ID ACACB_HUMAN Reviewed; 2458 AA.
AC O00763; A6NK36; Q16852; Q1HEC1; Q6KE87; Q6KE89; Q6TY48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 01-MAY-2013, entry version 131.
DE RecName: Full=Acetyl-CoA carboxylase 2;
DE EC=6.4.1.2;
DE AltName: Full=ACC-beta;
DE Includes:
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14;
GN Name=ACACB; Synonyms=ACC2, ACCB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9099716; DOI=10.1074/jbc.272.16.10669;
RA Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J.;
RT "Human acetyl-CoA carboxylase 2. Molecular cloning, characterization,
RT chromosomal mapping, and evidence for two isoforms.";
RL J. Biol. Chem. 272:10669-10677(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND VARIANT
RP ILE-2141.
RX PubMed=16854592; DOI=10.1016/j.pep.2006.06.005;
RA Cheng D., Chu C.-H., Chen L., Feder J.N., Mintier G.A., Wu Y.,
RA Cook J.W., Harpel M.R., Locke G.A., An Y., Tamura J.K.;
RT "Expression, purification, and characterization of human and rat
RT acetyl coenzyme A carboxylase (ACC) isozymes.";
RL Protein Expr. Purif. 51:11-21(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ILE-2141.
RC TISSUE=Heart;
RA Peng X.R., Lindgren K., Corneliussen B.;
RT "Corrected sequence for human acetyl-CoA carboxylase 2 obtained by
RT alignment to human genomic DNA and PCR cloning from human skeletal
RT muscle and heart cDNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Heart;
RA Mao J., Wakil S.J.;
RT "Alternative splicing in the human acetyl-CoA carboxylase 2 (ACC2)
RT gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1324-2109.
RC TISSUE=Adipose tissue;
RX PubMed=8670171;
RA Widmer J., Fassihi K.S., Schlichter S.C., Wheeler K.S., Crute B.E.,
RA King N., Nutile-Mcmenemy N., Noll W.W., Daniel S., Ha J., Kim K.-H.,
RA Witters L.A.;
RT "Identification of a second human acetyl-CoA carboxylase gene.";
RL Biochem. J. 316:915-922(1996).
RN [7]
RP PHOSPHORYLATION AT SER-222 BY AMPK.
RX PubMed=12488245; DOI=10.1152/ajpendo.00436.2002;
RA Wojtaszewski J.F., MacDonald C., Nielsen J.N., Hellsten Y.,
RA Hardie D.G., Kemp B.E., Kiens B., Richter E.A.;
RT "Regulation of 5'AMP-activated protein kinase activity and substrate
RT utilization in exercising human skeletal muscle.";
RL Am. J. Physiol. 284:E813-E822(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, AND INTERACTION WITH
RP MID1IP1.
RX PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
RA McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 217-775.
RX PubMed=17876819; DOI=10.1002/prot.21611;
RA Cho Y.S., Lee J.I., Shin D., Kim H.T., Cheon Y.H., Seo C.I., Kim Y.E.,
RA Hyun Y.L., Lee Y.S., Sugiyama K., Park S.Y., Ro S., Cho J.M.,
RA Lee T.G., Heo Y.S.;
RT "Crystal structure of the biotin carboxylase domain of human acetyl-
RT CoA carboxylase 2.";
RL Proteins 70:268-272(2008).
RN [11]
RP STRUCTURE BY NMR OF 885-971.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-053, an apo-biotin carboxy carrier
RT protein from human transcarboxylase.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-193.
RX PubMed=18772397; DOI=10.1126/science.1164368;
RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B.,
RA Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
RA Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
RA Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
RA Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
RA Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
RT "Core signaling pathways in human pancreatic cancers revealed by
RT global genomic analyses.";
RL Science 321:1801-1806(2008).
CC -!- FUNCTION: ACC-beta may be involved in the provision of malonyl-CoA
CC or in the regulation of fatty acid oxidation, rather than fatty
CC acid biosynthesis. Carries out three functions: biotin carboxyl
CC carrier protein, biotin carboxylase and carboxyltransferase.
CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC + malonyl-CoA.
CC -!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
CC CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
CC protein].
CC -!- COFACTOR: Biotin (By similarity).
CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC -!- ENZYME REGULATION: Activity is increased by oligomerization.
CC Activated by citrate. Citrate and MID1IP1 promote oligomerization.
CC Inhibited by malonyl-CoA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for ATP;
CC KM=58 uM for Acetyl-CoA;
CC KM=3.0 mM for NaHCO(3);
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC from acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
CC filamentous polymers. Interacts with MID1IP1; interaction with
CC MID1IP1 promotes oligomerization and increases its activity.
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Note=May associate with
CC membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O00763-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00763-2; Sequence=VSP_000547;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the heart, skeletal
CC muscles and liver.
CC -!- PTM: Phosphorylated by AMPK, leading to inactivate the enzyme.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC -!- SIMILARITY: Contains 1 biotinyl-binding domain.
CC -!- SIMILARITY: Contains 1 carboxyltransferase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58382.1; Type=Miscellaneous discrepancy; Note=Many Frameshifts and conflicts;
CC Sequence=CAE01470.2; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR EMBL; U89344; AAB58382.1; ALT_SEQ; mRNA.
