RPOM_HUMAN
ID RPOM_HUMAN Reviewed; 1230 AA.
AC O00411; O60370;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=DNA-directed RNA polymerase, mitochondrial {ECO:0000305};
DE Short=MtRPOL;
DE EC=2.7.7.6;
DE Flags: Precursor;
GN Name=POLRMT {ECO:0000312|HGNC:HGNC:9200};
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].
RC TISSUE=Liver;
RX PubMed=9097968; DOI=10.1093/hmg/6.4.615;
RA Tiranti V., Savoia A., Forti F., D'Apolito M.F., Centra M., Rocchi M.,
RA Zeviani M.;
RT "Identification of the gene encoding the human mitochondrial RNA polymerase
RT (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database.";
RL Hum. Mol. Genet. 6:615-625(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP INTERACTION WITH TFB1M AND TFB2M.
RX PubMed=12068295; DOI=10.1038/ng909;
RA Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA Gustafsson C.M.;
RT "Mitochondrial transcription factors B1 and B2 activate transcription of
RT human mtDNA.";
RL Nat. Genet. 31:289-294(2002).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH TEFM.
RX PubMed=21278163; DOI=10.1093/nar/gkq1224;
RA Minczuk M., He J., Duch A.M., Ettema T.J., Chlebowski A., Dzionek K.,
RA Nijtmans L.G., Huynen M.A., Holt I.J.;
RT "TEFM (c17orf42) is necessary for transcription of human mtDNA.";
RL Nucleic Acids Res. 39:4284-4299(2011).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH SIRT3 AND FOXO3, AND SUBCELLULAR LOCATION.
RX PubMed=23283301; DOI=10.1007/s00018-012-1244-6;
RA Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D.,
RA Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G.,
RA Puri P.L., Sartorelli V., Simone C.;
RT "A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing
RT glucose levels.";
RL Cell. Mol. Life Sci. 70:2015-2029(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND FOXO3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29445193; DOI=10.1038/s41419-018-0336-0;
RA Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G.,
RA Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A.,
RA Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G.,
RA Moschetta A., Grossi V., Simone C.;
RT "Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells
RT undergoing metabolic stress and chemotherapy.";
RL Cell Death Dis. 9:231-231(2018).
RN [9]
RP INTERACTION WITH MTRES1.
RX PubMed=31226201; DOI=10.1093/nar/gkz542;
RA Kotrys A.V., Cysewski D., Czarnomska S.D., Pietras Z., Borowski L.S.,
RA Dziembowski A., Szczesny R.J.;
RT "Quantitative proteomics revealed C6orf203/MTRES1 as a factor preventing
RT stress-induced transcription deficiency in human mitochondria.";
RL Nucleic Acids Res. 47:7502-7517(2019).
RN [10] {ECO:0007744|PDB:6ERP, ECO:0007744|PDB:6ERQ}
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 43-245 IN COMPLEX WITH TFAM;
RP TFB2M AND DNA, AND SUBUNIT.
RX PubMed=29149603; DOI=10.1016/j.cell.2017.10.036;
RA Hillen H.S., Morozov Y.I., Sarfallah A., Temiakov D., Cramer P.;
RT "Structural Basis of Mitochondrial Transcription Initiation.";
RL Cell 171:1072-1081.e10(2017).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC mitochondrial DNA into RNA using the four ribonucleoside triphosphates
CC as substrates (PubMed:21278163). Component of the mitochondrial
CC transcription initiation complex, composed at least of TFB2M, TFAM and
CC POLRMT that is required for basal transcription of mitochondrial DNA
CC (PubMed:29149603). In this complex, TFAM recruits POLRMT to a specific
CC promoter whereas TFB2M induces structural changes in POLRMT to enable
CC promoter opening and trapping of the DNA non-template strand
CC (PubMed:29149603). {ECO:0000269|PubMed:21278163,
CC ECO:0000269|PubMed:29149603}.
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031,
CC ECO:0000255|PROSITE-ProRule:PRU10032};
CC -!- SUBUNIT: Homodimer (PubMed:29149603). Component of the mitochondrial
CC transcription initiation complex, composed at least of TFB2M, TFAM and
CC POLRMT (PubMed:29149603). In this complex TFAM recruits POLRMT to the
CC promoter whereas TFB2M induces structural changes in POLRMT to enable
CC promoter opening and trapping of the DNA non-template strand
CC (PubMed:29149603). Upon metabolic stress, forms a complex composed of
CC FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is
CC recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also
CC forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT
CC (PubMed:29445193). Interacts with TFB1M and TFB2M, leading to the
CC stimulation of transcription (PubMed:12068295). Interacts with TEFM
CC (PubMed:21278163). Interacts with MTRES1 (PubMed:31226201).
CC {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:21278163,
CC ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29149603,
CC ECO:0000269|PubMed:29445193, ECO:0000269|PubMed:31226201}.
CC -!- INTERACTION:
CC O00411; P52815: MRPL12; NbExp=5; IntAct=EBI-355145, EBI-358272;
CC O00411; Q96QE5: TEFM; NbExp=6; IntAct=EBI-355145, EBI-725550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301,
CC ECO:0000269|PubMed:29445193}.
CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; U75370; AAB58255.1; -; mRNA.
DR EMBL; AC004449; AAC06147.1; -; Genomic_DNA.
DR CCDS; CCDS12036.1; -.
DR RefSeq; NP_005026.3; NM_005035.3.
DR PDB; 3SPA; X-ray; 2.50 A; A=105-1230.
DR PDB; 4BOC; X-ray; 2.65 A; A=151-1230.
DR PDB; 5OLA; X-ray; 3.90 A; E/F=151-1230.
DR PDB; 6ERP; X-ray; 4.50 A; A/B=105-1230.
DR PDB; 6ERQ; X-ray; 4.50 A; A/B=105-1230.
DR PDB; 7A8P; EM; 3.50 A; A=105-1230.
DR PDBsum; 3SPA; -.
DR PDBsum; 4BOC; -.
DR PDBsum; 5OLA; -.
DR PDBsum; 6ERP; -.
DR PDBsum; 6ERQ; -.
DR PDBsum; 7A8P; -.
DR AlphaFoldDB; O00411; -.
DR SMR; O00411; -.
DR BioGRID; 111438; 199.
DR ComplexPortal; CPX-7241; Mitochondrial transcription initiation complex.
DR DIP; DIP-56412N; -.
DR IntAct; O00411; 60.
DR MINT; O00411; -.
DR STRING; 9606.ENSP00000465759; -.
DR BindingDB; O00411; -.
DR ChEMBL; CHEMBL3120041; -.
DR iPTMnet; O00411; -.
DR MetOSite; O00411; -.
DR PhosphoSitePlus; O00411; -.
DR BioMuta; POLRMT; -.
DR EPD; O00411; -.
DR jPOST; O00411; -.
DR MassIVE; O00411; -.
DR MaxQB; O00411; -.
DR PaxDb; O00411; -.
DR PeptideAtlas; O00411; -.
DR PRIDE; O00411; -.
DR ProteomicsDB; 47875; -.
DR Antibodypedia; 1270; 110 antibodies from 29 providers.
DR DNASU; 5442; -.
DR Ensembl; ENST00000588649.7; ENSP00000465759.2; ENSG00000099821.14.
DR GeneID; 5442; -.
DR KEGG; hsa:5442; -.
DR MANE-Select; ENST00000588649.7; ENSP00000465759.2; NM_005035.4; NP_005026.3.
DR UCSC; uc002lpf.2; human.
DR CTD; 5442; -.
DR DisGeNET; 5442; -.
DR GeneCards; POLRMT; -.
DR HGNC; HGNC:9200; POLRMT.
DR HPA; ENSG00000099821; Low tissue specificity.
DR MIM; 601778; gene.
DR neXtProt; NX_O00411; -.
DR OpenTargets; ENSG00000099821; -.
DR PharmGKB; PA33522; -.
DR VEuPathDB; HostDB:ENSG00000099821; -.
DR eggNOG; KOG1038; Eukaryota.
DR GeneTree; ENSGT00390000008060; -.
DR HOGENOM; CLU_003364_2_1_1; -.
DR InParanoid; O00411; -.
DR OMA; YAEEIMP; -.
DR OrthoDB; 135329at2759; -.
DR PhylomeDB; O00411; -.
DR TreeFam; TF105700; -.
DR BRENDA; 2.7.7.6; 2681.
DR PathwayCommons; O00411; -.
DR Reactome; R-HSA-163282; Mitochondrial transcription initiation.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; O00411; -.
DR BioGRID-ORCS; 5442; 446 hits in 1084 CRISPR screens.
DR ChiTaRS; POLRMT; human.
DR GeneWiki; POLRMT; -.
DR GenomeRNAi; 5442; -.
DR Pharos; O00411; Tbio.
DR PRO; PR:O00411; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00411; protein.
DR Bgee; ENSG00000099821; Expressed in left testis and 163 other tissues.
DR ExpressionAtlas; O00411; baseline and differential.
DR Genevisible; O00411; HS.
DR GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; IDA:UniProtKB.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IDA:ComplexPortal.
DR DisProt; DP02703; -.
DR Gene3D; 1.10.1320.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR037159; RNA_POL_N_sf.
DR InterPro; IPR029262; RPOL_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10102; PTHR10102; 1.
DR Pfam; PF00940; RNA_pol; 1.
DR Pfam; PF14700; RPOL_N; 1.
