ID PAPD1_HUMAN Reviewed; 582 AA. AC Q9NVV4; D3DRX0; Q659E3; Q6P7E5; Q9HA74; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Poly(A) RNA polymerase, mitochondrial; DE Short=PAP; DE EC=2.7.7.19 {ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}; DE AltName: Full=PAP-associated domain-containing protein 1; DE AltName: Full=Polynucleotide adenylyltransferase; DE AltName: Full=Terminal uridylyltransferase 1; DE Short=TUTase 1; DE AltName: Full=mtPAP; DE Flags: Precursor; GN Name=MTPAP; Synonyms=PAPD1; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Cervix carcinoma; RX PubMed=15547249; DOI=10.1093/nar/gkh923; RA Tomecki R., Dmochowska A., Gewartowski K., Dziembowski A., Stepien P.P.; RT "Identification of a novel human nuclear-encoded mitochondrial poly(A) RT polymerase."; RL Nucleic Acids Res. 32:6001-6014(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15769737; DOI=10.1074/jbc.m500804200; RA Nagaike T., Suzuki T., Katoh T., Ueda T.; RT "Human mitochondrial mRNAs are stabilized with polyadenylation regulated by RT mitochondria-specific poly(A) polymerase and polynucleotide RT phosphorylase."; RL J. Biol. Chem. 280:19721-19727(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=16533400; DOI=10.1186/1471-2164-7-48; RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.; RT "NovelFam3000 -- uncharacterized human protein domains conserved across RT model organisms."; RL BMC Genomics 7:48-48(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Mammary gland; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-221; RP ARG-419 AND ASN-546. 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 [9] RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=18172165; DOI=10.1101/gad.1622708; RA Mullen T.E., Marzluff W.F.; RT "Degradation of histone mRNA requires oligouridylation followed by RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to RT 5'."; RL Genes Dev. 22:50-65(2008). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, 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 [11] 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 [12] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 44-538, FUNCTION, CATALYTIC RP ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS RP OF 221-TYR-PHE-222; PHE-230; 259-HIS--ILE-261; 294-HIS--PRO-297; LEU-312; RP ASP-325 AND PHE-378. RX PubMed=21292163; DOI=10.1016/j.molcel.2011.01.013; RA Bai Y., Srivastava S.K., Chang J.H., Manley J.L., Tong L.; RT "Structural basis for dimerization and activity of human PAPD1, a RT noncanonical poly(A) polymerase."; RL Mol. Cell 41:311-320(2011). RN [13] RP VARIANT SPAX4 ASP-478, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=20970105; DOI=10.1016/j.ajhg.2010.09.013; RA Crosby A.H., Patel H., Chioza B.A., Proukakis C., Gurtz K., Patton M.A., RA Sharifi R., Harlalka G., Simpson M.A., Dick K., Reed J.A., Al-Memar A., RA Chrzanowska-Lightowlers Z.M., Cross H.E., Lightowlers R.N.; RT "Defective mitochondrial mRNA maturation is associated with spastic RT ataxia."; RL Am. J. Hum. Genet. 87:655-660(2010). CC -!- FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial CC transcripts. Can use all four nucleotides, but has higher activity with CC ATP and UTP (in vitro). Plays a role in replication-dependent histone CC mRNA degradation. May be involved in the terminal uridylation of mature CC histone mRNAs before their degradation is initiated. Might be CC responsible for the creation of some UAA stop codons which are not CC encoded in mtDNA. {ECO:0000269|PubMed:15547249, CC ECO:0000269|PubMed:15769737, ECO:0000269|PubMed:18172165, CC ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, CC ChEBI:CHEBI:173115; EC=2.7.7.19; CC Evidence={ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:21292163}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:21292163}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.1 mM for ATP {ECO:0000269|PubMed:21292163}; CC KM=0.7 mM for UTP {ECO:0000269|PubMed:21292163}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21292163}. CC -!- INTERACTION: CC Q9NVV4; Q13137: CALCOCO2; NbExp=2; IntAct=EBI-2556166, EBI-739580; CC Q9NVV4; Q9NVV4: MTPAP; NbExp=3; IntAct=EBI-2556166, EBI-2556166; CC Q9NVV4; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-2556166, EBI-356402; CC Q9NVV4; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-2556166, EBI-6115874; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18172165}. CC Mitochondrion {ECO:0000269|PubMed:15547249, CC ECO:0000269|PubMed:15769737}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NVV4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NVV4-2; Sequence=VSP_020724; CC -!