RPA1_HUMAN
ID RPA1_HUMAN Reviewed; 1720 AA.
AC O95602; B7Z7T0; D6W5M0; Q0VG05; Q9UEH0; Q9UFT9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA1;
DE Short=RNA polymerase I subunit A1;
DE EC=2.7.7.6;
DE AltName: Full=A190;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
DE AltName: Full=DNA-directed RNA polymerase I subunit A;
DE AltName: Full=RNA polymerase I 194 kDa subunit;
DE Short=RPA194;
GN Name=POLR1A;
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], AND VARIANT ALA-150.
RA Wang D., Stetler D.A.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-150.
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1626-1720.
RC TISSUE=Uterus;
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 IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA Zomerdijk J.C.B.M.;
RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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 [11]
RP INTERACTION WITH ERBB2.
RX PubMed=21555369; DOI=10.1158/0008-5472.can-10-3504;
RA Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y.,
RA Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H.,
RA Hung M.C.;
RT "Nuclear ErbB2 enhances translation and cell growth by activating
RT transcription of ribosomal RNA genes.";
RL Cancer Res. 71:4269-4279(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, 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 [13]
RP INVOLVEMENT IN AFDCIN, AND VARIANTS AFDCIN GLN-593 AND PHE-1299.
RX PubMed=25913037; DOI=10.1016/j.ajhg.2015.03.011;
RA Weaver K.N., Watt K.E., Hufnagel R.B., Navajas Acedo J., Linscott L.L.,
RA Sund K.L., Bender P.L., Koenig R., Lourenco C.M., Hehr U., Hopkin R.J.,
RA Lohmann D.R., Trainor P.A., Wieczorek D., Saal H.M.;
RT "Acrofacial dysostosis, Cincinnati type, a mandibulofacial dysostosis
RT syndrome with limb anomalies, is caused by POLR1A dysfunction.";
RL Am. J. Hum. Genet. 96:765-774(2015).
RN [14]
RP INTERACTION WITH DDX11.
RX PubMed=26089203; DOI=10.1093/hmg/ddv213;
RA Sun X., Chen H., Deng Z., Hu B., Luo H., Zeng X., Han L., Cai G., Ma L.;
RT "The Warsaw breakage syndrome-related protein DDX11 is required for
RT ribosomal RNA synthesis and embryonic development.";
RL Hum. Mol. Genet. 24:4901-4915(2015).
RN [15]
RP INTERACTION WITH RECQL5.
RX PubMed=27502483; DOI=10.1083/jcb.201507099;
RA Urban V., Dobrovolna J., Huehn D., Fryzelkova J., Bartek J., Janscak P.;
RT "RECQ5 helicase promotes resolution of conflicts between replication and
RT transcription in human cells.";
RL J. Cell Biol. 214:401-415(2016).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase I which
CC synthesizes ribosomal RNA precursors. Forms the polymerase active
CC center together with the second largest subunit. A single stranded DNA
CC template strand of the promoter is positioned within the central active
CC site cleft of Pol I. A bridging helix emanates from RPA1 and crosses
CC the cleft near the catalytic site and is thought to promote
CC translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC hybrid through the active site by switching from straight to bent
CC conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250|UniProtKB:P10964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits (PubMed:16809778). Interacts with MYO1C (By
CC similarity). Interacts with ERBB2 (PubMed:21555369). Interacts with
CC DDX11 (PubMed:26089203). Interacts with RECQL5 (PubMed:27502483).
CC {ECO:0000250|UniProtKB:O35134, ECO:0000269|PubMed:16809778,
CC ECO:0000269|PubMed:21555369, ECO:0000269|PubMed:26089203,
CC ECO:0000269|PubMed:27502483}.
CC -!- INTERACTION:
CC O95602; Q96IM9: DYDC2; NbExp=3; IntAct=EBI-359472, EBI-749277;
CC O95602; P04626: ERBB2; NbExp=16; IntAct=EBI-359472, EBI-641062;
CC O95602; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-359472, EBI-16439278;
CC O95602; Q9H9Y6: POLR1B; NbExp=3; IntAct=EBI-359472, EBI-355441;
CC O95602; Q04864: REL; NbExp=3; IntAct=EBI-359472, EBI-307352;
CC O95602; P15884: TCF4; NbExp=3; IntAct=EBI-359472, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P10964}. Chromosome
CC {ECO:0000250|UniProtKB:O35134}.
