CP27A_RABIT
ID CP27A_RABIT Reviewed; 535 AA.
AC P17177;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sterol 26-hydroxylase, mitochondrial {ECO:0000303|PubMed:2722778};
DE EC=1.14.15.15 {ECO:0000269|PubMed:2722778};
DE AltName: Full=5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase {ECO:0000305|PubMed:2722778};
DE AltName: Full=Cytochrome P-450C27/25;
DE AltName: Full=Cytochrome P450 27;
DE AltName: Full=Sterol 27-hydroxylase {ECO:0000250|UniProtKB:Q02318};
DE AltName: Full=Vitamin D(3) 25-hydroxylase {ECO:0000250|UniProtKB:Q02318};
DE Flags: Precursor;
GN Name=CYP27A1; Synonyms=CYP27;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-51; 357-365; 367-380;
RP 414-424; 505-521 AND 526-535, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=2722778; DOI=10.1016/s0021-9258(18)83172-6;
RA Andersson S., Davis D.L., Dahlbaeck H., Joernvall H., Russell D.W.;
RT "Cloning, structure, and expression of the mitochondrial cytochrome P-450
RT sterol 26-hydroxylase, a bile acid biosynthetic enzyme.";
RL J. Biol. Chem. 264:8222-8229(1989).
CC -!- FUNCTION: Cytochrome P450 monooxygenase that catalyzes regio- and
CC stereospecific hydroxylation of cholesterol and its derivatives.
CC Hydroxylates (with R stereochemistry) the terminal methyl group of
CC cholesterol side-chain in a three step reaction to yield at first a C26
CC alcohol, then a C26 aldehyde and finally a C26 acid (By similarity).
CC Regulates cholesterol homeostasis by catalyzing the conversion of
CC excess cholesterol to bile acids via both the 'neutral' (classic) and
CC the 'acid' (alternative) pathways (PubMed:2722778). May also regulate
CC cholesterol homeostasis via generation of active oxysterols, which act
CC as ligands for NR1H2 and NR1H3 nuclear receptors, modulating the
CC transcription of genes involved in lipid metabolism. Plays a role in
CC cholestanol metabolism in the cerebellum. Similarly to cholesterol,
CC hydroxylates cholestanol and may facilitate sterol diffusion through
CC the blood-brain barrier to the systemic circulation for further
CC degradation. Also hydroxylates retinal 7-ketocholesterol, a noxious
CC oxysterol with pro-inflammatory and pro-apoptotic effects, and may play
CC a role in its elimination from the retinal pigment epithelium. May play
CC a redundant role in vitamin D biosynthesis. Catalyzes 25-hydroxylation
CC of vitamin D3 that is required for its conversion to a functionally
CC active form (By similarity). {ECO:0000250|UniProtKB:Q02318,
CC ECO:0000269|PubMed:2722778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 5 H(+) + 3 O2 +
CC 6 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-trihydroxy-
CC 5beta-cholestan-26-oate + 4 H2O + 6 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:34631, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16496, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58734; EC=1.14.15.15;
CC Evidence={ECO:0000269|PubMed:2722778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34632;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholestanol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-
CC 26-hydroxycholestanol + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:53812, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:86570,
CC ChEBI:CHEBI:137688; Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53813;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3beta-hydroxycholest-5-en-7-one-26-al + H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta-hydroxycholest-5-en-7-one-26-oate
CC + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:47380, Rhea:RHEA-
CC COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:87677, ChEBI:CHEBI:87678;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47381;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3beta,26-dihydroxycholest-5-en-7-one + 2 H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta-hydroxycholest-5-en-7-one-26-al +
CC 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:47376, Rhea:RHEA-
CC COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:87653, ChEBI:CHEBI:87677;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47377;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxocholesterol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC (25R)-3beta,26-dihydroxycholest-5-en-7-one + H2O + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:47344, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:64294,
CC ChEBI:CHEBI:87653; Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47345;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=calciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcidiol +
CC H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46588, Rhea:RHEA-
CC COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28940,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46589;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol + 2
CC H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-
CC trihydroxy-5beta-cholestan-26-al + 2 H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:40231, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:48939,
CC ChEBI:CHEBI:48940; Evidence={ECO:0000305|PubMed:2722778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40232;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-
CC cholest-5-ene-3beta,26-diol + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:46400, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:76591; Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46401;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3beta,4beta-dihydroxycholest-5-en-26-al + H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-3beta,4beta-dihydroxycholest-5-en-26-
CC oate + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46436,
CC Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:86115, ChEBI:CHEBI:86116;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46437;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-4beta,26-dihydroxycholesterol + 2 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta,4beta-dihydroxycholest-5-en-26-al + 2 H2O
CC + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:46432, Rhea:RHEA-
CC COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:86113, ChEBI:CHEBI:86115;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46433;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4beta-hydroxycholesterol + 2 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-4beta,26-dihydroxycholesterol + H2O + 2
CC oxidized [adrenodoxin]; Xref=Rhea:RHEA:46428, Rhea:RHEA-COMP:9998,
CC Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:85778, ChEBI:CHEBI:86113;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46429;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3beta-hydroxy-5-cholesten-26-al + H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta-hydroxy-5-cholestenoate + H2O + 2
CC oxidized [adrenodoxin]; Xref=Rhea:RHEA:45236, Rhea:RHEA-COMP:9998,
CC Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:86096, ChEBI:CHEBI:86098;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45237;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-cholest-5-ene-3beta,26-diol + 2 H(+) + O2 + 2 reduced
CC [adrenodoxin] = (25R)-3beta-hydroxy-5-cholesten-26-al + 2 H2O + 2
CC oxidized [adrenodoxin]; Xref=Rhea:RHEA:46092, Rhea:RHEA-COMP:9998,
CC Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:76591, ChEBI:CHEBI:86096;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46093;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al +
CC H(+) + O2 + 2 reduced [adrenodoxin] = (25R)-3alpha,7alpha,12alpha-
CC trihydroxy-5beta-cholestan-26-oate + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:34627, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:48940,
CC ChEBI:CHEBI:58734; Evidence={ECO:0000305|PubMed:2722778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34628;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + 2 H(+) + O2 + 2
CC reduced [adrenodoxin] = (25R)-5beta-cholestane-
CC 3alpha,7alpha,12alpha,26-tetrol + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:14373, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16496, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:48939; Evidence={ECO:0000250|UniProtKB:Q02318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14374;
CC Evidence={ECO:0000250|UniProtKB:Q02318};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:2722778};
CC -!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
CC {ECO:0000250|UniProtKB:Q02318}.
