ID   ACCC_ARATH              Reviewed;         537 AA.
AC   O04983; P93650; Q9C5F8;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Biotin carboxylase, chloroplastic;
DE            EC=6.3.4.14 {ECO:0000269|PubMed:9414551};
DE   AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305};
DE   Flags: Precursor;
GN   Name=CAC2; OrderedLocusNames=At5g35360; ORFNames=T26D22.8;
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=9349276; DOI=10.1023/a:1005881006620;
RA   Bao X., Shorrosh B.S., Ohlrogge J.B.;
RT   "Isolation and characterization of an Arabidopsis biotin carboxylase gene
RT   and its promoter.";
RL   Plant Mol. Biol. 35:539-550(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=9414551; DOI=10.1104/pp.115.4.1371;
RA   Sun J., Ke J., Johnson J.L., Nikolau B.J., Wurtele E.S.;
RT   "Biochemical and molecular biological characterization of CAC2, the
RT   Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the
RT   plastidic acetyl-coenzyme A carboxylase.";
RL   Plant Physiol. 115:1371-1383(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10759501; DOI=10.1104/pp.122.4.1057;
RA   Ke J., Wen T.N., Nikolau B.J., Wurtele E.S.;
RT   "Coordinate regulation of the nuclear and plastidic genes coding for the
RT   subunits of the heteromeric acetyl-coenzyme A carboxylase.";
RL   Plant Physiol. 122:1057-1071(2000).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA   van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT   proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000269|PubMed:9414551}.
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:0000269|PubMed:9414551};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00969};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00969};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00969};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 mM for biotin {ECO:0000269|PubMed:9414551};
CC         KM=88 mM for bicarbonate {ECO:0000269|PubMed:9414551};
CC         Vmax=16 nmol/min/mg enzyme {ECO:0000269|PubMed:9414551};
CC       pH dependence:
CC         Optimum pH is 8.3-8.9. {ECO:0000269|PubMed:9414551};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein, biotin carboxylase and two subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:18431481}.
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=O04983-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Accumulates in fatty acids synthesizing tissues.
CC       Mostly expressed in siliques, developing leaves, and flowers, present
CC       in roots and embryos (especially at torpedo stage), and, to a lower
CC       extent, in mature leaves. {ECO:0000269|PubMed:10759501,
CC       ECO:0000269|PubMed:9349276, ECO:0000269|PubMed:9414551}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA70282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y09061; CAA70282.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U90879; AAC09008.1; -; mRNA.
DR   EMBL; U91414; AAC09009.1; -; Genomic_DNA.
DR   EMBL; AB025636; BAB11486.1; -; Genomic_DNA.
DR   EMBL; AF058826; AAC13611.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93956.1; -; Genomic_DNA.
DR   EMBL; AF360279; AAK25989.1; -; mRNA.
DR   EMBL; AY142630; AAN13088.1; -; mRNA.
DR   EMBL; AY085968; AAM63178.1; -; mRNA.
DR   PIR; T01180; T01180.
DR   RefSeq; NP_198386.1; NM_122927.4. [O04983-1]
DR   AlphaFoldDB; O04983; -.
DR   SMR; O04983; -.
DR   BioGRID; 18751; 5.
DR   IntAct; O04983; 1.
DR   STRING; 3702.O04983; -.
DR   MetOSite; O04983; -.
DR   PaxDb; 3702-AT5G35360-3; -.
DR   ProteomicsDB; 244341; -. [O04983-1]
DR   EnsemblPlants; AT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
DR   GeneID; 833497; -.
DR   Gramene; AT5G35360.1; AT5G35360.1; AT5G35360. [O04983-1]
DR   KEGG; ath:AT5G35360; -.
DR   Araport; AT5G35360; -.
DR   TAIR; AT5G35360; CAC2.
DR   eggNOG; KOG0238; Eukaryota.
DR   InParanoid; O04983; -.
DR   OMA; AISHECT; -.
DR   PhylomeDB; O04983; -.
DR   BioCyc; ARA:AT5G35360-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G35360-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:O04983; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O04983; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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   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   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00514; accC; 1.
DR   PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   Genevisible; O04983; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Biotin; Chloroplast;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..71
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           72..537
FT                   /note="Biotin carboxylase, chloroplastic"
FT                   /id="PRO_0000391772"
FT   DOMAIN          192..389
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         236..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         272..275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         309
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         347
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         360
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         360
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         362
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         362
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   BINDING         364
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         367
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         410
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   BINDING         410
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:P24182"
FT   CONFLICT        181
FT                   /note="S -> T (in Ref. 1; CAA70282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="K -> T (in Ref. 1; CAA70282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="Missing (in Ref. 1; CAA70282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        447
FT                   /note="D -> N (in Ref. 6; AAK25989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  58387 MW;  CB57C973A2A735C8 CRC64;
     MDASMITNSK SITSPPSLAL GKSGGGGVIR SSLCNLMMPS KVNFPRQRTQ TLKVSQKKLK
     RATSGGLGVT CSGGDKILVA NRGEIAVRVI RTAHEMGIPC VAVYSTIDKD ALHVKLADEA
     VCIGEAPSNQ SYLVIPNVLS AAISRGCTML HPGYGFLSEN ALFVEMCRDH GINFIGPNPD
     SIRVMGDKAT ARETMKNAGV PTVPGSDGLL QSTEEAVRVA NEIGFPVMIK ATAGGGGRGM
     RLAKEPGEFV KLLQQAKSEA AAAFGNDGCY LEKFVQNPRH IEFQVLADKF GNVVHFGERD
     CSIQRRNQKL LEEAPSPALT AELRKAMGDA AVAAAASIGY IGVGTVEFLL DERGSFYFME
     MNTRIQVEHP VTEMIYSVDL IEEQIRVAMG EKLRYKQEDI VLRGHSIECR INAEDPFKGF
     RPGPGRITSY LPSGGPFVRM DSHVYSDYVV PPSYDSLLGK LIVWAPTREK AIERMKRALN
     DTIITGVPTT INYHKLILDV EDFKNGKVDT AFIVKHEEEL AEPQEIVAVK DLTNATV
//