CC -!- DISEASE: Acrofacial dysostosis, Cincinnati type (AFDCIN) [MIM:616462]:
CC A form of acrofacial dysostosis, a group of disorders which are
CC characterized by malformation of the craniofacial skeleton and, in some
CC patients, the limbs. {ECO:0000269|PubMed:25913037}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99959.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD09356.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U33460; AAC99959.1; ALT_FRAME; mRNA.
DR EMBL; AH007280; AAD09356.1; ALT_FRAME; Transcribed_RNA.
DR EMBL; AK302458; BAH13716.1; -; mRNA.
DR EMBL; CH471053; EAW99467.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99469.1; -; Genomic_DNA.
DR EMBL; BC117173; AAI17174.1; -; mRNA.
DR EMBL; BC126303; AAI26304.1; -; mRNA.
DR EMBL; AL117467; CAB55942.1; -; mRNA.
DR CCDS; CCDS42706.1; -.
DR PIR; T17252; T17252.
DR RefSeq; NP_056240.2; NM_015425.4.
DR PDB; 7OB9; EM; 2.70 A; A=1-1720.
DR PDB; 7OBA; EM; 3.10 A; A=1-1720.
DR PDB; 7OBB; EM; 3.30 A; A=1-1720.
DR PDB; 7VBA; EM; 2.89 A; A=1-1719.
DR PDB; 7VBB; EM; 2.81 A; A=1-1719.
DR PDB; 7VBC; EM; 3.01 A; A=1-1719.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; O95602; -.
DR SMR; O95602; -.
DR BioGRID; 117396; 153.
DR CORUM; O95602; -.
DR DIP; DIP-27537N; -.
DR IntAct; O95602; 70.
DR MINT; O95602; -.
DR STRING; 9606.ENSP00000263857; -.
DR BindingDB; O95602; -.
DR ChEMBL; CHEMBL3286067; -.
DR iPTMnet; O95602; -.
DR MetOSite; O95602; -.
DR PhosphoSitePlus; O95602; -.
DR SwissPalm; O95602; -.
DR BioMuta; POLR1A; -.
DR SWISS-2DPAGE; O95602; -.
DR EPD; O95602; -.
DR jPOST; O95602; -.
DR MassIVE; O95602; -.
DR MaxQB; O95602; -.
DR PaxDb; O95602; -.
DR PeptideAtlas; O95602; -.
DR PRIDE; O95602; -.
DR ProteomicsDB; 50948; -.
DR Antibodypedia; 4117; 124 antibodies from 27 providers.
DR DNASU; 25885; -.
DR Ensembl; ENST00000263857.11; ENSP00000263857.6; ENSG00000068654.17.
DR GeneID; 25885; -.
DR KEGG; hsa:25885; -.
DR MANE-Select; ENST00000263857.11; ENSP00000263857.6; NM_015425.6; NP_056240.2.
DR UCSC; uc002sqs.4; human.
DR CTD; 25885; -.
DR DisGeNET; 25885; -.
DR GeneCards; POLR1A; -.
DR HGNC; HGNC:17264; POLR1A.
DR HPA; ENSG00000068654; Low tissue specificity.
DR MalaCards; POLR1A; -.
DR MIM; 616404; gene.
DR MIM; 616462; phenotype.
DR neXtProt; NX_O95602; -.
DR OpenTargets; ENSG00000068654; -.
DR Orphanet; 1200; Burn-McKeown syndrome.
DR PharmGKB; PA134891380; -.
DR VEuPathDB; HostDB:ENSG00000068654; -.
DR eggNOG; KOG0262; Eukaryota.
DR GeneTree; ENSGT00920000149138; -.
DR InParanoid; O95602; -.
DR OMA; RFFNRED; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; O95602; -.
DR TreeFam; TF103033; -.
