NMNA2_HUMAN
ID NMNA2_HUMAN Reviewed; 307 AA.
AC Q9BZQ4; O75067; Q5T1Q3; Q8WU99; Q96QW1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
DE Short=NMN/NaMN adenylyltransferase 2;
DE EC=2.7.7.1 {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
DE EC=2.7.7.18 {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
DE AltName: Full=Nicotinamide mononucleotide adenylyltransferase 2;
DE Short=NMN adenylyltransferase 2;
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 2;
DE Short=NaMN adenylyltransferase 2;
GN Name=NMNAT2 {ECO:0000312|HGNC:HGNC:16789};
GN Synonyms=C1orf15 {ECO:0000312|HGNC:HGNC:16789},
GN KIAA0479 {ECO:0000303|PubMed:9455484};
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 [MRNA] (ISOFORM 1).
RX PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA Carpten J.D.;
RT "Cloning and characterization of 13 novel transcripts and the human RGS8
RT gene from the 1q25 region encompassing the hereditary prostate cancer
RT (HPC1) locus.";
RL Genomics 73:211-222(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung carcinoma;
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 [5]
RP SUBUNIT, COFACTOR, TISSUE SPECIFICITY, AND PH DEPENDENCE.
RX PubMed=12359228; DOI=10.1016/s0006-291x(02)02285-4;
RA Raffaelli N., Sorci L., Amici A., Emanuelli M., Mazzola F., Magni G.;
RT "Identification of a novel human nicotinamide mononucleotide
RT adenylyltransferase.";
RL Biochem. Biophys. Res. Commun. 297:835-840(2002).
RN [6]
RP MUTAGENESIS OF HIS-24 AND TRP-92, COFACTOR, AND TISSUE SPECIFICITY.
RX PubMed=14516279; DOI=10.1042/bj20030518;
RA Yalowitz J.A., Xiao S., Biju M.P., Antony A.C., Cummings O.W., Deeg M.A.,
RA Jayaram H.N.;
RT "Characterization of human brain nicotinamide 5'-mononucleotide
RT adenylyltransferase-2 and expression in human pancreas.";
RL Biochem. J. 377:317-326(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16118205; DOI=10.1074/jbc.m508660200;
RA Berger F., Lau C., Dahlmann M., Ziegler M.;
RT "Subcellular compartmentation and differential catalytic properties of the
RT three human nicotinamide mononucleotide adenylyltransferase isoforms.";
RL J. Biol. Chem. 280:36334-36341(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=17402747; DOI=10.1021/bi6023379;
RA Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L.,
RA Franchetti P., Orsomando G., Magni G.;
RT "Initial-rate kinetics of human NMN-adenylyltransferases: substrate and
RT metal ion specificity, inhibition by products and multisubstrate analogues,
RT and isozyme contributions to NAD+ biosynthesis.";
RL Biochemistry 46:4912-4922(2007).
RN [9]
RP UBIQUITINATION.
RX PubMed=29643511; DOI=10.1038/s41586-018-0026-1;
RA Pao K.C., Wood N.T., Knebel A., Rafie K., Stanley M., Mabbitt P.D.,
RA Sundaramoorthy R., Hofmann K., van Aalten D.M.F., Virdee S.;
RT "Activity-based E3 ligase profiling uncovers an E3 ligase with
RT esterification activity.";
RL Nature 556:381-385(2018).
CC -!- FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that
CC acts as an axon maintenance factor (By similarity). Catalyzes the
CC formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP
CC (PubMed:16118205, PubMed:17402747). Can also use the deamidated form;
CC nicotinic acid mononucleotide (NaMN) as substrate but with a lower
CC efficiency (PubMed:16118205, PubMed:17402747). Cannot use triazofurin
CC monophosphate (TrMP) as substrate (PubMed:16118205, PubMed:17402747).