DR EMBL; DQ493870; ABF48723.1; -; mRNA.
DR EMBL; AJ575431; CAE01470.2; ALT_SEQ; mRNA.
DR EMBL; AJ575592; CAE01471.3; -; mRNA.
DR EMBL; AY382667; AAR37018.1; -; mRNA.
DR EMBL; AC007637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U34591; AAC50571.1; -; mRNA.
DR IPI; IPI00013003; -.
DR IPI; IPI00157056; -.
DR PIR; S71091; S71091.
DR RefSeq; NP_001084.3; NM_001093.3.
DR UniGene; Hs.234898; -.
DR PDB; 2DN8; NMR; -; A=885-971.
DR PDB; 2HJW; X-ray; 2.50 A; A=217-775.
DR PDB; 2KCC; NMR; -; A=891-965.
DR PDB; 3FF6; X-ray; 3.19 A; A/B/C/D=1693-2450.
DR PDB; 3GID; X-ray; 2.30 A; A/B=238-760.
DR PDB; 3GLK; X-ray; 2.10 A; A=238-760.
DR PDB; 3JRW; X-ray; 2.60 A; A=217-775.
DR PDB; 3JRX; X-ray; 2.50 A; A=217-775.
DR PDB; 3TDC; X-ray; 2.41 A; A=1690-2445.
DR PDBsum; 2DN8; -.
DR PDBsum; 2HJW; -.
DR PDBsum; 2KCC; -.
DR PDBsum; 3FF6; -.
DR PDBsum; 3GID; -.
DR PDBsum; 3GLK; -.
DR PDBsum; 3JRW; -.
DR PDBsum; 3JRX; -.
DR PDBsum; 3TDC; -.
DR ProteinModelPortal; O00763; -.
DR SMR; O00763; 237-758, 891-960, 1695-2449.
DR DIP; DIP-51617N; -.
DR IntAct; O00763; 3.
DR STRING; 9606.ENSP00000367079; -.
DR PhosphoSite; O00763; -.
DR PaxDb; O00763; -.
DR PRIDE; O00763; -.
DR DNASU; 32; -.
DR Ensembl; ENST00000338432; ENSP00000341044; ENSG00000076555.
DR Ensembl; ENST00000377848; ENSP00000367079; ENSG00000076555.
DR GeneID; 32; -.
DR KEGG; hsa:32; -.
DR UCSC; uc001tob.3; human.
DR CTD; 32; -.
DR GeneCards; GC12P109577; -.
DR H-InvDB; HIX0036741; -.
DR HGNC; HGNC:85; ACACB.
DR HPA; HPA006554; -.
DR MIM; 601557; gene.
DR neXtProt; NX_O00763; -.
DR PharmGKB; PA24422; -.
DR eggNOG; COG0511; -.
DR HOVERGEN; HBG005371; -.
DR KO; K11262; -.
DR OMA; TVIMDPF; -.
DR OrthoDB; EOG4X0MRD; -.
DR BRENDA; 6.4.1.2; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_11163; Activated AMPK stimulates fatty-acid oxidation in muscle.
DR SABIO-RK; O00763; -.
DR UniPathway; UPA00655; UER00711.
DR BindingDB; O00763; -.
DR ChEMBL; CHEMBL4829; -.
DR DrugBank; DB00121; Biotin.
DR EvolutionaryTrace; O00763; -.
DR GenomeRNAi; 32; -.
DR NextBio; 123; -.
DR ArrayExpress; O00763; -.
DR Bgee; O00763; -.
DR CleanEx; HS_ACACB; -.
DR Genevestigator; O00763; -.
DR GermOnline; ENSG00000076555; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0046320; P:regulation of fatty acid oxidation; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR000022; Carboxyl_trans.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF00289; CPSase_L_chain; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; FALSE_NEG.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Biotin; Complete proteome; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Manganese; Membrane; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 2458 Acetyl-CoA carboxylase 2.
FT /FTId=PRO_0000146767.
FT DOMAIN 259 761 Biotin carboxylation.
FT DOMAIN 414 609 ATP-grasp.
FT DOMAIN 895 961 Biotinyl-binding.
FT DOMAIN 1809 2305 Carboxyltransferase.
FT NP_BIND 458 463 ATP (Potential).
FT ACT_SITE 584 584 By similarity.
FT METAL 567 567 Manganese 1 (By similarity).
FT METAL 580 580 Manganese 1 (By similarity).
FT METAL 580 580 Manganese 2 (By similarity).
FT METAL 582 582 Manganese 2 (By similarity).
FT BINDING 1934 1934 Coenzyme A (By similarity).
FT BINDING 2238 2238 Coenzyme A (By similarity).
FT BINDING 2240 2240 Coenzyme A (By similarity).
FT MOD_RES 222 222 Phosphoserine; by AMPK.
FT MOD_RES 929 929 N6-biotinyllysine (By similarity).
FT VAR_SEQ 1118 1187 Missing (in isoform Short).
FT /FTId=VSP_000547.