DR PathwayCommons; O95602; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR SignaLink; O95602; -.
DR SIGNOR; O95602; -.
DR BioGRID-ORCS; 25885; 684 hits in 1050 CRISPR screens.
DR ChiTaRS; POLR1A; human.
DR GeneWiki; POLR1A; -.
DR GenomeRNAi; 25885; -.
DR Pharos; O95602; Tchem.
DR PRO; PR:O95602; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95602; protein.
DR Bgee; ENSG00000068654; Expressed in sural nerve and 129 other tissues.
DR ExpressionAtlas; O95602; baseline and differential.
DR Genevisible; O95602; HS.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Disease variant; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1720
FT /note="DNA-directed RNA polymerase I subunit RPA1"
FT /id="PRO_0000073923"
FT REGION 961..973
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1365..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1409
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 150
FT /note="P -> A (in dbSNP:rs4832242)"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.3"
FT /id="VAR_047493"
FT VARIANT 349
FT /note="Q -> E (in dbSNP:rs17026866)"
FT /id="VAR_047494"
FT VARIANT 364
FT /note="K -> E (in dbSNP:rs35239368)"
FT /id="VAR_047495"
FT VARIANT 396
FT /note="S -> N (in dbSNP:rs35443467)"
FT /id="VAR_047496"
FT VARIANT 593
FT /note="E -> Q (in AFDCIN; dbSNP:rs794729674)"
FT /evidence="ECO:0000269|PubMed:25913037"
FT /id="VAR_073964"
FT VARIANT 815
FT /note="I -> V (in dbSNP:rs34302587)"
FT /id="VAR_047497"
FT VARIANT 1141
FT /note="A -> T (in dbSNP:rs34892520)"
FT /id="VAR_047498"
FT VARIANT 1299
FT /note="V -> F (in AFDCIN; dbSNP:rs751377255)"
FT /evidence="ECO:0000269|PubMed:25913037"
FT /id="VAR_073965"
FT VARIANT 1608
FT /note="I -> M (in dbSNP:rs35093541)"
FT /id="VAR_047499"
FT CONFLICT 143
FT /note="N -> S (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Y -> S (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="M -> R (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="YA -> ST (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="A -> R (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="S -> T (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="M -> L (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 925..926
FT /note="RP -> ST (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="G -> A (in Ref. 1; AAD09356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371..1373
FT /note="RAT -> TRI (in Ref. 1; AAD09356)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470..1471
FT /note="Missing (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT CONFLICT 1616
FT /note="Missing (in Ref. 1; AAC99959)"
FT /evidence="ECO:0000305"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 258..279
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 323..345
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:7OBB"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 387..402
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 433..447
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 477..486
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 561..571
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 582..585
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 593..597
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 602..610
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 632..641
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 650..660
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 684..693
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:7OBA"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 736..740
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 743..747
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 751..754
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 761..768
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 771..791
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 800..802
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 806..819
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 824..831
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 839..849
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:7OBB"
FT HELIX 857..880
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 881..887
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 889..891
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 893..899
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 906..913
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 945..948
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 955..957
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 961..996
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1003..1005
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1014..1018
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1019..1021
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1026..1028
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1034..1036
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1037..1041
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1044..1048
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1054..1056
FT /evidence="ECO:0007829|PDB:7OBB"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1063..1078
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1088..1094
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1098..1101