CC Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic
CC cleavage of NAD(+) (PubMed:16118205, PubMed:17402747). For the
CC pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates
CC and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less
CC effectively (PubMed:16118205, PubMed:17402747). Fails to cleave
CC phosphorylated dinucleotides NADP(+), NADPH and NaADP(+)
CC (PubMed:16118205, PubMed:17402747). Axon survival factor required for
CC the maintenance of healthy axons: acts by delaying Wallerian axon
CC degeneration, an evolutionarily conserved process that drives the loss
CC of damaged axons (By similarity). {ECO:0000250|UniProtKB:Q8BNJ3,
CC ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC Evidence={ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21361;
CC Evidence={ECO:0000305|PubMed:16118205};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21362;
CC Evidence={ECO:0000305|PubMed:16118205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58437; EC=2.7.7.18;
CC Evidence={ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22861;
CC Evidence={ECO:0000305|PubMed:16118205};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22862;
CC Evidence={ECO:0000305|PubMed:16118205};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12359228, ECO:0000269|PubMed:14516279,
CC ECO:0000269|PubMed:17402747};
CC Note=Divalent metal cations. Mg(2+) confers the highest activity.
CC {ECO:0000269|PubMed:12359228, ECO:0000269|PubMed:14516279,
CC ECO:0000269|PubMed:17402747};
CC -!- ACTIVITY REGULATION: Inhibited by P1-(adenosine-5')-P3-(nicotinamide-
CC riboside-5')-triphosphate (Np3AD) and P1-(adenosine-5')-P4-
CC (nicotinamide-riboside-5')-tetraphosphate (Np4AD).
CC {ECO:0000269|PubMed:17402747}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for NMN {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC KM=70 uM for NAD(+) {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC KM=204 uM for ATP {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC KM=1119 uM for PPi {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC KM=14.5 uM for NaMN {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC KM=304 uM for NMNH {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747};
CC Vmax=1.1 umol/min/mg enzyme for NAD synthesis
CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC Vmax=3 umol/min/mg enzyme for pyrophosphorolytic NAD(+) cleavage
CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC Vmax=7 umol/min/mg enzyme for pyrophosphorolytic NADH cleavage
CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC Note=KM is >100 uM for triazofurin monophosphate.;
CC pH dependence:
CC Optimum pH is 6.0-9.0. {ECO:0000269|PubMed:12359228,
CC ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000269|PubMed:16118205,
CC ECO:0000269|PubMed:17402747}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12359228}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16118205}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8BNJ3}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasm
CC {ECO:0000269|PubMed:16118205}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q8BNJ3}. Note=Delivered to axons with Golgi-
CC derived cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q8BNJ3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZQ4-2; Sequence=VSP_015571;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, in particular in
CC cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and
CC putamen. Also found in the heart, skeletal muscle, pancreas and islets
CC of Langerhans. {ECO:0000269|PubMed:12359228,
CC ECO:0000269|PubMed:14516279, ECO:0000269|PubMed:16118205}.
CC -!- PTM: Degraded in response to injured neurite. Degradation is probably
CC caused by ubiquitination by MYCBP2 (By similarity). Ubiquitinated on
CC threonine and/or serine residues by MYCBP2; consequences of threonine
CC and/or serine ubiquitination are however unclear (PubMed:29643511).
CC {ECO:0000250|UniProtKB:Q8BNJ3, ECO:0000269|PubMed:29643511}.
CC -!- PTM: Palmitoylated; palmitoylation is required for membrane
CC association. {ECO:0000250|UniProtKB:Q8BNJ3}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32324.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF288395; AAG60615.1; -; mRNA.
DR EMBL; AB007948; BAA32324.1; ALT_INIT; mRNA.
DR EMBL; AL354953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020998; AAH20998.1; -; mRNA.
DR CCDS; CCDS1353.1; -. [Q9BZQ4-1]
DR CCDS; CCDS1354.1; -. [Q9BZQ4-2]
DR RefSeq; NP_055854.1; NM_015039.3. [Q9BZQ4-1]
DR RefSeq; NP_733820.1; NM_170706.3. [Q9BZQ4-2]
DR AlphaFoldDB; Q9BZQ4; -.