DR SMART; SM01311; RPOL_N; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Mitochondrion;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..1230
FT /note="DNA-directed RNA polymerase, mitochondrial"
FT /id="PRO_0000031068"
FT REGION 18..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..1230
FT /note="Mediates interaction with TEFM"
FT /evidence="ECO:0000269|PubMed:21278163"
FT COMPBIAS 732..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 922
FT /evidence="ECO:0000250"
FT ACT_SITE 991
FT /evidence="ECO:0000250"
FT ACT_SITE 1151
FT /evidence="ECO:0000250"
FT VARIANT 555
FT /note="E -> A (in dbSNP:rs2238549)"
FT /id="VAR_019427"
FT CONFLICT 399
FT /note="L -> F (in Ref. 1; AAB58255)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="G -> S (in Ref. 1; AAB58255)"
FT /evidence="ECO:0000305"
FT HELIX 221..236
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3SPA"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4BOC"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:7A8P"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7A8P"
FT HELIX 427..461
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 476..489
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 497..519
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 522..533
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:7A8P"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 569..586
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:4BOC"
FT STRAND 604..610
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:4BOC"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 625..634
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 677..685
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 693..703
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 711..721
FT /evidence="ECO:0007829|PDB:3SPA"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:4BOC"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:4BOC"
FT HELIX 772..789
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:7A8P"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 806..809
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 819..823
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 825..829
FT /evidence="ECO:0007829|PDB:3SPA"
FT TURN 834..836
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 837..849
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 853..855
FT /evidence="ECO:0007829|PDB:7A8P"
FT HELIX 857..876
FT /evidence="ECO:0007829|PDB:3SPA"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 884..887
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 891..905
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 907..909
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 910..912
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:7A8P"
FT STRAND 918..922
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 926..934
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 938..943
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 955..972
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 976..980
FT /evidence="ECO:0007829|PDB:3SPA"
FT TURN 981..983
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 987..999
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1002..1004
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1005..1015
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1018..1020
FT /evidence="ECO:0007829|PDB:4BOC"
FT TURN 1022..1024
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1025..1043
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1045..1063
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1073..1075
FT /evidence="ECO:0007829|PDB:7A8P"
FT STRAND 1077..1079
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1112..1141
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1147..1149
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1152..1156
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1157..1159
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1160..1176
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1179..1191
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1198..1209
FT /evidence="ECO:0007829|PDB:3SPA"
FT HELIX 1219..1224
FT /evidence="ECO:0007829|PDB:3SPA"
FT STRAND 1228..1230
FT /evidence="ECO:0007829|PDB:4BOC"
SQ SEQUENCE 1230 AA; 138620 MW; 47AFBF2E0884AEFA CRC64;
MSALCWGRGA AGLKRALRPC GRPGLPGKEG TAGGVCGPRR SSSASPQEQD QDRRKDWGHV
ELLEVLQARV RQLQAESVSE VVVNRVDVAR LPECGSGDGS LQPPRKVQMG AKDATPVPCG
RWAKILEKDK RTQQMRMQRL KAKLQMPFQS GEFKALTRRL QVEPRLLSKQ MAGCLEDCTR
QAPESPWEEQ LARLLQEAPG KLSLDVEQAP SGQHSQAQLS GQQQRLLAFF KCCLLTDQLP
LAHHLLVVHH GQRQKRKLLT LDMYNAVMLG WARQGAFKEL VYVLFMVKDA GLTPDLLSYA
AALQCMGRQD QDAGTIERCL EQMSQEGLKL QALFTAVLLS EEDRATVLKA VHKVKPTFSL
PPQLPPPVNT SKLLRDVYAK DGRVSYPKLH LPLKTLQCLF EKQLHMELAS RVCVVSVEKP
TLPSKEVKHA RKTLKTLRDQ WEKALCRALR ETKNRLEREV YEGRFSLYPF LCLLDEREVV
RMLLQVLQAL PAQGESFTTL ARELSARTFS RHVVQRQRVS GQVQALQNHY RKYLCLLASD
AEVPEPCLPR QYWEELGAPE ALREQPWPLP VQMELGKLLA EMLVQATQMP CSLDKPHRSS
RLVPVLYHVY SFRNVQQIGI LKPHPAYVQL LEKAAEPTLT FEAVDVPMLC PPLPWTSPHS
GAFLLSPTKL MRTVEGATQH QELLETCPPT ALHGALDALT QLGNCAWRVN GRVLDLVLQL
FQAKGCPQLG VPAPPSEAPQ PPEAHLPHSA APARKAELRR ELAHCQKVAR EMHSLRAEAL
YRLSLAQHLR DRVFWLPHNM DFRGRTYPCP PHFNHLGSDV ARALLEFAQG RPLGPHGLDW
LKIHLVNLTG LKKREPLRKR LAFAEEVMDD ILDSADQPLT GRKWWMGAEE PWQTLACCME
VANAVRASDP AAYVSHLPVH QDGSCNGLQH YAALGRDSVG AASVNLEPSD VPQDVYSGVA
AQVEVFRRQD AQRGMRVAQV LEGFITRKVV KQTVMTVVYG VTRYGGRLQI EKRLRELSDF
PQEFVWEASH YLVRQVFKSL QEMFSGTRAI QHWLTESARL ISHMGSVVEW VTPLGVPVIQ
PYRLDSKVKQ IGGGIQSITY THNGDISRKP NTRKQKNGFP PNFIHSLDSS HMMLTALHCY
RKGLTFVSVH DCYWTHAADV SVMNQVCREQ FVRLHSEPIL QDLSRFLVKR FCSEPQKILE
ASQLKETLQA VPKPGAFDLE QVKRSTYFFS
