ID   ACACA_SHEEP             Reviewed;        2346 AA.
AC   Q28559; O62847; Q6KEV5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Acetyl-CoA carboxylase 1 {ECO:0000250|UniProtKB:Q13085};
DE            Short=ACC1;
DE            EC=6.4.1.2 {ECO:0000250|UniProtKB:Q13085};
DE   AltName: Full=ACC-alpha;
GN   Name=ACACA {ECO:0000250|UniProtKB:Q13085}; Synonyms=ACAC;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Finn-Dorset; TISSUE=Adipose tissue;
RX   PubMed=7890176; DOI=10.1016/0378-1119(94)00871-o;
RA   Barber M.C., Travers M.T.;
RT   "Cloning and characterisation of multiple acetyl-CoA carboxylase
RT   transcripts in ovine adipose tissue.";
RL   Gene 154:271-275(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-144 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   INDUCTION BY LACTATION.
RC   STRAIN=Finn-Dorset; TISSUE=Mammary gland;
RX   PubMed=9639557; DOI=10.1042/bj3330017;
RA   Barber M.C., Travers M.T.;
RT   "Elucidation of a promoter activity that directs the expression of acetyl-
RT   CoA carboxylase alpha with an alternative N-terminus in a tissue-restricted
RT   fashion.";
RL   Biochem. J. 333:17-25(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
RA   Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.;
RT   "Asymmetric expression of transcripts derived from the shared promoter
RT   between the divergently oriented ACACA and TADA2L genes.";
RL   Genomics 85:71-84(2005).
CC   -!- FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-
CC       CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty
CC       acid biosynthesis. This is a 2 steps reaction starting with the ATP-
CC       dependent carboxylation of the biotin carried by the biotin carboxyl
CC       carrier (BCC) domain followed by the transfer of the carboxyl group
CC       from carboxylated biotin to acetyl-CoA. {ECO:0000250|UniProtKB:Q13085}.
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:Q13085};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC         Evidence={ECO:0000250|UniProtKB:Q13085};
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   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:Q13085, ECO:0000255|PROSITE-
CC         ProRule:PRU01066};
CC   -!- ACTIVITY REGULATION: Inhibited by phosphorylation (By similarity).
CC       Citrate promotes oligomerization of the protein into filaments that
CC       correspond to the most active form of the carboxylase (By similarity).
CC       {ECO:0000250|UniProtKB:Q13085}.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:Q13085}.
CC   -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form filamentous
CC       polymers. Interacts in its inactive phosphorylated form with the BRCT
CC       domains of BRCA1 which prevents ACACA dephosphorylation and inhibits
CC       lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1
CC       promotes oligomerization and increases its activity.
CC       {ECO:0000250|UniProtKB:Q13085}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q5SWU9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q28559-1; Sequence=Displayed;
CC       Name=2; Synonyms=E5A;
CC         IsoId=Q28559-2; Sequence=VSP_026102;
CC       Name=3;
CC         IsoId=Q28559-3; Sequence=VSP_026103;
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed at high levels in mammary
CC       gland. {ECO:0000269|PubMed:9639557}.
CC   -!- INDUCTION: [Isoform 2]: Induced in mammary gland during lactation.
CC       {ECO:0000269|PubMed:9639557}.
CC   -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC       domain that catalyzes the ATP-dependent transient carboxylation of the
CC       biotin covalently attached to the central biotinyl-binding/biotin
CC       carboxyl carrier (BCC) domain. The C-terminal carboxyl transferase (CT)
CC       domain catalyzes the transfer of the carboxyl group from carboxylated
CC       biotin to acetyl-CoA to produce malonyl-CoA.
CC       {ECO:0000250|UniProtKB:Q13085}.
CC   -!- PTM: Phosphorylation on Ser-1263 is required for interaction with
CC       BRCA1. {ECO:0000250|UniProtKB:Q13085}.
CC   -!- PTM: Phosphorylation at Ser-80 by AMPK inactivates enzyme activity.
CC       {ECO:0000250|UniProtKB:P11497}.
CC   -!- PTM: The biotin cofactor is covalently attached to the central
CC       biotinyl-binding domain and is required for the catalytic activity.
CC       {ECO:0000250|UniProtKB:Q13085}.
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DR   EMBL; X80045; CAA56352.1; -; mRNA.
DR   EMBL; AJ001056; CAA04506.1; -; mRNA.
DR   EMBL; AJ564445; CAD92090.1; -; mRNA.
DR   RefSeq; NP_001009256.1; NM_001009256.1. [Q28559-1]
DR   AlphaFoldDB; Q28559; -.
DR   SMR; Q28559; -.
DR   STRING; 9940.ENSOARP00000000876; -.
DR   PaxDb; 9940-ENSOARP00000000876; -.
DR   GeneID; 443186; -.
DR   KEGG; oas:443186; -.
DR   CTD; 31; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   OrthoDB; 911at2759; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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:SF5; ACETYL-COA CARBOXYLASE 1; 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   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; Alternative promoter usage; ATP-binding;
KW   Biotin; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..2346
FT                   /note="Acetyl-CoA carboxylase 1"
FT                   /id="PRO_0000146766"
FT   DOMAIN          117..618
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   DOMAIN          275..466
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          745..819
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1576..1914
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1918..2234
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1576..2234
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000250"
FT   BINDING         315..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         424
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         424
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         437
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         437
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         437
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         437
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         439
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         439
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         1823
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2127
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2129
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         58
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497"
FT   MOD_RES         80
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT   MOD_RES         610
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         786
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497,
FT                   ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         835
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         1201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497"
FT   MOD_RES         1216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11497"
FT   MOD_RES         1218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT   MOD_RES         1227
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT   MOD_RES         1259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SWU9"
FT   MOD_RES         1263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         1273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         1334
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   MOD_RES         2153
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13085"
FT   VAR_SEQ         1..75
FT                   /note="MGEPSSLAKPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPA
FT                   SVSSDTLSDLGISSLQDGLALHM -> MEGSAEESKEMRYYMLQ (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:9639557"
FT                   /id="VSP_026102"
FT   VAR_SEQ         1
FT                   /note="M -> MWWSTLMSILRASSFWKWISAQTIRIIRALRARFEGTM (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15607423"
FT                   /id="VSP_026103"
SQ   SEQUENCE   2346 AA;  265251 MW;  BCA010ADF6CD24EF CRC64;
     MGEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVSSDTLS
     DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK
     VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
     GPNNNNYANV ELILDIARRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL
     GDKIASSIVA QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA
     AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
     QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV FEHMEQCAVK LARMVGYVSA
     GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY
     GVSPWGDAPI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
     FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
     ESFQLNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN FLHSLERGQV
     LSAHTLLNTV DVELIYEGEK IVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG
     SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA
     EIEVMKMVMT LTAAESGCIH YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ
     STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVEGLMKTLR DPSLPLLELQ
     DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
     FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD
     MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR
     ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
     SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
     SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFCDSP
     PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDSLAAMFRE FTQQNKATLV
     EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ
     LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE
     YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
     SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA
     YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSSQA
     FLPPPPLPSD ILTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI
     GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD
     PEDPYKGYKY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS
     GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR
     EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS YMPKSVYSSV PLLNSKDPID
     RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG
     IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL
     MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI
     NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSARE
     RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG VINDILDWKT SRTFFYWRLR
     RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE
     EDGVRSVIEE NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST
     MDSPST
//