ATPB_RAT
ID ATPB_RAT Reviewed; 529 AA.
AC P10719; Q499W0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE EC=7.1.2.2;
DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000312|RGD:621368};
DE Flags: Precursor;
GN Name=Atp5f1b {ECO:0000312|RGD:621368}; Synonyms=Atp5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RX PubMed=2522775; DOI=10.1016/0006-291x(89)92235-3;
RA Boulet D., Poirier J., Cote C.;
RT "Studies on the biogenesis of the mammalian ATP synthase complex: isolation
RT and characterization of a full-length cDNA encoding the rat F1-beta-
RT subunit.";
RL Biochem. Biophys. Res. Commun. 159:1184-1190(1989).
RN [3]
RP PROTEIN SEQUENCE OF 47-60.
RC TISSUE=Liver;
RX PubMed=2531579; DOI=10.1016/0006-291x(89)91791-9;
RA Cretin F., Baggetto L.G., Denoroy L., Godinot C.;
RT "N-terminal sequence of the rat liver beta-subunit in the mitochondrial
RT ATPase-ATPsynthase.";
RL Biochem. Biophys. Res. Commun. 164:1165-1169(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-529.
RX PubMed=2894849; DOI=10.1021/bi00402a008;
RA Garboczi D.N., Fox A.H., Gerring S.L., Pedersen P.L.;
RT "Beta subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino
RT acid sequence, expression in Escherichia coli, and structural relationship
RT to adenylate kinase.";
RL Biochemistry 27:553-560(1988).
RN [5]
RP PROTEIN SEQUENCE OF 87-98; 208-219; 225-234; 268-279 AND 433-454, AND
RP CALCIUM-BINDING.
RX PubMed=8764999; DOI=10.1016/0014-5793(96)00767-3;
RA Hubbard M.J., McHugh N.J.;
RT "Mitochondrial ATP synthase F1-beta-subunit is a calcium-binding protein.";
RL FEBS Lett. 391:323-329(1996).
RN [6]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 226-239; 242-259;
RP 265-279; 282-345; 388-422; 427-456 AND 463-480, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-529.
RX PubMed=2907347;
RA Lee Y.M., Chu L.P., Lee S.C.;
RT "Molecular cloning of cDNA for the rat F1-ATPase beta subunit.";
RL Taiwan Yi Xue Hui Za Zhi 87:933-938(1988).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pancreatic acinar cell;
RX PubMed=14673794; DOI=10.1002/pmic.200300585;
RA Yu J.-H., Yun S.-Y., Lim J.-W., Kim H., Kim K.-H.;
RT "Mass spectrometry and tandem mass spectrometry analysis of rat
RT mitochondrial ATP synthase: up-regulation in pancreatic acinar cells
RT treated with cerulein.";
RL Proteomics 3:2437-2445(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
RN [10]
RP INTERACTION WITH BCL2L1.
RX PubMed=21926988; DOI=10.1038/ncb2330;
RA Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S.,
RA Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M.,
RA Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J., Hardwick J.M.,
RA Jonas E.A.;
RT "Bcl-xL regulates metabolic efficiency of neurons through interaction with
RT the mitochondrial F1FO ATP synthase.";
RL Nat. Cell Biol. 13:1224-1233(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP GLYCOSYLATION AT SER-106.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=9736690; DOI=10.1073/pnas.95.19.11065;
RA Bianchet M.A., Hullihen J., Pedersen P.L., Amzel L.M.;
RT "The 2.8-A structure of rat liver F1-ATPase: configuration of a critical
RT intermediate in ATP synthesis/hydrolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11065-11070(1998).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (PubMed:17575325). Interacts with PPIF (By similarity).
CC Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the
CC association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane
CC F(1)F(0) ATP synthase and enhances neurons metabolic efficiency
CC (PubMed:21926988). Interacts with CLN5 and PPT1 (By similarity).
