COX3_BOVIN
ID COX3_BOVIN Reviewed; 261 AA.
AC P00415; Q576A5; Q8SE13;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3;
OS Bos taurus (Bovine).
OG Mitochondrion.
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 [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Hiendleder S., Wolf E.;
RT "Complete sequence of a new Bos taurus mitochondrial genome.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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:P00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
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). {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}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; V00654; CAA24003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF490528; AAM08332.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF490529; AAM08345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF493541; AAM12795.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF493542; AAM12808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF492351; AAQ06599.1; -; Genomic_DNA.
DR PIR; A00483; OTBO3.
DR PDB; 1OCC; X-ray; 2.80 A; C/P=1-261.
DR PDB; 1OCO; X-ray; 2.80 A; C/P=1-261.
DR PDB; 1OCR; X-ray; 2.35 A; C/P=1-261.
DR PDB; 1OCZ; X-ray; 2.90 A; C/P=1-261.
DR PDB; 1V54; X-ray; 1.80 A; C/P=1-261.
DR PDB; 1V55; X-ray; 1.90 A; C/P=1-261.
DR PDB; 2DYR; X-ray; 1.80 A; C/P=1-261.
DR PDB; 2DYS; X-ray; 2.20 A; C/P=1-261.
DR PDB; 2EIJ; X-ray; 1.90 A; C/P=1-261.
DR PDB; 2EIK; X-ray; 2.10 A; C/P=1-261.
DR PDB; 2EIL; X-ray; 2.10 A; C/P=1-261.
DR PDB; 2EIM; X-ray; 2.60 A; C/P=1-261.
DR PDB; 2EIN; X-ray; 2.70 A; C/P=1-261.
DR PDB; 2OCC; X-ray; 2.30 A; C/P=1-261.
DR PDB; 2Y69; X-ray; 1.95 A; C/P=1-261.
DR PDB; 2YBB; EM; 19.00 A; N=1-261.
DR PDB; 2ZXW; X-ray; 2.50 A; C/P=1-261.
DR PDB; 3ABK; X-ray; 2.00 A; C/P=1-261.
DR PDB; 3ABL; X-ray; 2.10 A; C/P=1-261.
DR PDB; 3ABM; X-ray; 1.95 A; C/P=1-261.
DR PDB; 3AG1; X-ray; 2.20 A; C/P=1-261.
DR PDB; 3AG2; X-ray; 1.80 A; C/P=1-261.
DR PDB; 3AG3; X-ray; 1.80 A; C/P=1-261.
DR PDB; 3AG4; X-ray; 2.05 A; C/P=1-261.
DR PDB; 3ASN; X-ray; 3.00 A; C/P=1-261.
DR PDB; 3ASO; X-ray; 2.30 A; C/P=1-261.
DR PDB; 3WG7; X-ray; 1.90 A; C/P=1-261.
DR PDB; 3X2Q; X-ray; 2.00 A; C/P=1-261.
DR PDB; 5B1A; X-ray; 1.50 A; C/P=1-261.
DR PDB; 5B1B; X-ray; 1.60 A; C/P=1-261.
DR PDB; 5B3S; X-ray; 1.68 A; C/P=1-261.
DR PDB; 5IY5; X-ray; 2.00 A; C/P=3-261.
DR PDB; 5LUF; EM; 9.10 A; z=1-261.
DR PDB; 5W97; X-ray; 2.30 A; C/c=1-261.
DR PDB; 5WAU; X-ray; 1.95 A; C/c=1-261.
DR PDB; 5X19; X-ray; 2.20 A; C/P=1-261.
DR PDB; 5X1B; X-ray; 2.40 A; C/P=1-261.
DR PDB; 5X1F; X-ray; 2.20 A; C/P=1-261.
DR PDB; 5XDQ; X-ray; 1.77 A; C/P=1-261.
DR PDB; 5XDX; X-ray; 1.99 A; C/P=2-261.
