VATB_YEAST
ID VATB_YEAST Reviewed; 517 AA.
AC P16140; D6VQC4; P32123;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=V-type proton ATPase subunit B;
DE Short=V-ATPase subunit B;
DE AltName: Full=V-ATPase 57 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit B;
GN Name=VMA2; Synonyms=VAT2; OrderedLocusNames=YBR127C; ORFNames=YBR1002;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2521486; DOI=10.1016/s0021-9258(18)94254-7;
RA Nelson H., Mandiyan S., Nelson N.;
RT "A conserved gene encoding the 57-kDa subunit of the yeast vacuolar H+-
RT ATPase.";
RL J. Biol. Chem. 264:1775-1778(1989).
RN [2]
RP ERRATUM OF PUBMED:2521486, AND SEQUENCE REVISION.
RA Nelson H., Mandiyan S., Nelson N.;
RL J. Biol. Chem. 264:5313-5313(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-517.
RX PubMed=1371275; DOI=10.1016/s0021-9258(19)50581-6;
RA Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M.;
RT "Differential expression of the 'B' subunit of the vacuolar H(+)-ATPase in
RT bovine tissues.";
RL J. Biol. Chem. 267:3696-3706(1992).
RN [8]
RP PROTEIN SEQUENCE OF 13-28, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2141385; DOI=10.1128/mcb.10.7.3737-3749.1990;
RA Yamashiro C.T., Kane P.M., Wolczyk D.F., Preston R.A., Stevens T.H.;
RT "Role of vacuolar acidification in protein sorting and zymogen activation:
RT a genetic analysis of the yeast vacuolar proton-translocating ATPase.";
RL Mol. Cell. Biol. 10:3737-3749(1990).
RN [9]
RP INTERACTION WITH RAV1 AND RAV2.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP IDENTIFICATION IN THE V-ATPASE COMPLEX, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RX PubMed=18055462; DOI=10.1074/jbc.m707924200;
RA Kitagawa N., Mazon H., Heck A.J.R., Wilkens S.;
RT "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase
RT determined by mass spectrometry.";
RL J. Biol. Chem. 283:3329-3337(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-137; SER-503 AND
RP SER-504, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-511 AND SER-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-508, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [18] {ECO:0007744|PDB:3J9T, ECO:0007744|PDB:3J9U, ECO:0007744|PDB:3J9V}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
RX PubMed=25971514; DOI=10.1038/nature14365;
RA Zhao J., Benlekbir S., Rubinstein J.L.;
RT "Electron cryomicroscopy observation of rotational states in a eukaryotic
RT V-ATPase.";
RL Nature 521:241-245(2015).
RN [19] {ECO:0007744|PDB:5BW9, ECO:0007744|PDB:5D80}
RP X-RAY CRYSTALLOGRAPHY (6.20 ANGSTROMS), AND IDENTIFICATION IN THE V-ATPASE
RP COMPLEX.
RX PubMed=27295975; DOI=10.15252/embj.201593447;
RA Oot R.A., Kane P.M., Berry E.A., Wilkens S.;
RT "Crystal structure of yeast V1-ATPase in the autoinhibited state.";
RL EMBO J. 35:1694-1706(2016).
CC -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC that translocates protons (PubMed:2141385). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments
CC (PubMed:2141385). {ECO:0000269|PubMed:2141385}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1) (PubMed:25971514, PubMed:18055462, PubMed:27295975). Interacts
CC with RAV1 and RAV2 components of the RAVE complex, which are essential
CC for the stability and assembly of V-ATPase (PubMed:11283612).
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:18055462,
CC ECO:0000269|PubMed:25971514, ECO:0000269|PubMed:27295975}.
CC -!- INTERACTION:
CC P16140; P47104: RAV1; NbExp=3; IntAct=EBI-20254, EBI-25471;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:2141385};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=57630.5; Mass_error=32.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18055462};
CC -!- MISCELLANEOUS: Present with 131000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:1371275 sequence was incorrectly thought to originate
CC from bovine. {ECO:0000305}.
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DR EMBL; J04450; AAA66890.1; -; Genomic_DNA.
DR EMBL; X75891; CAA53486.1; -; Genomic_DNA.
DR EMBL; Z35996; CAA85084.1; -; Genomic_DNA.
DR EMBL; AY693158; AAT93177.1; -; Genomic_DNA.
DR EMBL; M83130; AAA30389.1; -; mRNA.
DR EMBL; BK006936; DAA07244.1; -; Genomic_DNA.
