RPB1_DROME
ID RPB1_DROME Reviewed; 1887 AA.
AC P04052; Q9VYX6;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE Short=RNA polymerase II subunit B1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN Name=RpII215; ORFNames=CG1554;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2496296; DOI=10.1007/bf00339727;
RA Jokerst R.S., Weeks J.R., Zehring W.A., Greenleaf A.L.;
RT "Analysis of the gene encoding the largest subunit of RNA polymerase II in
RT Drosophila.";
RL Mol. Gen. Genet. 215:266-275(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=3025586; DOI=10.1128/mcb.6.10.3312-3319.1986;
RA Searles L.L., Greenleaf A.L., Kemp W.E., Voelker R.A.;
RT "Sites of P element insertion and structures of P element deletions in the
RT 5' region of Drosophila melanogaster RpII215.";
RL Mol. Cell. Biol. 6:3312-3319(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-472.
RX PubMed=2992806; DOI=10.1016/0092-8674(85)90118-7;
RA Biggs J., Searles L.L., Greenleaf A.L.;
RT "Structure of the eukaryotic transcription apparatus: features of the gene
RT for the largest subunit of Drosophila RNA polymerase II.";
RL Cell 42:611-621(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 778-827.
RX PubMed=8552047; DOI=10.1007/bf00287104;
RA Petersen G., Song D., Hugle-Dorr B., Oldenburg I., Bautz E.K.;
RT "Mapping of linear epitopes recognized by monoclonal antibodies with gene-
RT fragment phage display libraries.";
RL Mol. Gen. Genet. 249:425-431(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1441-1887.
RX PubMed=3122024; DOI=10.1128/mcb.8.1.321-329.1988;
RA Allison L.A., Wong J.K.-C., Fitzpatrick V.D., Moyle M., Ingles C.J.;
RT "The C-terminal domain of the largest subunit of RNA polymerase II of
RT Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved
RT structure with an essential function.";
RL Mol. Cell. Biol. 8:321-329(1988).
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 component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. It is composed of mobile elements that move
CC relative to each other. RPB1 is part of the core element with the
CC central large cleft, the clamp element that moves to open and close the
CC cleft and the jaws that are thought to grab the incoming DNA template.
CC At the start of transcription, a single-stranded DNA template strand of
CC the promoter is positioned within the central active site cleft of Pol
CC II. A bridging helix emanates from RPB1 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol II by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. During transcription elongation, Pol II moves on
CC the template as the transcript elongates. Elongation is influenced by
CC the phosphorylation status of the C-terminal domain (CTD) of Pol II
CC largest subunit (RPB1), which serves as a platform for assembly of
CC factors that regulate transcription initiation, elongation, termination
CC and mRNA processing (By similarity). {ECO:0000250}.
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 II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II.
CC Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the
CC heptapeptide repeat. The phosphorylation state is believed to result
CC from the balanced action of site-specific CTD kinases and phosphatase,
CC and a 'CTD code' that specifies the position of Pol II within the
CC transcription cycle has been proposed.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion temporarily coordinated by three conserved
CC aspartate residues of the two largest RNA Pol II subunits. The
CC ribonucleoside triphosphate is transferred by a rotation to the
CC nucleotide addition (A) site for pairing with the template DNA. The
CC catalytic A site involves three conserved aspartate residues of the RNA
CC Pol II largest subunit which permanently coordinate a second magnesium
CC ion.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; M27431; AAA28868.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48057.1; -; Genomic_DNA.
DR EMBL; M14203; AAA28864.1; -; Genomic_DNA.
DR EMBL; M11798; AAA28863.1; -; Genomic_DNA.
DR EMBL; M19537; AAA28827.1; -; Genomic_DNA.
DR PIR; S04457; RNFF2L.
DR RefSeq; NP_511124.1; NM_078569.3.
DR AlphaFoldDB; P04052; -.
DR SMR; P04052; -.
DR BioGRID; 58510; 45.
DR DIP; DIP-22282N; -.
DR IntAct; P04052; 13.
DR MINT; P04052; -.
DR STRING; 7227.FBpp0073387; -.
DR iPTMnet; P04052; -.
DR PaxDb; P04052; -.
DR PRIDE; P04052; -.
DR ABCD; P04052; 1 sequenced antibody.
DR DNASU; 32100; -.
DR EnsemblMetazoa; FBtr0073542; FBpp0073387; FBgn0003277.
