ACAC_SCHPO
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 03-AUG-2022, entry version 187.
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; 8.
DR IntAct; P78820; 1.
DR STRING; 4896.SPAC56E4.04c.1; -.
DR iPTMnet; P78820; -.
DR MaxQB; P78820; -.
DR PaxDb; P78820; -.
DR PRIDE; P78820; -.
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; LIQCAMP; -.
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; ISO:PomBase.
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 Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
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 Pfam; PF08326; ACC_central; 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; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 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