DR SMR; Q9BZQ4; -.
DR BioGRID; 116693; 24.
DR CORUM; Q9BZQ4; -.
DR DIP; DIP-60169N; -.
DR STRING; 9606.ENSP00000287713; -.
DR iPTMnet; Q9BZQ4; -.
DR PhosphoSitePlus; Q9BZQ4; -.
DR SwissPalm; Q9BZQ4; -.
DR BioMuta; NMNAT2; -.
DR DMDM; 30580486; -.
DR MassIVE; Q9BZQ4; -.
DR PaxDb; Q9BZQ4; -.
DR PeptideAtlas; Q9BZQ4; -.
DR PRIDE; Q9BZQ4; -.
DR Antibodypedia; 2924; 161 antibodies from 22 providers.
DR DNASU; 23057; -.
DR Ensembl; ENST00000287713.7; ENSP00000287713.6; ENSG00000157064.11. [Q9BZQ4-1]
DR Ensembl; ENST00000294868.8; ENSP00000294868.4; ENSG00000157064.11. [Q9BZQ4-2]
DR GeneID; 23057; -.
DR KEGG; hsa:23057; -.
DR MANE-Select; ENST00000287713.7; ENSP00000287713.6; NM_015039.4; NP_055854.1.
DR UCSC; uc001gqb.2; human. [Q9BZQ4-1]
DR CTD; 23057; -.
DR DisGeNET; 23057; -.
DR GeneCards; NMNAT2; -.
DR HGNC; HGNC:16789; NMNAT2.
DR HPA; ENSG00000157064; Tissue enhanced (brain, heart muscle, pituitary gland).
DR MIM; 608701; gene.
DR neXtProt; NX_Q9BZQ4; -.
DR OpenTargets; ENSG00000157064; -.
DR PharmGKB; PA25604; -.
DR VEuPathDB; HostDB:ENSG00000157064; -.
DR eggNOG; KOG3199; Eukaryota.
DR GeneTree; ENSGT00950000183179; -.
DR HOGENOM; CLU_033366_1_0_1; -.
DR InParanoid; Q9BZQ4; -.
DR OMA; VNHPMSI; -.
DR OrthoDB; 1308027at2759; -.
DR PhylomeDB; Q9BZQ4; -.
DR TreeFam; TF315035; -.
DR BioCyc; MetaCyc:HS08173-MON; -.
DR BRENDA; 2.7.7.1; 2681.
DR BRENDA; 2.7.7.18; 2681.
DR PathwayCommons; Q9BZQ4; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SABIO-RK; Q9BZQ4; -.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR BioGRID-ORCS; 23057; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; NMNAT2; human.
DR GeneWiki; NMNAT2; -.
DR GenomeRNAi; 23057; -.
DR Pharos; Q9BZQ4; Tbio.
DR PRO; PR:Q9BZQ4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZQ4; protein.
DR Bgee; ENSG00000157064; Expressed in middle temporal gyrus and 137 other tissues.
DR Genevisible; Q9BZQ4; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IC:UniProtKB.
DR CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Magnesium; Membrane;
KW NAD; Nucleotide-binding; Nucleotidyltransferase; Palmitate;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW Ubl conjugation.
FT CHAIN 1..307
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase 2"
FT /id="PRO_0000135014"
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 55..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 200..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 271..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT LIPID 164
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8BNJ3"
FT LIPID 165
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8BNJ3"
FT VAR_SEQ 1..28
FT /note="MTETTKTHVILLACGSFNPITKGHIQMF -> MEIQELEEIQACQGLWEVFV
FT TLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015571"
FT MUTAGEN 24
FT /note="H->A: Reduces activity by 95%."
FT /evidence="ECO:0000269|PubMed:14516279"
FT MUTAGEN 92
FT /note="W->G: Reduces activity by 95%."
FT /evidence="ECO:0000269|PubMed:14516279"
SQ SEQUENCE 307 AA; 34439 MW; 702F1C74B38ECECB CRC64;
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL
VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP
SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI
MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ
LYINASG