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1110..1112
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1115..1125
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1129..1131
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1132..1137
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1146..1149
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1152..1154
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1161..1180
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1181..1183
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1189..1202
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1211..1220
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1222..1225
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1235..1237
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1244..1252
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1264..1268
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1272..1285
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1290..1293
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1294..1299
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1302..1304
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1307..1309
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1312..1314
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1317..1321
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1324..1326
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1328..1330
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1335..1344
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1346..1358
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1500..1506
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1514..1517
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1519..1521
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1524..1528
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1529..1531
FT /evidence="ECO:0007829|PDB:7OBA"
FT HELIX 1540..1550
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1552..1554
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1559..1566
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1570..1572
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1577..1582
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1585..1587
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1588..1590
FT /evidence="ECO:0007829|PDB:7OBB"
FT TURN 1592..1594
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1597..1599
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1601..1603
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1605..1611
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1614..1629
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1630..1633
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1638..1648
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1649..1651
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 1659..1661
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1662..1664
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1668..1674
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1677..1687
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 1696..1701
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1707..1709
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 1712..1718
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 1720 AA; 194811 MW; AD4BA543FFB98DC6 CRC64;
MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS
KEVCSTCVQD FSNCSGHLGH IELPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAVIHLL
LCQLRVLEVG ALQAVYELER ILNRFLEENP DPSASEIREE LEQYTTEIVQ NNLLGSQGAH
VKNVCESKSK LIALFWKAHM NAKRCPHCKT GRSVVRKEHN SKLTITFPAM VHRTAGQKDS
EPLGIEEAQI GKRGYLTPTS AREHLSALWK NEGFFLNYLF SGMDDDGMES RFNPSVFFLD
FLVVPPSRYR PVSRLGDQMF TNGQTVNLQA VMKDVVLIRK LLALMAQEQK LPEEVATPTT
DEEKDSLIAI DRSFLSTLPG QSLIDKLYNI WIRLQSHVNI VFDSEMDKLM MDKYPGIRQI
LEKKEGLFRK HMMGKRVDYA ARSVICPDMY INTNEIGIPM VFATKLTYPQ PVTPWNVQEL
RQAVINGPNV HPGASMVINE DGSRTALSAV DMTQREAVAK QLLTPATGAP KPQGTKIVCR
HVKNGDILLL NRQPTLHRPS IQAHRARILP EEKVLRLHYA NCKAYNADFD GDEMNAHFPQ
SELGRAEAYV LACTDQQYLV PKDGQPLAGL IQDHMVSGAS MTTRGCFFTR EHYMELVYRG
LTDKVGRVKL LSPSILKPFP LWTGKQVVST LLINIIPEDH IPLNLSGKAK ITGKAWVKET
PRSVPGFNPD SMCESQVIIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GETSGKVLTC
LARLFTAYLQ LYRGFTLGVE DILVKPKADV KRQRIIEEST HCGPQAVRAA LNLPEAASYD
EVRGKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQFP ENSLQMMVQS
GAKGSTVNTM QISCLLGQIE LEGRRPPLMA SGKSLPCFEP YEFTPRAGGF VTGRFLTGIK
PPEFFFHCMA GREGLVDTAV KTSRSGYLQR CIIKHLEGLV VQYDLTVRDS DGSVVQFLYG
EDGLDIPKTQ FLQPKQFPFL ASNYEVIMKS QHLHEVLSRA DPKKALHHFR AIKKWQSKHP
NTLLRRGAFL SYSQKIQEAV KALKLESENR NGRSPGTQEM LRMWYELDEE SRRKYQKKAA
ACPDPSLSVW RPDIYFASVS ETFETKVDDY SQEWAAQTEK SYEKSELSLD RLRTLLQLKW
QRSLCEPGEA VGLLAAQSIG EPSTQMTLNT FHFAGRGEMN VTLGIPRLRE ILMVASANIK
TPMMSVPVLN TKKALKRVKS LKKQLTRVCL GEVLQKIDVQ ESFCMEEKQN KFQVYQLRFQ
FLPHAYYQQE KCLRPEDILR FMETRFFKLL MESIKKKNNK ASAFRNVNTR RATQRDLDNA
GELGRSRGEQ EGDEEEEGHI VDAEAEEGDA DASDAKRKEK QEEEVDYESE EEEEREGEEN
DDEDMQEERN PHREGARKTQ EQDEEVGLGT EEDPSLPALL TQPRKPTHSQ EPQGPEAMER
RVQAVREIHP FIDDYQYDTE ESLWCQVTVK LPLMKINFDM SSLVVSLAHG AVIYATKGIT
RCLLNETTNN KNEKELVLNT EGINLPELFK YAEVLDLRRL YSNDIHAIAN TYGIEAALRV
IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIRSNSSPLQ QMTFETSFQF
LKQATMLGSH DELRSPSACL VVGKVVRGGT GLFELKQPLR