DR GeneID; 32100; -.
DR KEGG; dme:Dmel_CG1554; -.
DR CTD; 32100; -.
DR FlyBase; FBgn0003277; RpII215.
DR VEuPathDB; VectorBase:FBgn0003277; -.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_000487_1_1_1; -.
DR InParanoid; P04052; -.
DR OMA; SLLHICM; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; P04052; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-6803529; FGFR2 alternative splicing.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-72086; mRNA Capping.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; P04052; -.
DR BioGRID-ORCS; 32100; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32100; -.
DR PRO; PR:P04052; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003277; Expressed in cleaving embryo and 25 other tissues.
DR ExpressionAtlas; P04052; baseline and differential.
DR Genevisible; P04052; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:FlyBase.
DR DisProt; DP01433; -.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 11.
PE 3: Inferred from homology;
KW DNA-binding; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transferase; Zinc.
FT CHAIN 1..1887
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073937"
FT REPEAT 1579..1585
FT /note="1"
FT REPEAT 1586..1592
FT /note="2; approximate"
FT REPEAT 1598..1604
FT /note="3"
FT REPEAT 1605..1611
FT /note="4"
FT REPEAT 1631..1637
FT /note="5"
FT REPEAT 1638..1644
FT /note="6"
FT REPEAT 1671..1677
FT /note="7"
FT REPEAT 1678..1684
FT /note="8"
FT REPEAT 1685..1691
FT /note="9"
FT REPEAT 1692..1698
FT /note="10"
FT REPEAT 1699..1705
FT /note="11"
FT REPEAT 1706..1712
FT /note="12"
FT REPEAT 1713..1719
FT /note="13"
FT REPEAT 1720..1726
FT /note="14"
FT REPEAT 1727..1733
FT /note="15"
FT REPEAT 1740..1746
FT /note="16"
FT REPEAT 1754..1760
FT /note="17"
FT REPEAT 1761..1767
FT /note="18"
FT REPEAT 1777..1783
FT /note="19"
FT REPEAT 1784..1790
FT /note="20"
FT REPEAT 1791..1797
FT /note="21"
FT REPEAT 1798..1804
FT /note="22"
FT REPEAT 1811..1817
FT /note="23"
FT REPEAT 1818..1824
FT /note="24; approximate"
FT REPEAT 1825..1831
FT /note="25"
FT REPEAT 1832..1838
FT /note="26"
FT REPEAT 1839..1845
FT /note="27"
FT REPEAT 1846..1852
FT /note="28"
FT REPEAT 1853..1859
FT /note="29"
FT REPEAT 1860..1866
FT /note="30"
FT REPEAT 1868..1874
FT /note="31"
FT REPEAT 1875..1881
FT /note="32"
FT REGION 156..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..837
FT /note="Bridging helix"
FT REGION 1528..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1881
FT /note="C-terminal domain (CTD); 32 X 7 AA approximate
FT tandem repeats of Y-[ST]-P-[STNVAPGN]-[STGMA]-[PSTR]-
FT [SNAGCQKTLRIMH]"
FT COMPBIAS 1530..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 319..324
FT /note="RAMQKS -> GYAKV (in Ref. 5; AAA28863)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="F -> G (in Ref. 5; AAA28863)"
