COX7C_BOVIN
ID COX7C_BOVIN Reviewed; 63 AA.
AC P00430; Q3T0U0; Q56K07;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cytochrome c oxidase subunit 7C, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIIA;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIc;
DE Flags: Precursor;
GN Name=COX7C; Synonyms=COX7CP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2554257; DOI=10.1093/nar/17.20.8376;
RA Aqua M.S., Lomax M.I., Schon E.A., Grossman L.I.;
RT "Nucleotide sequence of a cDNA for bovine cytochrome c oxidase subunit
RT VIIc.";
RL Nucleic Acids Res. 17:8376-8376(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1655579; DOI=10.1016/0378-1119(91)90252-7;
RA Aqua M.S., Bachman N.J., Lomax M.I., Grossman L.I.;
RT "Characterization and expression of a cDNA specifying subunit VIIc of
RT bovine cytochrome c oxidase.";
RL Gene 104:211-217(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9092564; DOI=10.1074/jbc.272.15.10175;
RA Seelan R.S., Grossman L.I.;
RT "Structural organization and promoter analysis of the bovine cytochrome c
RT oxidase subunit VIIc gene. A functional role for YY1.";
RL J. Biol. Chem. 272:10175-10181(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 17-63.
RC TISSUE=Heart;
RX PubMed=213363; DOI=10.1515/bchm2.1978.359.2.1005;
RA Buse G., Steffens G.J.;
RT "Studies on cytochrome c oxidase, II. The chemical constitution of a short
RT polypeptide from the beef heart enzyme.";
RL Hoppe-Seyler's Z. Physiol. Chem. 359:1005-1009(1978).
RN [7]
RP PROTEIN SEQUENCE OF 17-42.
RC TISSUE=Liver;
RX PubMed=2844245; DOI=10.1021/bi00413a048;
RA Yanamura W., Zhang Y.-Z., Takamiya S., Capaldi R.A.;
RT "Tissue-specific differences between heart and liver cytochrome c
RT oxidase.";
RL Biochemistry 27:4909-4914(1988).
RN [8]
RP SUBUNIT.
RX PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA Oosaki M., Ogura T., Tsukihara T.;
RT "Purification of active respiratory supercomplex from bovine heart
RT mitochondria enables functional studies.";
RL J. Biol. Chem. 291:4178-4184(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT A.";
RL Science 272:1136-1144(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10089392; DOI=10.1107/s0907444998006362;
RA Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT resolution.";
RL Acta Crystallogr. D 55:31-45(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10771420; DOI=10.1107/s0907444900002213;
RA Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT bovine heart at 2.9 A resolution.";
RL Acta Crystallogr. D 56:529-535(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "Bovine cytochrome c oxidase structures enable O2 reduction with
RT minimization of reactive oxygens and provide a proton-pumping gate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT collects four pumping proton equivalents in each catalytic cycle.";
RL J. Biol. Chem. 291:23882-23894(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(2019).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P04039}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04039}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC or a dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:26698328,
CC PubMed:27830641). Interacts with RAB5IF (By similarity).
CC {ECO:0000250|UniProtKB:P15954, ECO:0000269|PubMed:26698328,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- TISSUE SPECIFICITY: Liver, heart, muscle and brain, contain the same
CC isoform of COX VIIc, but at different concentrations.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIc family.
CC {ECO:0000305}.
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DR EMBL; X15725; CAB57793.1; -; mRNA.
DR EMBL; X58823; CAA41627.1; -; Genomic_DNA.
DR EMBL; U58655; AAC48719.1; -; Genomic_DNA.
DR EMBL; AY911320; AAW82088.1; -; mRNA.
DR EMBL; BC102263; AAI02264.1; -; mRNA.
DR PIR; JH0473; OSBO8A.
DR RefSeq; XP_005209785.1; XM_005209728.3.
DR RefSeq; XP_010797710.1; XM_010799408.2.
DR RefSeq; XP_010805898.1; XM_010807596.2.
DR RefSeq; XP_010807835.1; XM_010809533.1.
DR RefSeq; XP_010814166.1; XM_010815864.2.
DR RefSeq; XP_010821463.1; XM_010823161.2.
DR RefSeq; XP_010822314.2; XM_010824012.2.
DR RefSeq; XP_015319858.1; XM_015464372.1.
DR PDB; 1OCC; X-ray; 2.80 A; L/Y=17-63.
DR PDB; 1OCO; X-ray; 2.80 A; L/Y=17-63.
DR PDB; 1OCR; X-ray; 2.35 A; L/Y=17-63.
DR PDB; 1OCZ; X-ray; 2.90 A; L/Y=17-63.
DR PDB; 1V54; X-ray; 1.80 A; L/Y=17-63.
DR PDB; 1V55; X-ray; 1.90 A; L/Y=17-63.
DR PDB; 2DYR; X-ray; 1.80 A; L/Y=17-63.
