ID   ACC2_ARATH              Reviewed;        2355 AA.
AC   F4I1L3; Q9C8G0; Q9FR96;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Acetyl-CoA carboxylase 2;
DE            EC=6.4.1.2;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACC2; OrderedLocusNames=At1g36180; ORFNames=F15C21.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
RA   Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J., Ichikawa N.;
RT   "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
RT   Arabidopsis: tandem gene duplication has made two differentially expressed
RT   isozymes.";
RL   Plant Cell Physiol. 36:779-787(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=12943542; DOI=10.1046/j.1365-313x.2003.016010.x;
RA   Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M., Caboche M.,
RA   Lepiniec L., Rochat C.;
RT   "Multifunctional acetyl-CoA carboxylase 1 is essential for very long chain
RT   fatty acid elongation and embryo development in Arabidopsis.";
RL   Plant J. 33:75-86(2003).
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation of
CC       acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty
CC       acid synthesis and in the cytosol in various biosynthetic pathways
CC       including fatty acid elongation. {ECO:0000250|UniProtKB:Q38970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01066};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC       ProRule:PRU00969};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=F4I1L3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC       {ECO:0000269|PubMed:12943542, ECO:0000269|PubMed:7551584}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG40564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51252.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF062308; AAG40564.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC025781; AAG51252.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31851.1; -; Genomic_DNA.
DR   PIR; E86483; E86483.
DR   RefSeq; NP_174850.4; NM_103314.5. [F4I1L3-1]
DR   AlphaFoldDB; F4I1L3; -.
DR   SMR; F4I1L3; -.
DR   BioGRID; 25754; 1.
DR   IntAct; F4I1L3; 1.
DR   STRING; 3702.F4I1L3; -.
DR   iPTMnet; F4I1L3; -.
DR   PaxDb; 3702-AT1G36180-1; -.
DR   ProteomicsDB; 244567; -. [F4I1L3-1]
DR   EnsemblPlants; AT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
DR   GeneID; 840522; -.
DR   Gramene; AT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
DR   KEGG; ath:AT1G36180; -.
DR   Araport; AT1G36180; -.
DR   TAIR; AT1G36180; ACC2.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   InParanoid; F4I1L3; -.
DR   OMA; GTVAWNM; -.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:F4I1L3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I1L3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   Genevisible; F4I1L3; AT.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding; Biotin; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..2355
FT                   /note="Acetyl-CoA carboxylase 2"
FT                   /id="PRO_0000412212"
FT   DOMAIN          138..645
FT                   /note="Biotin carboxylation"
FT   DOMAIN          291..485
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          772..846
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1593..1932
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1936..2251
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1593..2251
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000250"
FT   BINDING         317..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         440
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         440
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         454
