RPAB5_HUMAN
ID RPAB5_HUMAN Reviewed; 67 AA.
AC P62875; P52436; Q6FHX3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC5;
DE Short=RNA polymerases I, II, and III subunit ABC5;
DE AltName: Full=DNA-directed RNA polymerase III subunit L;
DE AltName: Full=RNA polymerase II 7.6 kDa subunit;
DE Short=RPB7.6;
DE AltName: Full=RPB10 homolog;
GN Name=POLR2L;
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].
RX PubMed=8524256; DOI=10.1128/mcb.15.12.6895;
RA McKune K., Moore P.A., Hull M.W., Woychik N.A.;
RT "Six human RNA polymerase subunits functionally substitute for their yeast
RT counterparts.";
RL Mol. Cell. Biol. 15:6895-6900(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=7651387; DOI=10.1128/mcb.15.9.4702;
RA Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P.,
RA Vigneron M.;
RT "Four subunits that are shared by the three classes of RNA polymerase are
RT functionally interchangeable between Homo sapiens and Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 15:4702-4710(1995).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [7]
RP IDENTIFICATION IN THE RNA POL I COMPLEX, AND SUBCELLULAR LOCATION.
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 [8]
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. Pols are composed of mobile elements that move
CC relative to each other. In Pol II, POLR2L/RBP10 is part of the core
CC element with the central large cleft (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC least 13, 12 and 17 subunits, respectively. {ECO:0000250}.
CC -!- INTERACTION:
CC P62875; O95994: AGR2; NbExp=3; IntAct=EBI-359527, EBI-712648;
CC P62875; Q8N9N5: BANP; NbExp=3; IntAct=EBI-359527, EBI-744695;
CC P62875; P38432: COIL; NbExp=3; IntAct=EBI-359527, EBI-945751;
CC P62875; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-359527, EBI-19153639;
CC P62875; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-359527, EBI-2686809;
CC P62875; Q96RE7: NACC1; NbExp=3; IntAct=EBI-359527, EBI-7950997;
CC P62875; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-359527, EBI-713786;
CC P62875; O15514: POLR2D; NbExp=3; IntAct=EBI-359527, EBI-394737;
CC P62875; P60900: PSMA6; NbExp=3; IntAct=EBI-359527, EBI-357793;
CC P62875; Q04864: REL; NbExp=3; IntAct=EBI-359527, EBI-307352;
CC P62875; Q04864-2: REL; NbExp=3; IntAct=EBI-359527, EBI-10829018;
CC P62875; Q9BWH6: RPAP1; NbExp=3; IntAct=EBI-359527, EBI-1048085;
CC P62875; Q96R06: SPAG5; NbExp=3; IntAct=EBI-359527, EBI-413317;
CC P62875; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-359527, EBI-741515;
CC P62875; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-359527, EBI-10175039;
CC P62875; Q15645: TRIP13; NbExp=3; IntAct=EBI-359527, EBI-358993;
CC P62875; O43829: ZBTB14; NbExp=3; IntAct=EBI-359527, EBI-10176632;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16809778,
CC ECO:0000269|PubMed:9852112}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC polymerase subunit family. {ECO:0000305}.
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DR EMBL; U37690; AAA91459.1; -; mRNA.
DR EMBL; CR536565; CAG38802.1; -; mRNA.
DR EMBL; AK311997; BAG34935.1; -; mRNA.
DR EMBL; BC005903; AAH05903.1; -; mRNA.
DR EMBL; BC018649; AAH18649.1; -; mRNA.
DR EMBL; Z47729; CAA87658.1; -; Genomic_DNA.
DR EMBL; Z47728; CAA87657.1; -; Genomic_DNA.
DR CCDS; CCDS7720.1; -.
DR PIR; S53015; S53015.
DR RefSeq; NP_066951.1; NM_021128.4.
DR PDB; 5IY6; EM; 7.20 A; J=1-67.
DR PDB; 5IY7; EM; 8.60 A; J=1-67.
DR PDB; 5IY8; EM; 7.90 A; J=1-67.
DR PDB; 5IY9; EM; 6.30 A; J=1-67.
DR PDB; 5IYA; EM; 5.40 A; J=1-67.
DR PDB; 5IYB; EM; 3.90 A; J=1-67.
DR PDB; 5IYC; EM; 3.90 A; J=1-67.
DR PDB; 5IYD; EM; 3.90 A; J=1-67.
DR PDB; 6DRD; EM; 3.90 A; J=1-67.
DR PDB; 6O9L; EM; 7.20 A; J=1-67.
DR PDB; 6XRE; EM; 4.60 A; J=1-67.
DR PDB; 7A6H; EM; 3.30 A; J=1-67.
DR PDB; 7AE1; EM; 2.80 A; J=1-67.