- TISSUE SPECIFICITY: Ubiquitous, with stronger expression in tissues CC with high energy requirements: heart, brain, and skeletal muscle. CC {ECO:0000269|PubMed:15547249}. CC -!- DISEASE: Spastic ataxia 4, autosomal recessive (SPAX4) [MIM:613672]: A CC slowly progressive neurodegenerative disease characterized by CC cerebellar ataxia, spastic paraparesis, dysarthria, and optic atrophy. CC {ECO:0000269|PubMed:20970105}. Note=The disease is caused by variants CC affecting the gene represented in this entry. MTPAP mutations result in CC a defect of mitochondrial mRNA maturation. Affected individuals exhibit CC a drastic decrease in poly(A) tail length of mitochondrial mRNA CC transcripts, including COX1 and RNA14 (PubMed:20970105). CC {ECO:0000269|PubMed:20970105}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. CC {ECO:0000305}. 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; AB194709; BAD98252.1; -; mRNA. DR EMBL; AY364242; AAQ76801.1; -; mRNA. DR EMBL; AK001348; BAA91641.1; -; mRNA. DR EMBL; AK022188; BAB13981.1; -; mRNA. DR EMBL; AL122121; CAH56395.1; -; mRNA. DR EMBL; AL161651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353796; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86014.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86015.1; -; Genomic_DNA. DR EMBL; BC061703; AAH61703.1; -; mRNA. DR CCDS; CCDS7165.1; -. [Q9NVV4-1] DR RefSeq; NP_060579.3; NM_018109.3. [Q9NVV4-1] DR PDB; 3PQ1; X-ray; 3.10 A; A/B=44-134, A/B=172-452, A/B=490-538. DR PDBsum; 3PQ1; -. DR AlphaFoldDB; Q9NVV4; -. DR SMR; Q9NVV4; -. DR BioGRID; 120452; 196. DR IntAct; Q9NVV4; 29. DR MINT; Q9NVV4; -. DR STRING; 9606.ENSP00000263063; -. DR iPTMnet; Q9NVV4; -. DR PhosphoSitePlus; Q9NVV4; -. DR SwissPalm; Q9NVV4; -. DR BioMuta; MTPAP; -. DR DMDM; 74753002; -. DR EPD; Q9NVV4; -. DR jPOST; Q9NVV4; -. DR MassIVE; Q9NVV4; -. DR MaxQB; Q9NVV4; -. DR PaxDb; 9606-ENSP00000263063; -. DR PeptideAtlas; Q9NVV4; -. DR ProteomicsDB; 82864; -. [Q9NVV4-1] DR ProteomicsDB; 82865; -. [Q9NVV4-2] DR Pumba; Q9NVV4; -. DR Antibodypedia; 35309; 115 antibodies from 17 providers. DR DNASU; 55149; -. DR Ensembl; ENST00000263063.9; ENSP00000263063.3; ENSG00000107951.15. [Q9NVV4-1] DR GeneID; 55149; -. DR KEGG; hsa:55149; -. DR MANE-Select; ENST00000263063.9; ENSP00000263063.3; NM_018109.4; NP_060579.3. DR UCSC; uc001iva.5; human. [Q9NVV4-1] DR AGR; HGNC:25532; -. DR CTD; 55149; -. DR DisGeNET; 55149; -. DR GeneCards; MTPAP; -. DR HGNC; HGNC:25532; MTPAP. DR HPA; ENSG00000107951; Tissue enhanced (bone). DR MalaCards; MTPAP; -. DR MIM; 613669; gene. DR MIM; 613672; phenotype. DR neXtProt; NX_Q9NVV4; -. DR OpenTargets; ENSG00000107951; -. DR Orphanet; 254343; Autosomal recessive spastic ataxia-optic atrophy-dysarthria syndrome. DR PharmGKB; PA164723192; -. DR VEuPathDB; HostDB:ENSG00000107951; -. DR eggNOG; KOG2277; Eukaryota. DR GeneTree; ENSGT00940000158582; -. DR HOGENOM; CLU_018757_3_1_1; -. DR InParanoid; Q9NVV4; -. DR OMA; RTVLIKC; -. DR OrthoDB; 170176at2759; -. DR PhylomeDB; Q9NVV4; -. DR TreeFam; TF354308; -. DR BRENDA; 2.7.7.19; 2681. DR PathwayCommons; Q9NVV4; -. DR SABIO-RK; Q9NVV4; -. DR SignaLink; Q9NVV4; -. DR BioGRID-ORCS; 55149; 531 hits in 1171 CRISPR screens. DR ChiTaRS; MTPAP; human. DR EvolutionaryTrace; Q9NVV4; -. DR GenomeRNAi; 55149; -. DR Pharos; Q9NVV4; Tbio. DR PRO; PR:Q9NVV4; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9NVV4; Protein. DR Bgee; ENSG00000107951; Expressed in oocyte and 199 other cell types or tissues. DR ExpressionAtlas; Q9NVV4; baseline and differential. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0002134; F:UTP binding; IDA:UniProtKB. DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0000965; P:mitochondrial RNA 3'-end processing; IDA:UniProtKB. DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central. DR CDD; cd05402; NT_PAP_TUTase; 1. DR Gene3D; 1.10.1410.10; -; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002058; PAP_assoc. DR InterPro; IPR041252; RL. DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1. DR PANTHER; PTHR12271:SF133; POLY(A) RNA POLYMERASE, MITOCHONDRIAL; 1. DR Pfam; PF03828; PAP_assoc; 1. DR Pfam; PF17797; RL; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1. DR Genevisible; Q9NVV4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Disease variant; Magnesium; Manganese; Metal-binding; Mitochondrion; KW mRNA processing; Neurodegeneration; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transcription; KW Transferase; Transit peptide. FT TRANSIT 1..37 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 38..582 FT /note="Poly(A) RNA polymerase, mitochondrial" FT /id="PRO_0000250689" FT DOMAIN 437..483 FT /note="PAP-associated" FT BINDING 107..