CC -!- PATHWAY: Steroid metabolism; cholesterol degradation.
CC {ECO:0000250|UniProtKB:Q02318}.
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000269|PubMed:2722778}.
CC -!- SUBUNIT: Interacts with HSP70; this interaction is required for initial
CC targeting to mitochondria. {ECO:0000250|UniProtKB:P17178}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P17178}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17178}. Note=Post-translationally targeted to
CC mitochondria. All three of the receptor proteins in the TOM complex,
CC TOMM70, TOMM20 and TOMM22 are required for the translocation across the
CC mitochondrial outer membrane. After translocation into the matrix,
CC associates with the inner membrane as a membrane extrinsic protein.
CC {ECO:0000250|UniProtKB:P17178}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest expression
CC in liver and duodenum, followed by adrenal gland and lung. Low
CC expression in kidney and spleen. {ECO:0000269|PubMed:2722778}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J04717; AAA31225.1; -; mRNA.
DR PIR; A33813; A33813.
DR RefSeq; NP_001177359.1; NM_001190430.1.
DR AlphaFoldDB; P17177; -.
DR SMR; P17177; -.
DR STRING; 9986.ENSOCUP00000002930; -.
DR GeneID; 100348736; -.
DR KEGG; ocu:100348736; -.
DR CTD; 1593; -.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; P17177; -.
DR OrthoDB; 871849at2759; -.
DR UniPathway; UPA00221; -.
DR UniPathway; UPA00955; -.
DR UniPathway; UPA01058; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0047103; F:3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047748; F:cholestanetetraol 26-dehydrogenase activity; IEA:RHEA.
DR GO; GO:0047749; F:cholestanetriol 26-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0031073; F:cholesterol 26-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0008123; F:cholesterol 7-alpha-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030343; F:vitamin D3 25-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036378; P:calcitriol biosynthetic process from calciol; ISS:UniProtKB.
DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol metabolism; Direct protein sequencing; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol metabolism; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2722778"
FT CHAIN 37..535
FT /note="Sterol 26-hydroxylase, mitochondrial"
FT /id="PRO_0000003620"
FT REGION 387..401
FT /note="Sterol-binding"
FT /evidence="ECO:0000255"
FT BINDING 480
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBG1"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBG1"
SQ SEQUENCE 535 AA; 60255 MW; CC44B9820E2FCCC2 CRC64;
MAALGCARLR WALLGPRVAG CGLCPQGARA KAAIPTALPA DEAAQAPGAG PGDRRRRRSL
EELPRLGQLR FFYQAFVQGY LLHLHKLQVL NKARYGPMWV SYLGPQLFVN LASAPLVETV
MRQEGKYPVR NDMQLWKEHR DHQDLAYGVF TTDGHDWYQL RQALNQRLLK PAEAALYTDA
LNEVIDSFVV RLDQLRAESA SGDQVPDMAD LLYHFALEAI CYILFEKRIG CLEASIPKDT
ENFIRSVGLM FQNSVYVTFL PKWTRPLLPF WKRYLDGWDT IFSFGKNLID QKLQEVVAQL
QSAGSDGVQV SGYLHSLLTS GQLSPREALG SLPELLLAGV DTTSNTLTWA LYHLSKNPEI
QAALRKEVVG VVAAGQVPQH KDFAHMPLLK AVLKETLRLY PVIPANSRII VDKEIEVGGF
LFPKNTQFVF CHYVTSRDPS TFSEPDTFWP YRWLRKGQPE TSKTQHPFGS VPFGYGVRAC
LGRRIAELEM QLLLARLIQR YELMLAPETG EVQSVARIVL VPNKKVGLRF LPTQR