CC Interacts with S100A1; this interaction increases F1-ATPase activity
CC (By similarity). Interacts with MTLN (By similarity). Interacts with
CC TTC5/STRAP; the interaction results in decreased mitochondrial ATP
CC production (By similarity). {ECO:0000250|UniProtKB:P00829,
CC ECO:0000250|UniProtKB:P06576, ECO:0000250|UniProtKB:P56480,
CC ECO:0000269|PubMed:17575325, ECO:0000269|PubMed:21926988}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00829}; Matrix side
CC {ECO:0000250|UniProtKB:P00829}.
CC -!- MISCELLANEOUS: Binds calcium ions.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; BC099743; AAH99743.1; -; mRNA.
DR EMBL; M25301; AAA57154.1; -; mRNA.
DR EMBL; M19044; AAB02288.1; ALT_SEQ; mRNA.
DR EMBL; M57634; AAA40778.1; -; mRNA.
DR PIR; A28701; A28701.
DR PIR; A30160; A30160.
DR RefSeq; NP_599191.1; NM_134364.1.
DR PDB; 1MAB; X-ray; 2.80 A; B=51-529.
DR PDB; 2F43; X-ray; 3.00 A; B=51-529.
DR PDBsum; 1MAB; -.
DR PDBsum; 2F43; -.
DR AlphaFoldDB; P10719; -.
DR SMR; P10719; -.
DR BioGRID; 251212; 9.
DR CORUM; P10719; -.
DR IntAct; P10719; 11.
DR MINT; P10719; -.
DR STRING; 10116.ENSRNOP00000003965; -.
DR ChEMBL; CHEMBL2176796; -.
DR CarbonylDB; P10719; -.
DR GlyGen; P10719; 1 site.
DR iPTMnet; P10719; -.
DR PhosphoSitePlus; P10719; -.
DR UCD-2DPAGE; P10719; -.
DR World-2DPAGE; 0004:P10719; -.
DR jPOST; P10719; -.
DR PaxDb; P10719; -.
DR PRIDE; P10719; -.
DR GeneID; 171374; -.
DR KEGG; rno:171374; -.
DR UCSC; RGD:621368; rat.
DR CTD; 506; -.
DR RGD; 621368; Atp5f1b.
DR eggNOG; KOG1350; Eukaryota.
DR InParanoid; P10719; -.
DR OrthoDB; 495235at2759; -.
DR PhylomeDB; P10719; -.
DR BRENDA; 7.1.2.2; 5301.
DR Reactome; R-RNO-1268020; Mitochondrial protein import.
DR Reactome; R-RNO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-RNO-8949613; Cristae formation.
DR EvolutionaryTrace; P10719; -.
DR PRO; PR:P10719; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:CAFA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; ISO:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0043532; F:angiostatin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0030228; F:lipoprotein particle receptor activity; IDA:RGD.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:RGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0009631; P:cold acclimation; IEP:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; ISO:RGD.
DR GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
DR GO; GO:1904643; P:response to curcumin; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; ATP-binding; CF(1);
KW Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide;
KW Translocase; Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2531579"
FT CHAIN 47..529
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002445"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 106
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT CONFLICT 257..258
FT /note="NL -> KV (in Ref. 7; AAA40778)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..430
FT /note="QD -> HV (in Ref. 7; AAA40778)"
FT /evidence="ECO:0000305"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2F43"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2F43"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 276..294
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:2F43"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2F43"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 410..414
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 415..434
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 435..439
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 448..464
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1MAB"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:2F43"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:1MAB"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:1MAB"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:2F43"
SQ SEQUENCE 529 AA; 56354 MW; 9753BFBDBCD30E0F CRC64;
MLSLVGRVAS ASASGALRGL NPLAALPQAH LLLRTAPAGV HPARDYAAQS SAAPKAGTAT
GQIVAVIGAV VDVQFDEGLP PILNALEVQG RESRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
LVPLKETIKG FQQILAGDYD HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
