ACACA_SHEEP
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 03-AUG-2022, entry version 137.
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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC 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,
CC ECO:0000255|PROSITE-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 PRIDE; Q28559; -.
DR GeneID; 443186; -.
DR KEGG; oas:443186; -.
DR CTD; 31; -.
DR eggNOG; KOG0368; Eukaryota.
DR OrthoDB; 156081at2759; -.
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 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 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