FT /evidence="ECO:0000305"
FT CONFLICT 455..458
FT /note="TLHK -> RCTT (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..472
FT /note="GHRVKVLPWS -> VTGESVASST (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="R -> H (in Ref. 1; AAA28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1485..1524
FT /note="SMLGGAAMFIGGGSTPSMTPPMTPWANCNTPRYFSPPGHV -> I (in
FT Ref. 7; AAA28827)"
FT /evidence="ECO:0000305"
FT CONFLICT 1506..1508
FT /note="MTP -> ELDSA (in Ref. 1; AAA28868)"
FT /evidence="ECO:0000305"
FT CONFLICT 1887
FT /note="D -> DVRKGGRG (in Ref. 1; AAA28868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1887 AA; 209168 MW; 4EC68C7708A167A3 CRC64;
MSTPTDSKAP LRQVKRVQFG ILSPDEIRRM SVTEGGVQFA ETMEGGRPKL GGLMDPRQGV
IDRTSRCQTC AGNMTECPGH FGHIDLAKPV FHIGFITKTI KILRCVCFYC SKMLVSPHNP
KIKEIVMKSR GQPRKRLAYV YDLCKGKTIC EGGEDMDLTK ENQQPDPNKK PGHGGCGHYQ
PSIRRTGLDL TAEWKHQNED SQEKKIVVSA ERVWEILKHI TDEECFILGM DPKYARPDWM
IVTVLPVPPL AVRPAVVMFG AAKNQDDLTH KLSDIIKANN ELRKNEASGA AAHVIQENIK
MLQFHVATLV DNDMPGMPRA MQKSGKPLKA IKARLKGKEG RIRGNLMGKR VDFSARTVIT
PDPNLRIDQV GVPRSIAQNL TFPELVTPFN IDRMQELVRR GNSQYPGAKY IVRDNGERID
LRFHPKSSDL HLQCGYKVER HLRDDDLVIF NRQPTLHKMS MMGHRVKVLP WSTFRMNLSC
TSPYNADFDG DEMNLHVPQS METRAEVENI HITPRQIITP QANKPVMGIV QDTLTAVRKM
TKRDVFITRE QVMNLLMFLP TWDAKMPQPC ILKPRPLWTG KQIFSLIIPG NVNMIRTHST
HPDEEDEGPY KWISPGDTKV MVEHGELIMG ILCKKSLGTS AGSLLHICFL ELGHDIAGRF
YGNIQTVINN WLLFEGHSIG IGDTIADPQT YNEIQQAIKK AKDDVINVIQ KAHNMELEPT
PGNTLRQTFE NKVNRILNDA RDKTGGSAKK SLTEYNNLKA MVVSGSKGSN INISQVIACV
GQQNVEGKRI PYGFRKRTLP HFIKDDYGPE SRGFVENSYL AGLTPSEFYF HAMGGREGLI
DTAVKTAETG YIQRRLIKAM ESVMVNYDGT VRNSVGQLIQ LRYGEDGLCG ELVEFQNMPT
VKLSNKSFEK RFKFDWSNER LMKKVFTDDV IKEMTDSSEA IQELEAEWDR LVSDRDSLRQ
IFPNGESKVV LPCNLQRMIW NVQKIFHINK RLPTDLSPIR VIKGVKTLLE RCVIVTGNDR
ISKQANENAT LLFQCLIRST LCTKYVSEEF RLSTEAFEWL VGEIETRFQQ AQANPGEMVG
ALAAQSLGEP ATQMTLNTFH FAGVSSKNVT LGVPRLKEII NISKKPKAPS LTVFLTGGAA
RDAEKAKNVL CRLEHTTLRK VTANTAIYYD PDPQRTVISE DQEFVNVYYE MPDFDPTRIS
PWLLRIELDR KRMTDKKLTM EQIAEKINVG FGEDLNCIFN DDNADKLVLR IRIMNNEENK
FQDEDEAVDK MEDDMFLRCI EANMLSDMTL QGIEAIGKVY MHLPQTDSKK RIVITETGEF
KAIGEWLLET DGTSMMKVLS ERDVDPIRTS SNDICEIFQV LGIEAVRKSV EKEMNAVLQF
YGLYVNYRHL ALLCDVMTAK GHLMAITRHG INRQDTGALM RCSFEETVDV LMDAAAHAET
DPMRGVSENI IMGQLPKMGT GCFDLLLDAE KCRFGIEIPN TLGNSMLGGA AMFIGGGSTP
SMTPPMTPWA NCNTPRYFSP PGHVSAMTPG GPSFSPSAAS DASGMSPSWS PAHPGSSPSS
PGPSMSPYFP ASPSVSPSYS PTSPNYTASS PGGASPNYSP SSPNYSPTSP LYASPRYAST
TPNFNPQSTG YSPSSSGYSP TSPVYSPTVQ FQSSPSFAGS GSNIYSPGNA YSPSSSNYSP
NSPSYSPTSP SYSPSSPSYS PTSPCYSPTS PSYSPTSPNY TPVTPSYSPT SPNYSASPQY
SPASPAYSQT GVKYSPTSPT YSPPSPSYDG SPGSPQYTPG SPQYSPASPK YSPTSPLYSP
SSPQHSPSNQ YSPTGSTYSA TSPRYSPNMS IYSPSSTKYS PTSPTYTPTA RNYSPTSPMY
SPTAPSHYSP TSPAYSPSSP TFEESED