DR PDB; 2DYS; X-ray; 2.20 A; L/Y=17-63.
DR PDB; 2EIJ; X-ray; 1.90 A; L/Y=17-63.
DR PDB; 2EIK; X-ray; 2.10 A; L/Y=17-63.
DR PDB; 2EIL; X-ray; 2.10 A; L/Y=17-63.
DR PDB; 2EIM; X-ray; 2.60 A; L/Y=17-63.
DR PDB; 2EIN; X-ray; 2.70 A; L/Y=17-63.
DR PDB; 2OCC; X-ray; 2.30 A; L/Y=17-63.
DR PDB; 2Y69; X-ray; 1.95 A; L/Y=1-63.
DR PDB; 2YBB; EM; 19.00 A; W=17-63.
DR PDB; 2ZXW; X-ray; 2.50 A; L/Y=17-63.
DR PDB; 3ABK; X-ray; 2.00 A; L/Y=17-63.
DR PDB; 3ABL; X-ray; 2.10 A; L/Y=17-63.
DR PDB; 3ABM; X-ray; 1.95 A; L/Y=17-63.
DR PDB; 3AG1; X-ray; 2.20 A; L/Y=17-63.
DR PDB; 3AG2; X-ray; 1.80 A; L/Y=17-63.
DR PDB; 3AG3; X-ray; 1.80 A; L/Y=17-63.
DR PDB; 3AG4; X-ray; 2.05 A; L/Y=17-63.
DR PDB; 3ASN; X-ray; 3.00 A; L/Y=17-63.
DR PDB; 3ASO; X-ray; 2.30 A; L/Y=17-63.
DR PDB; 3WG7; X-ray; 1.90 A; L/Y=17-63.
DR PDB; 3X2Q; X-ray; 2.00 A; L/Y=17-63.
DR PDB; 5B1A; X-ray; 1.50 A; L/Y=17-63.
DR PDB; 5B1B; X-ray; 1.60 A; L/Y=17-63.
DR PDB; 5B3S; X-ray; 1.68 A; L/Y=17-63.
DR PDB; 5GPN; EM; 5.40 A; 9=17-63.
DR PDB; 5IY5; X-ray; 2.00 A; L/Y=18-63.
DR PDB; 5LUF; EM; 9.10 A; 9=17-63.
DR PDB; 5W97; X-ray; 2.30 A; L/l=17-63.
DR PDB; 5WAU; X-ray; 1.95 A; L/l=17-63.
DR PDB; 5X19; X-ray; 2.20 A; L/Y=17-63.
DR PDB; 5X1B; X-ray; 2.40 A; L/Y=17-63.
DR PDB; 5X1F; X-ray; 2.20 A; L/Y=17-63.
DR PDB; 5XDQ; X-ray; 1.77 A; L/Y=17-63.
DR PDB; 5XDX; X-ray; 1.99 A; L/Y=17-63.
DR PDB; 5XTH; EM; 3.90 A; 8=17-63.
DR PDB; 5XTI; EM; 17.40 A; 8/B8=17-63.
DR PDB; 5Z84; X-ray; 1.85 A; L/Y=17-63.
DR PDB; 5Z85; X-ray; 1.85 A; L/Y=17-63.
DR PDB; 5Z86; X-ray; 1.85 A; L/Y=17-63.
DR PDB; 5ZCO; X-ray; 1.90 A; L/Y=17-63.
DR PDB; 5ZCP; X-ray; 1.65 A; L/Y=17-63.
DR PDB; 5ZCQ; X-ray; 1.65 A; L/Y=17-63.
DR PDB; 6J8M; X-ray; 1.90 A; L/Y=17-63.
DR PDB; 6JUW; X-ray; 1.80 A; L/Y=18-63.
DR PDB; 6JY3; X-ray; 1.85 A; L=17-63.
DR PDB; 6JY4; X-ray; 1.95 A; L=17-63.
DR PDB; 6NKN; X-ray; 2.50 A; L/Y=17-63.
DR PDB; 6NMF; X-ray; 2.80 A; L/Y=17-63.
DR PDB; 6NMP; X-ray; 2.90 A; L/Y=17-63.
DR PDB; 7COH; X-ray; 1.30 A; L/Y=17-63.
DR PDB; 7CP5; X-ray; 1.76 A; L/Y=18-63.
DR PDB; 7D5W; X-ray; 1.84 A; L/Y=18-63.
DR PDB; 7D5X; X-ray; 1.74 A; L/Y=18-63.
DR PDB; 7EV7; X-ray; 1.70 A; L/Y=17-63.
DR PDB; 7THU; X-ray; 1.93 A; LLL/YYY=17-63.
DR PDB; 7TIE; X-ray; 1.90 A; LLL/YYY=17-63.
DR PDB; 7TIH; X-ray; 2.35 A; LLL/YYY=17-63.
DR PDB; 7TII; X-ray; 2.45 A; LLL/YYY=17-63.
