ID   ACAC_SCHPO              Reviewed;        2280 AA.
AC   P78820; O94557; Q09447; Q09576; Q09616; Q09667;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Acetyl-CoA carboxylase;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   AltName: Full=Cell untimely torn protein 6;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=cut6; ORFNames=SPAC56E4.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / HM123;
RA   Saito A., Kazuta Y., Toh H., Kondo H., Tanabe T.;
RT   "Biotin-dependent enzymes in Schizosaccharomyces pombe: cloning and
RT   nucleotide sequences of acetyl-CoA carboxylase and pyruvate carboxylase.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-161; 636-871; 998-1098 AND
RP   1380-1547.
RX   PubMed=8769419; DOI=10.1083/jcb.134.4.949;
RA   Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y.,
RA   Hirata A., Yanagida M.;
RT   "Aberrant mitosis in fission yeast mutants defective in fatty acid
RT   synthetase and acetyl CoA carboxylase.";
RL   J. Cell Biol. 134:949-961(1996).
RN   [4]
RP   INTERACTION WITH SAD1.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1181, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Carries out three functions: biotin carboxyl carrier protein,
CC       biotin carboxylase and carboxyltransferase.
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:Q00955};
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:Q5SWU9};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: By phosphorylation. {ECO:0000250}.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11916.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA11917.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D78169; BAA11238.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16395.1; -; Genomic_DNA.
DR   EMBL; D83413; BAA11914.1; -; Genomic_DNA.
DR   EMBL; D83414; BAA11915.1; -; Genomic_DNA.
DR   EMBL; D83416; BAA11917.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; D83415; BAA11916.1; ALT_FRAME; Genomic_DNA.
DR   PIR; T38906; T38906.
DR   PIR; T42531; T42531.
DR   RefSeq; NP_593271.1; NM_001018668.2.
DR   AlphaFoldDB; P78820; -.
DR   SMR; P78820; -.
DR   BioGRID; 279766; 9.
DR   IntAct; P78820; 1.
DR   STRING; 284812.P78820; -.
DR   iPTMnet; P78820; -.
DR   MaxQB; P78820; -.
DR   PaxDb; 4896-SPAC56E4-04c-1; -.
DR   EnsemblFungi; SPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c.
DR   GeneID; 2543344; -.
DR   KEGG; spo:SPAC56E4.04c; -.
DR   PomBase; SPAC56E4.04c; cut6.
DR   VEuPathDB; FungiDB:SPAC56E4.04c; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   InParanoid; P78820; -.
DR   OMA; PTPKGHC; -.
DR   PhylomeDB; P78820; -.
DR   Reactome; R-SPO-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-SPO-196780; Biotin transport and metabolism.
DR   Reactome; R-SPO-200425; Carnitine metabolism.
DR   Reactome; R-SPO-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:P78820; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:PomBase.
DR   GO; GO:0004075; F:biotin carboxylase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0101026; P:mitotic nuclear membrane biogenesis; IMP:PomBase.
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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Biotin; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..2280
FT                   /note="Acetyl-CoA carboxylase"
FT                   /id="PRO_0000146769"
FT   DOMAIN          68..577
FT                   /note="Biotin carboxylation"
FT   DOMAIN          226..418
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          704..778
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1524..1863
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1867..2181
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1524..2181
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000250"
FT   BINDING         266..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         375
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1772
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2074
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2076
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         745
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   MOD_RES         1179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        14..42
FT                   /note="LYAIKATISLPRLFYRRLRTMAPRVASHF -> RFIFIDVLLISQLSISSFS
FT                   FFILYFINHI (in Ref. 3; BAA11914)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="P -> S (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339..340
FT                   /note="IE -> L (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        512
FT                   /note="A -> S (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="A -> T (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636..639
FT                   /note="DNTR -> YRIP (in Ref. 3; BAA11915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1017
FT                   /note="K -> N (in Ref. 3; BAA11917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1073
FT                   /note="R -> H (in Ref. 3; BAA11917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1098
FT                   /note="F -> L (in Ref. 3; BAA11917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105
FT                   /note="V -> Y (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1362
FT                   /note="R -> S (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1427
FT                   /note="F -> Y (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1444
FT                   /note="G -> E (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1445
FT                   /note="F -> C (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1449
FT                   /note="F -> L (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1451
FT                   /note="R -> S (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1465
FT                   /note="I -> F (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1480
FT                   /note="V -> L (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1485
FT                   /note="V -> L (in Ref. 3; BAA11916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1496
FT                   /note="A -> S (in Ref. 1; BAA11238)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2280 AA;  256843 MW;  8262C9A1A5C8E891 CRC64;
     MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK APAGKVKDYI
     ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER AIKFTVMATP DDLKVNADYI
     RMADQYVEVP GGSNNNNYAN VELIVDIAER MNVHAVWAGW GHASENPKLP EMLSASSKKI
     VFIGPPGSAM RSLGDKISST IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA
     CIRSAEEGIA VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM
     KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA TFHEMERAAV
     RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQVAMGL
     PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE SFKVQKVPTP KGHCVACRIT SEDPGEGFKP
     SSGMIKDLNF RSSSNVWGYF SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL
     SIRGDFRTTV EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH
     ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG SYHLFLNGSR
     CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL SCMLEQENDP TQLRTPSPGK
     LVRFLVETGE HIKAGEAYAE VEVMKMIMPL VATEDGVVQL IKQPGASLDA GDILGILTLD
     DPSRVTHALP FDGQLPNWGE PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV
     EVLRNHELPY SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD
     GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF SGINKREEDV
     ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK SEPSTFVSLY FNDILRKLTD
     LDSRVTSKVS LKARELLITC AMPSLNERFS QMEHILKSSV VESHYGDAKF SHRTPSLDIL
     KELIDSKYTV FDVLPAFFCH TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW
     RFQLHSSGAP GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM
     IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV VNVALTSTGD
     LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA YPSYYTYRVS AEQKDGNLVH
     YNEDERIRHI EPALAFQLEL GRLSNFNIEP VFTDNHNIHV YRATAKNMDT DKRFFTRALV
     RPGRLRDEIP TAEYLISETH RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA
     ALGGFLERFG RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT
     ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP ELFRRAFTDS
     WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT NSCGMVAWCI TVKTPEYPNG
     RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ LARQRGIPRI YLAANSGARI GVADEIVPLF
     NIAWVDPDSP EKGFDYIYLT PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG
     LGVECLRGSG LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA
     PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY IPDKRNNPVP
     ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL FDKGSFQETL NGWAKTVVVG
     RARMGGIPTG VIAVETRTIE NTVPADPANP DSTEQVLMEA GQVWYPNSAF KTAQAINDFN
     HGEQLPLFIL ANWRGFSGGQ RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW
     VVVDPTINED QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR
     DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR KPLKWTEARR
     FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE EWCGKQDWDE SDKSVVCWIE
     EHNDDLSKRT QELKSTYYSE RLSKLLRSDR KGMIDSLAQV LTELDENEKK ELAGKLASVN
//