DR PDB; 5XTH; EM; 3.90 A; z=1-261.
DR PDB; 5XTI; EM; 17.40 A; Bz/z=1-261.
DR PDB; 5Z84; X-ray; 1.85 A; C/P=1-261.
DR PDB; 5Z85; X-ray; 1.85 A; C/P=1-261.
DR PDB; 5Z86; X-ray; 1.85 A; C/P=1-261.
DR PDB; 5ZCO; X-ray; 1.90 A; C/P=1-261.
DR PDB; 5ZCP; X-ray; 1.65 A; C/P=1-261.
DR PDB; 5ZCQ; X-ray; 1.65 A; C/P=1-261.
DR PDB; 6J8M; X-ray; 1.90 A; C/P=1-261.
DR PDB; 6JUW; X-ray; 1.80 A; C/P=3-261.
DR PDB; 6JY3; X-ray; 1.85 A; C=1-261.
DR PDB; 6JY4; X-ray; 1.95 A; C=1-261.
DR PDB; 6NKN; X-ray; 2.50 A; C/P=1-261.
DR PDB; 6NMF; X-ray; 2.80 A; C/P=1-261.
DR PDB; 6NMP; X-ray; 2.90 A; C/P=1-261.
DR PDB; 7COH; X-ray; 1.30 A; C/P=1-261.
DR PDB; 7CP5; X-ray; 1.76 A; C/P=3-261.
DR PDB; 7D5W; X-ray; 1.84 A; C/P=3-261.
DR PDB; 7D5X; X-ray; 1.74 A; C/P=3-261.
DR PDB; 7EV7; X-ray; 1.70 A; C/P=1-261.
DR PDB; 7THU; X-ray; 1.93 A; CCC/PPP=1-261.
DR PDB; 7TIE; X-ray; 1.90 A; CCC/PPP=1-261.
DR PDB; 7TIH; X-ray; 2.35 A; CCC/PPP=1-261.
DR PDB; 7TII; X-ray; 2.45 A; CCC/PPP=1-261.
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; 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; P00415; -.
DR SMR; P00415; -.
DR CORUM; P00415; -.
DR DIP; DIP-60938N; -.
DR IntAct; P00415; 1.
DR STRING; 9913.ENSBTAP00000053157; -.
DR TCDB; 3.D.4.7.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P00415; -.
DR eggNOG; KOG4664; Eukaryota.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; P00415; -.
DR BRENDA; 7.1.1.9; 908.
DR EvolutionaryTrace; P00415; -.
DR Proteomes; UP000009136; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183746"
FT TOPO_DOM 1..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 16..34
FT /note="Helical; Name=I"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 35..40
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 41..66
FT /note="Helical; Name=II"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 67..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 73..105
FT /note="Helical; Name=III"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 106..128
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 129..152
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 153..155
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 156..183
FT /note="Helical; Name=V"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 184..190
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 191..223
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 224..232
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 233..256
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 257..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT CONFLICT 238
FT /note="A -> G (in Ref. 1; CAA24003)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3AG1"
FT HELIX 16..37
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 41..65
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 73..106
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5X19"
FT HELIX 129..152
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 156..183
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 191..223
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 233..255
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 261 AA; 29933 MW; A521E76A9089B3FC CRC64;
MTHQTHAYHM VNPSPWPLTG ALSALLMTSG LTMWFHFNSM TLLMIGLTTN MLTMYQWWRD
VIRESTFQGH HTPAVQKGLR YGMILFIISE VLFFTGFFWA FYHSSLAPTP ELGGCWPPTG
IHPLNPLEVP LLNTSVLLAS GVSITWAHHS LMEGDRKHML QALFITITLG VYFTLLQASE
YYEAPFTISD GVYGSTFFVA TGFHGLHVII GSTFLIVCFF RQLKFHFTSN HHFGFEAAAW
YWHFVDVVWL FLYVSIYWWG S