FT VARIANT 193 193 R -> L (in a pancreatic ductal
FT adenocarcinoma sample; somatic mutation).
FT /FTId=VAR_062667.
FT VARIANT 552 552 I -> V (in dbSNP:rs16940029).
FT /FTId=VAR_031255.
FT VARIANT 651 651 A -> T (in dbSNP:rs2300455).
FT /FTId=VAR_031256.
FT VARIANT 2141 2141 V -> I (in dbSNP:rs2075260).
FT /FTId=VAR_031257.
FT CONFLICT 9 9 C -> R (in Ref. 2; ABF48723).
FT CONFLICT 120 120 T -> I (in Ref. 4; AAR37018).
FT CONFLICT 422 422 I -> T (in Ref. 4; AAR37018).
FT CONFLICT 1340 1340 S -> N (in Ref. 6; AAC50571).
FT CONFLICT 1383 1383 D -> G (in Ref. 6; AAC50571).
FT CONFLICT 1425 1425 V -> M (in Ref. 6; AAC50571).
FT CONFLICT 1819 1821 AEG -> PEA (in Ref. 6; AAC50571).
FT CONFLICT 1892 1893 MI -> IM (in Ref. 6; AAC50571).
FT HELIX 247 253
FT STRAND 262 265
FT HELIX 269 287
FT STRAND 292 299
FT HELIX 301 305
FT HELIX 309 313
FT STRAND 314 319
FT HELIX 325 327
FT TURN 328 330
FT HELIX 332 341
FT STRAND 345 348
FT HELIX 353 356
FT HELIX 359 366
FT STRAND 370 373
FT HELIX 376 379
FT HELIX 385 394
FT TURN 403 406
FT HELIX 426 431
FT HELIX 437 447
FT STRAND 449 455
FT STRAND 464 467
FT TURN 470 472
FT HELIX 473 483
FT STRAND 489 493
FT STRAND 496 507
FT STRAND 509 511
FT STRAND 513 523
FT STRAND 530 535
FT HELIX 541 558
FT STRAND 562 571
FT STRAND 572 574
FT STRAND 576 582
FT HELIX 589 596
FT HELIX 600 608
FT HELIX 613 615
FT HELIX 617 622
FT STRAND 635 637
FT STRAND 646 653
FT STRAND 669 671
FT STRAND 679 685
FT STRAND 700 709
FT HELIX 710 724
FT HELIX 728 730
FT HELIX 732 742
FT HELIX 744 748
FT HELIX 754 756
FT STRAND 896 898
FT STRAND 900 902
FT STRAND 903 910
FT STRAND 914 916
FT STRAND 921 927
FT STRAND 930 935
FT STRAND 937 944
FT STRAND 957 961
FT TURN 1698 1700
FT HELIX 1703 1711
FT HELIX 1717 1719
FT HELIX 1720 1732
FT STRAND 1742 1750
FT STRAND 1756 1759
FT STRAND 1767 1777
FT STRAND 1786 1793
FT HELIX 1798 1800
FT HELIX 1804 1820
FT STRAND 1824 1828
FT HELIX 1839 1842
FT STRAND 1846 1850
FT HELIX 1855 1857
FT STRAND 1859 1864
FT HELIX 1866 1872
FT TURN 1873 1876
FT STRAND 1878 1885
FT STRAND 1888 1896
FT STRAND 1899 1901
FT HELIX 1905 1924
FT STRAND 1927 1931
FT STRAND 1933 1936
FT HELIX 1938 1946
FT STRAND 1948 1952
FT STRAND 1956 1960
FT HELIX 1962 1969
FT HELIX 1977 1981
FT HELIX 1983 1986
FT TURN 1987 1990
FT STRAND 1993 1998
FT HELIX 1999 2010
FT HELIX 2045 2050
FT STRAND 2055 2057
FT STRAND 2072 2075
FT STRAND 2082 2089
FT STRAND 2092 2099
FT STRAND 2104 2108
FT STRAND 2120 2124
FT HELIX 2131 2147
FT STRAND 2151 2154
FT HELIX 2164 2168
FT HELIX 2171 2183
FT STRAND 2189 2193
FT STRAND 2198 2200
FT HELIX 2201 2205
FT HELIX 2209 2211
FT TURN 2213 2215
FT STRAND 2216 2221
FT STRAND 2225 2229
FT HELIX 2231 2238
FT HELIX 2241 2251
FT HELIX 2253 2261
FT HELIX 2269 2299
FT HELIX 2300 2302
FT HELIX 2304 2309
FT STRAND 2312 2317
FT HELIX 2319 2321
FT HELIX 2322 2344
FT HELIX 2345 2348
FT HELIX 2352 2365
FT HELIX 2369 2376
FT HELIX 2378 2388
FT HELIX 2404 2420
FT TURN 2423 2425
FT HELIX 2426 2435
FT HELIX 2439 2448
SQ SEQUENCE 2458 AA; 276541 MW; ED12674A1A8A0706 CRC64;
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS
RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF
GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK
DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK
YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL
AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL
GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR
APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF
SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA
DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK
AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK
QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST
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