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         454
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         456
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT                   ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         1841
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2142
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2144
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         813
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         1133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q38970"
FT   MOD_RES         1293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q38970"
FT   CONFLICT        1855
FT                   /note="R -> K (in Ref. 1; AAG40564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2355 AA;  262729 MW;  D3E322E33E847E0A CRC64;
     MEMRALGSSC STGNGGSAPI TLTNISPWIT TVFPSTVKLR SSLRTFKGVS SRVRTFKGVS
     STRVLSRTKQ QFPLFCFLNP DPISFLENDV SEAERTVVLP DGSVNGAGSV NGYHSDVVPG
     RNVAEVNEFC KALGGKRPIH SILVATNGMA AVKFIRSVRT WAYETFGSEK AVKLVAMATP
     EDMRINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEMAEV TRVDAVWPGW GHASENPELP
     DALKEKGIIF LGPPADSMIA LGDKIGSSLI AQAADVPTLP WSGSHVKIPP GRSLVTVPEE
     IYKKACVYTT EEAIASCQVV GYPAMIKASW GGGGKGIRKV HNDDEVRALF KQVQGEVPGS
     PIFIMKVASQ SRHLEAQLLC DQYGNVAALH SRDCSVQRRH QKIIEEGPIT VAPQETIKKL
     EQAARRLAKS VNYVGAATVE YLYSMDTGEY YFLELNPRLQ VEHPVTEWIA EVNLPAAQVA
     VGMGIPLWQI PEIRRFYGME HGGGYDSWRK TSVVASPFDF DEAESLRPKG HCVAVRVTSE
     DPDDGFKPTS GEIQELSFKS KPNMWSYFSV KSGGGIHEFS DSQFGHVFAF GESRSVAIAN
     MVLALKEIQI RGDIRTNVDY TIDLLHASDY RENKIHTGWL DSRIAMRVRA ERPPWYLSVV
     GGALYKASTT SSAVVSDYVG YLEKGQIPPK HISLVHSQVS LNIEGSKYTI DVVRGGSGTY
     RLRMSNSEVV AEIHTLRDGG LLMQLDGKSH VIYAKEEATG TRLLIDGRTC LLQNDHDPSK
     LMAETPCKLL RYLVSDNSSI DTDTPYAEVE VMKMCMPLIS PASGVIHFKL SEGQAMQAGE
     LIAKLDLDDP SAVRKAKPFR GSFPRLGLPT AISGKVHQRC AATLNAARMI LAGYDHKVDE
     VLQDLLNCLD SPELPFLQWQ ECFAVLATRL PKDLRNMLEL KYKEFEIISK TSLTPDFPAK
     LLKGILEAHL SSCDEKERGS LERLIEPLMS LVKSYEGGRE SHARLIVHSL FEEYLSVEEL
     FNDNMLADVI ERMRQQYKKD RLKIVDIVLS HQGIIHKNKL VLRLMEQLVY PNPAAYREKL
     IRFSALNHTN YSQLALKASQ LLEQTKRSEL RSNIARSLSE LEMFTEAGEN MDTPKRKSAI
     SETMENLVSS SLAVEDALVG LFDHSDHTLQ RRVVETYIHR LYQPYVVKES VRMQWHQSGV
     IASWEFLEHF ERKNTGPDDH EISEKGIVAK SSKRKRGTMV IIKSLQFLPS IINASLRETN
     HSHCEYARAP LSGNMMHIAV VGINNQMSLL QDSGDEDQTQ ERVNKLAKIL KEEEVSLTLC
     SAGVGVISCI IQRDEGRTPM RHSFHWLMEK QYYVEEPLLR HVEPPLSVYL ELDKLKGYSN
     IQYSPSRDRQ WHMYSVTDRP VPIKRMFLRS LVRQTTMNDG FLLQQGQDYQ LSQTVLSMAF
     TSKCILRSLM NAMEELELNA HNAAMKPDHA HMFLCILREQ QIDDLVPYPR RFEVNAEDEE
     TTVETILEEA TQEIHRSVGV RMHALGVCEW EVRLWLVSSG LANGAWRVVV ANVTGRTCTV
     HIYREVEATG RNSLIYHSIT KKGPLHGTLI NGQYKPLNNL DRKRLAARRS NTTYCYDFPL
     AFETALELNW ASQHSGVRKP CKNRLINVKE LVFSNTEGSL GTSLIPVERP AGLNDIGMVA
     WILEMSTPEF PMGRKLLIVA NDVTFKAGSF GPREDAFFLA VTELACTKKL PLIYLAANSG
     ARLGVAEEVK ACFKVGWSDE VSPGNDFQYI YLSSEDYARI GSSVIAHEVK LPSGETRWVI
     DTIVGKEDGL GVENLTGSGA IAGAYSRAYN ETFTLTFVSG RSVGIGAYLA RLGMRCIQRL
     DQPIILTGFS TLNKLLGREV YSSHMQLGGP KIMGTNGVVH LTVSDDLEGV SAILNWLSYI
     PAYVGGPLPV LAPLDPPERT VEYIPENSCD PRAAIAGIND NTGKWLGGIF DKNSFVETLE
     GWARTVVTGR AKLGGIPIGV VAVETQTVMH VIPADPGQLD SHERVVPQAG QVWFPDSAAK
     TAQALMDFNR EQLPLFIIAN WRGFSGGQRD LFEGILQAGS AIVENLRTYR QPVFVYIPMM
     GELRGGAWVV VDSQINSDYI EMYADETARG NVLEPEGMIE IKFRRKELLE CMGRLDQTLI
     NLKANIQDAK RNKAYANIEL LQKQIKTREK QLLPVYTQIA TKFAELHDTS MRMAAKGVIK
     SVVEWSGSRS FFYKKLYRRI AESSLVRNIR KASGDILSYK SAMGLIQDWF RKSEIAKGKE
     EAWTDDQLFF TWKDNVSNYE QKLSELRTQK LLNQLAEIGN SSDLQALPQG LANLLNKVDL
     SRREELVDAI RKVLG
//