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 241..242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 243 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT MOD_RES 90 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..52 FT /note="MAVPGVGLLTRLNLCARRRTRVQRPIVRLLSCPGTVAKDLRRDEQPSGSVET FT -> MAWAKKVGGRAGQGRSLSRCDPIILDPEWLYGPPEGEGGPEGVGGETRASIHPPLR FT TGRHHQKVNHNIRGPEGSAKDAAPGGGGHHQAGPGQRGDEDGALQHLCGGGGGVGVSVG FT RGTGTSVAAEHPSLQVKLLELQELVLRLAGDHNEGHGKFLAAAQNPADDPAPGAPAPQE FT LGAADKQG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_020724" FT VARIANT 162 FT /note="R -> C (in dbSNP:rs1047991)" FT /id="VAR_027601" FT VARIANT 221 FT /note="Y -> H (in dbSNP:rs17855118)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027602" FT VARIANT 419 FT /note="C -> R (in dbSNP:rs17857517)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027603" FT VARIANT 478 FT /note="N -> D (in SPAX4; dbSNP:rs267606900)" FT /evidence="ECO:0000269|PubMed:20970105" FT /id="VAR_064907" FT VARIANT 546 FT /note="S -> N (in dbSNP:rs17855116)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027604" FT MUTAGEN 221..222 FT /note="YF->AA: Reduces dimerization." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 230 FT /note="F->A: Reduced enzyme activity." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 259..261 FT /note="HKI->AAA: No effect on dimerization. Loss of FT dimerization and of enzyme activity; when associated with FT 294-AAAA-297." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 294..297 FT /note="HFGP->AAGA: Reduced dimerization. Loss of FT dimerization and of enzyme activity; when associated with FT 259-AAA-261." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 312 FT /note="L->A: Reduced enzyme activity." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 325 FT /note="D->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:21292163" FT MUTAGEN 378 FT /note="F->A: Reduced enzyme activity." FT /evidence="ECO:0000269|PubMed:21292163" FT CONFLICT 507 FT /note="W -> L (in Ref. 4; BAB13981)" FT /evidence="ECO:0000305" FT CONFLICT 554 FT /note="V -> A (in Ref. 4; BAB13981)" FT /evidence="ECO:0000305" FT HELIX 64..75 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 90..95 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 109..117 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 125..128 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 174..180 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 186..197 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 201..218 FT /evidence="ECO:0007829|PDB:3PQ1" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 277..294 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 299..305 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 312..317 FT /evidence="ECO:0007829|PDB:3PQ1" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:3PQ1" FT STRAND 323..327 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 333..344 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 348..363 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 377..389 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 403..406 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 437..447 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 448..450 FT /evidence="ECO:0007829|PDB:3PQ1" FT TURN 482..484 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 492..510 FT /evidence="ECO:0007829|PDB:3PQ1" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:3PQ1" SQ SEQUENCE 582 AA; 66172 MW; EBA5BECEA39A5090 CRC64; MAVPGVGLLT RLNLCARRRT RVQRPIVRLL SCPGTVAKDL RRDEQPSGSV ETGFEDKIPK RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP INNHFFYESF GLYAVVEFCQ KESIGSLQNG THTPSTAMET AIPFRSRFFN LKLKNQTSER SRVRSSNQLP RSNKQLFELL CYAESIDDQL NTLLKEFQLT EENTKLRYLT CSLIEDMAAA YFPDCIVRPF GSSVNTFGKL GCDLDMFLDL DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE CLDHFGPGCV GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV RALVFSVRCW ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD SLKTLADAED KCVIEGNNCT FVRDLSRIKP SQNTETLELL LKEFFEYFGN FAFDKNSINI RQGREQNKPD SSPLYIQNPF ETSLNISKNV SQSQLQKFVD LARESAWILQ QEDTDRPSIS SNRPWGLVSL LLPSAPNRKS FTKKKSNKFA IETVKNLLES LKGNRTENFT KTSGKRTIST QT //