DR PDBsum; 1OCC; -.
DR PDBsum; 1OCO; -.
DR PDBsum; 1OCR; -.
DR PDBsum; 1OCZ; -.
DR PDBsum; 1V54; -.
DR PDBsum; 1V55; -.
DR PDBsum; 2DYR; -.
DR PDBsum; 2DYS; -.
DR PDBsum; 2EIJ; -.
DR PDBsum; 2EIK; -.
DR PDBsum; 2EIL; -.
DR PDBsum; 2EIM; -.
DR PDBsum; 2EIN; -.
DR PDBsum; 2OCC; -.
DR PDBsum; 2Y69; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 2ZXW; -.
DR PDBsum; 3ABK; -.
DR PDBsum; 3ABL; -.
DR PDBsum; 3ABM; -.
DR PDBsum; 3AG1; -.
DR PDBsum; 3AG2; -.
DR PDBsum; 3AG3; -.
DR PDBsum; 3AG4; -.
DR PDBsum; 3ASN; -.
DR PDBsum; 3ASO; -.
DR PDBsum; 3WG7; -.
DR PDBsum; 3X2Q; -.
DR PDBsum; 5B1A; -.
DR PDBsum; 5B1B; -.
DR PDBsum; 5B3S; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5W97; -.
DR PDBsum; 5WAU; -.
DR PDBsum; 5X19; -.
DR PDBsum; 5X1B; -.
DR PDBsum; 5X1F; -.
DR PDBsum; 5XDQ; -.
DR PDBsum; 5XDX; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR PDBsum; 5Z84; -.
DR PDBsum; 5Z85; -.
DR PDBsum; 5Z86; -.
DR PDBsum; 5ZCO; -.
DR PDBsum; 5ZCP; -.
DR PDBsum; 5ZCQ; -.
DR PDBsum; 6J8M; -.
DR PDBsum; 6JUW; -.
DR PDBsum; 6JY3; -.
DR PDBsum; 6JY4; -.
DR PDBsum; 6NKN; -.
DR PDBsum; 6NMF; -.
DR PDBsum; 6NMP; -.
DR PDBsum; 7COH; -.
DR PDBsum; 7CP5; -.
DR PDBsum; 7D5W; -.
DR PDBsum; 7D5X; -.
DR PDBsum; 7EV7; -.
DR PDBsum; 7THU; -.
DR PDBsum; 7TIE; -.
DR PDBsum; 7TIH; -.
DR PDBsum; 7TII; -.
DR AlphaFoldDB; P00430; -.
DR SMR; P00430; -.
DR CORUM; P00430; -.
DR DIP; DIP-60940N; -.
DR IntAct; P00430; 1.
DR STRING; 9913.ENSBTAP00000048302; -.
DR iPTMnet; P00430; -.
DR PaxDb; P00430; -.
DR PRIDE; P00430; -.
DR Ensembl; ENSBTAT00000052050; ENSBTAP00000048302; ENSBTAG00000039555.
DR Ensembl; ENSBTAT00000079150; ENSBTAP00000059946; ENSBTAG00000039555.
DR GeneID; 101902937; -.
DR GeneID; 101903567; -.
DR GeneID; 327718; -.
DR KEGG; bta:101902937; -.
DR KEGG; bta:101903567; -.
DR KEGG; bta:327718; -.
DR CTD; 1350; -.
DR VEuPathDB; HostDB:ENSBTAG00000039555; -.
DR eggNOG; KOG4527; Eukaryota.
DR GeneTree; ENSGT00390000018086; -.
DR HOGENOM; CLU_194769_0_0_1; -.
DR InParanoid; P00430; -.
DR OMA; MMAAFFG; -.
DR OrthoDB; 1642074at2759; -.
DR TreeFam; TF105069; -.
DR BRENDA; 7.1.1.9; 908.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P00430; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000039555; Expressed in cardiac ventricle and 107 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00929; Cyt_c_Oxidase_VIIc; 1.
DR Gene3D; 4.10.49.10; -; 1.
DR InterPro; IPR004202; COX7C/Cox8.
DR InterPro; IPR036636; COX7C/Cox8_sf.
DR PANTHER; PTHR13313; PTHR13313; 1.
DR Pfam; PF02935; COX7C; 1.
DR SUPFAM; SSF81427; SSF81427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:213363,
FT ECO:0000269|PubMed:2844245"
FT CHAIN 17..63
FT /note="Cytochrome c oxidase subunit 7C, mitochondrial"
FT /id="PRO_0000006162"
FT TOPO_DOM 17..33
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 34..60
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 61..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT MOD_RES 25
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17665"
FT MOD_RES 25
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17665"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 34..61
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 63 AA; 7331 MW; C6A2AD5CC4E63C0B CRC64;
MLGQSIRRFT TSVVRRSHYE EGPGKNIPFS VENKWRLLAM MTLFFGSGFA APFFIVRHQL
LKK