DR PDB; 7AE3; EM; 3.10 A; J=1-67.
DR PDB; 7AEA; EM; 3.40 A; J=1-67.
DR PDB; 7AST; EM; 4.00 A; B=1-67.
DR PDB; 7D58; EM; 2.90 A; J=1-67.
DR PDB; 7D59; EM; 3.10 A; J=1-67.
DR PDB; 7DN3; EM; 3.50 A; J=1-67.
DR PDB; 7DU2; EM; 3.35 A; J=1-67.
DR PDB; 7FJI; EM; 3.60 A; J=1-67.
DR PDB; 7FJJ; EM; 3.60 A; J=1-67.
DR PDB; 7LBM; EM; 4.80 A; J=1-67.
DR PDB; 7OB9; EM; 2.70 A; J=1-67.
DR PDB; 7OBA; EM; 3.10 A; J=1-67.
DR PDB; 7OBB; EM; 3.30 A; J=1-67.
DR PDB; 7VBA; EM; 2.89 A; J=1-67.
DR PDB; 7VBB; EM; 2.81 A; J=1-67.
DR PDB; 7VBC; EM; 3.01 A; J=1-67.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6DRD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6XRE; -.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; P62875; -.
DR SMR; P62875; -.
DR BioGRID; 111437; 156.
DR CORUM; P62875; -.
DR DIP; DIP-32960N; -.
DR IntAct; P62875; 55.
DR MINT; P62875; -.
DR STRING; 9606.ENSP00000324124; -.
DR iPTMnet; P62875; -.
DR PhosphoSitePlus; P62875; -.
DR SwissPalm; P62875; -.
DR BioMuta; POLR2L; -.
DR DMDM; 51338657; -.
DR EPD; P62875; -.
DR jPOST; P62875; -.
DR MassIVE; P62875; -.
DR MaxQB; P62875; -.
DR PaxDb; P62875; -.
DR PeptideAtlas; P62875; -.
DR PRIDE; P62875; -.
DR ProteomicsDB; 57442; -.
DR TopDownProteomics; P62875; -.
DR Antibodypedia; 22712; 103 antibodies from 20 providers.
DR DNASU; 5441; -.
DR Ensembl; ENST00000322028.5; ENSP00000324124.4; ENSG00000177700.6.
DR Ensembl; ENST00000534030.1; ENSP00000432807.1; ENSG00000177700.6.
DR GeneID; 5441; -.
DR KEGG; hsa:5441; -.
DR MANE-Select; ENST00000322028.5; ENSP00000324124.4; NM_021128.5; NP_066951.1.
DR UCSC; uc001lsc.4; human.
DR CTD; 5441; -.
DR DisGeNET; 5441; -.
DR GeneCards; POLR2L; -.
DR HGNC; HGNC:9199; POLR2L.
DR HPA; ENSG00000177700; Low tissue specificity.
DR MIM; 601189; gene.
DR neXtProt; NX_P62875; -.
DR OpenTargets; ENSG00000177700; -.
DR PharmGKB; PA33519; -.
DR VEuPathDB; HostDB:ENSG00000177700; -.
DR eggNOG; KOG3497; Eukaryota.
DR GeneTree; ENSGT00390000007087; -.
DR HOGENOM; CLU_143122_1_1_1; -.
DR InParanoid; P62875; -.
DR OMA; YCCRRMF; -.
DR OrthoDB; 1639063at2759; -.
DR PhylomeDB; P62875; -.
DR TreeFam; TF103046; -.
DR PathwayCommons; P62875; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
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-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR SignaLink; P62875; -.
DR SIGNOR; P62875; -.
DR BioGRID-ORCS; 5441; 816 hits in 1070 CRISPR screens.
DR ChiTaRS; POLR2L; human.
DR GeneWiki; POLR2L; -.
DR GenomeRNAi; 5441; -.
DR Pharos; P62875; Tbio.
DR PRO; PR:P62875; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P62875; protein.
DR Bgee; ENSG00000177700; Expressed in apex of heart and 211 other tissues.
DR Genevisible; P62875; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; TAS:ProtInc.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central.
DR HAMAP; MF_00250; RNApol_arch_Rpo10; 1.
DR InterPro; IPR023580; RNA_pol_su_RPB10.
DR InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR InterPro; IPR000268; RPABC5/Rpb10.
DR PANTHER; PTHR23431; PTHR23431; 1.
DR Pfam; PF01194; RNA_pol_N; 1.
DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1.
DR SUPFAM; SSF46924; SSF46924; 1.
DR PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Zinc.
FT CHAIN 1..67
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC5"
FT /id="PRO_0000121333"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 67 AA; 7645 MW; 9E8A72F667FE7EC5 CRC64;
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL
NYAPLEK
