203; -.
DR KEGG; hsa:203; -.
DR MANE-Select; ENST00000644144.2; ENSP00000494600.1; NM_000476.3; NP_000467.1.
DR CTD; 203; -.
DR DisGeNET; 203; -.
DR GeneCards; AK1; -.
DR HGNC; HGNC:361; AK1.
DR HPA; ENSG00000106992; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; AK1; -.
DR MIM; 103000; gene.
DR MIM; 612631; phenotype.
DR neXtProt; NX_P00568; -.
DR OpenTargets; ENSG00000106992; -.
DR Orphanet; 86817; Hemolytic anemia due to adenylate kinase deficiency.
DR PharmGKB; PA24655; -.
DR VEuPathDB; HostDB:ENSG00000106992; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000158325; -.
DR HOGENOM; CLU_032354_0_3_1; -.
DR InParanoid; P00568; -.
DR OMA; TQCDRMI; -.
DR PhylomeDB; P00568; -.
DR TreeFam; TF354283; -.
DR BRENDA; 2.7.4.3; 2681.
DR PathwayCommons; P00568; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P00568; -.
DR SignaLink; P00568; -.
DR BioGRID-ORCS; 203; 15 hits in 1110 CRISPR screens.
DR EvolutionaryTrace; P00568; -.
DR GenomeRNAi; 203; -.
DR Pharos; P00568; Tbio.
DR PRO; PR:P00568; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P00568; protein.
DR Bgee; ENSG00000106992; Expressed in apex of heart and 98 other tissues.
DR ExpressionAtlas; P00568; baseline and differential.
DR Genevisible; P00568; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001520; C:outer dense fiber; IEA:Ensembl.
DR GO; GO:0004017; F:adenylate kinase activity; EXP:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03171; Adenylate_kinase_AK1; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR028582; AK1.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Disease variant; Hereditary hemolytic anemia;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158910"
FT REGION 38..67
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT REGION 131..141
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 65..67
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 94..97
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 138
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 149
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171,
FT ECO:0000269|PubMed:183954"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 40
FT /note="G -> R (in HAAKD; dbSNP:rs137853204)"
FT /evidence="ECO:0000269|PubMed:12649162"
FT /id="VAR_055337"
FT VARIANT 64
FT /note="G -> R (in HAAKD; dbSNP:rs137853205)"
FT /evidence="ECO:0000269|PubMed:12649162"
FT /id="VAR_055338"
FT VARIANT 123
FT /note="E -> Q (in dbSNP:rs8192462)"
FT /id="VAR_034046"
FT VARIANT 128
FT /note="R -> W (in HAAKD; dbSNP:rs104894101)"
FT /evidence="ECO:0000269|PubMed:2542324"
FT /id="VAR_004021"
FT VARIANT 140
FT /note="Missing (in HAAKD)"
FT /evidence="ECO:0000269|PubMed:12649162"
FT /id="VAR_055339"
FT VARIANT 164
FT /note="Y -> C (in HAAKD; dbSNP:rs137853203)"
FT /evidence="ECO:0000269|PubMed:9432020"
FT /id="VAR_055340"
FT CONFLICT 9
FT /note="K -> N (in Ref. 5; AAH01116)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Q -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:2C95"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2C95"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2C95"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:2C95"
SQ SEQUENCE 194 AA; 21635 MW; 95EC5AAA92D1F00F CRC64;
MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI
MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA
GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD
SVFSQVCTHL DALK