DR PIR; B42254; B42254.
DR PIR; S45996; S45996.
DR RefSeq; NP_009685.3; NM_001178475.3.
DR PDB; 3J9T; EM; 6.90 A; B/D/F=1-517.
DR PDB; 3J9U; EM; 7.60 A; B/D/F=1-517.
DR PDB; 3J9V; EM; 8.30 A; B/D/F=1-517.
DR PDB; 5BW9; X-ray; 7.00 A; D/E/F/d/e/f=1-517.
DR PDB; 5D80; X-ray; 6.20 A; D/E/F/d/e/f=1-517.
DR PDB; 5VOX; EM; 6.80 A; B/D/F=1-517.
DR PDB; 5VOY; EM; 7.90 A; B/D/F=1-517.
DR PDB; 5VOZ; EM; 7.60 A; B/D/F=1-517.
DR PDB; 6O7V; EM; 6.60 A; B/D/F=1-517.
DR PDB; 6O7W; EM; 7.00 A; B/D/F=1-517.
DR PDB; 6O7X; EM; 8.70 A; B/D/F=1-517.
DR PDB; 7FDA; EM; 4.20 A; B/D/F=1-517.
DR PDB; 7FDB; EM; 4.80 A; B/D/F=1-517.
DR PDB; 7FDC; EM; 6.60 A; B/D/F=1-517.
DR PDB; 7FDE; EM; 3.80 A; B/D/F=1-517.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
DR PDBsum; 5BW9; -.
DR PDBsum; 5D80; -.
DR PDBsum; 5VOX; -.
DR PDBsum; 5VOY; -.
DR PDBsum; 5VOZ; -.
DR PDBsum; 6O7V; -.
DR PDBsum; 6O7W; -.
DR PDBsum; 6O7X; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR PDBsum; 7FDE; -.
DR AlphaFoldDB; P16140; -.
DR SMR; P16140; -.
DR BioGRID; 32828; 222.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR DIP; DIP-2292N; -.
DR IntAct; P16140; 610.
DR MINT; P16140; -.
DR STRING; 4932.YBR127C; -.
DR ChEMBL; CHEMBL6106; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P16140; -.
DR MaxQB; P16140; -.
DR PaxDb; P16140; -.
DR PRIDE; P16140; -.
DR EnsemblFungi; YBR127C_mRNA; YBR127C; YBR127C.
DR GeneID; 852424; -.
DR KEGG; sce:YBR127C; -.
DR SGD; S000000331; VMA2.
DR VEuPathDB; FungiDB:YBR127C; -.
DR eggNOG; KOG1351; Eukaryota.
DR GeneTree; ENSGT00960000189262; -.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; P16140; -.
DR OMA; GFKIKPR; -.
DR BioCyc; YEAST:G3O-29082-MON; -.
DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SCE-77387; Insulin receptor recycling.
DR Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P16140; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P16140; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:SGD.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0000425; P:pexophagy; IMP:SGD.
DR GO; GO:1902906; P:proteasome storage granule assembly; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Isopeptide bond; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transport;
KW Ubl conjugation; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18055462"
FT CHAIN 2..517
FT /note="V-type proton ATPase subunit B"
FT /id="PRO_0000144648"
FT REGION 487..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P21281"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 511
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 14
FT /note="K -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> L (in Ref. 1; AAA66890)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Q -> R (in Ref. 7; AAA30389)"
FT /evidence="ECO:0000305"
FT CONFLICT 500..517
FT /note="DTRSSGKKKDASQEESLI -> TQEAPVRRRTPAKKNL (in Ref. 1;
FT AAA66890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 57749 MW; 02A7DEC571EFF7C2 CRC64;
MVLSDKELFA INKKAVEQGF NVKPRLNYNT VSGVNGPLVI LEKVKFPRYN EIVNLTLPDG
TVRQGQVLEI RGDRAIVQVF EGTSGIDVKK TTVEFTGESL RIPVSEDMLG RIFDGSGRPI
DNGPKVFAED YLDINGSPIN PYARIYPEEM ISTGVSAIDT MNSIARGQKI PIFSASGLPH
NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL
FLNLANDPTI ERIITPRLAL TTAEYLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQIFV
DRQLHNKGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG KDAAAMKAVV
GEEALSIEDK LSLEFLEKFE KTFITQGAYE DRTVFESLDQ AWSLLRIYPK EMLNRISPKI
LDEFYDRARD DADEDEEDPD TRSSGKKKDA SQEESLI
