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Cytochrome b559 subunit alpha (PSII reaction center subunit V)

 PSBE_THEEB              Reviewed;          84 AA.
Q8DIP0;
30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 117.
RecName: Full=Cytochrome b559 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00642};
AltName: Full=PSII reaction center subunit V {ECO:0000255|HAMAP-Rule:MF_00642};
Name=psbE {ECO:0000255|HAMAP-Rule:MF_00642};
OrderedLocusNames=tsr1541;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[2]
PROTEIN SEQUENCE OF 2-8, CLEAVAGE OF INITIATOR METHIONINE, AND
SUBCELLULAR LOCATION.
PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y.,
Satoh K., Sugiura M.;
"Ycf12 is a core subunit in the photosystem II complex.";
Biochim. Biophys. Acta 1767:1269-1275(2007).
[3]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
DOI=10.1039/B406989G;
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
"Crystal structure of cyanobacterial photosystem II at 3.2 A
resolution: a closer look at the Mn-cluster.";
Phys. Chem. Chem. Phys. 6:4733-4736(2004).
[4]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14764885; DOI=10.1126/science.1093087;
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
"Architecture of the photosynthetic oxygen-evolving center.";
Science 303:1831-1838(2004).
[5]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16049768; DOI=10.1007/s11120-004-7077-x;
Kern J., Loll B., Zouni A., Saenger W., Irrgang K.D., Biesiadka J.;
"Cyanobacterial photosystem II at 3.2 A resolution -- the
plastoquinone binding pockets.";
Photosyn. Res. 84:153-159(2005).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=16355230; DOI=10.1038/nature04224;
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
"Towards complete cofactor arrangement in the 3.0 A resolution
structure of photosystem II.";
Nature 438:1040-1044(2005).
[7]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16172937; DOI=10.1007/s11120-005-4117-0;
Loll B., Kern J., Zouni A., Saenger W., Biesiadka J., Irrgang K.D.;
"The antenna system of photosystem II from Thermosynechococcus
elongatus at 3.2 A resolution.";
Photosyn. Res. 86:175-184(2005).
[8]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
TOPOLOGY.
STRAIN=BP-1;
PubMed=19219048; DOI=10.1038/nsmb.1559;
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
"Cyanobacterial photosystem II at 2.9-A resolution and the role of
quinones, lipids, channels and chloride.";
Nat. Struct. Mol. Biol. 16:334-342(2009).
[9]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 2-84 IN PHOTOSYSTEM II WITH
HEME, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
STRAIN=BP-1;
PubMed=20558739; DOI=10.1074/jbc.M110.127589;
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
Zouni A.;
"Crystal structure of monomeric photosystem II from
Thermosynechococcus elongatus at 3.6 A resolution.";
J. Biol. Chem. 285:26255-26262(2010).
[10]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=21367867; DOI=10.1074/jbc.M110.215970;
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J.,
Kern J., Muh F., Dau H., Saenger W., Zouni A.;
"Structural basis of cyanobacterial photosystem II inhibition by the
herbicide terbutryn.";
J. Biol. Chem. 286:15964-15972(2011).
[11]
X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 2-84 IN PHOTOSYSTEM II WITH
HEME, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=22665786; DOI=10.1073/pnas.1204598109;
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J.,
McQueen T.A., DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A.,
Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H.,
White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J.,
Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J.,
Yachandra V.K.;
"Room temperature femtosecond X-ray diffraction of photosystem II
microcrystals.";
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
[12]
X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=23413188; DOI=10.1126/science.1234273;
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
Glockner C., Hellmich J., Laksmono H., Sierra R.G.,
Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D.,
Milathianaki D., Fry A.R., Miahnahri A., Schafer D.W.,
Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C.,
Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H.,
White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J.,
Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K.,
Bergmann U., Yano J.;
"Simultaneous femtosecond X-ray spectroscopy and diffraction of
photosystem II at room temperature.";
Science 340:491-495(2013).
[13]
X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 4-84 IN PHOTOSYSTEM II WITH
HEME, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25043005; DOI=10.1038/nature13453;
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A.,
Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D.,
Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A.,
Aquila A.L., Deponte D., Kirian R.A., Bari S., Bergkamp J.J.,
Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E.,
Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S.,
Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V.,
Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S.,
Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C.,
Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S.,
Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C.,
Fromme P.;
"Serial time-resolved crystallography of photosystem II using a
femtosecond X-ray laser.";
Nature 513:261-265(2014).
[14]
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25006873; DOI=10.1038/ncomms5371;
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S.,
Stan C.A., Gloeckner C., Lampe A., DiFiore D., Milathianaki D.,
Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D.,
Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M.,
Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A.,
Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.;
"Taking snapshots of photosynthetic water oxidation using femtosecond
X-ray diffraction and spectroscopy.";
Nat. Commun. 5:4371-4371(2014).
-!- FUNCTION: This b-type cytochrome is tightly associated with the
reaction center of photosystem II (PSII). PSII is a light-driven
water:plastoquinone oxidoreductase that uses light energy to
abstract electrons from H(2)O, generating O(2) and a proton
gradient subsequently used for ATP formation. It consists of a
core antenna complex that captures photons, and an electron
transfer chain that converts photonic excitation into a charge
separation. {ECO:0000255|HAMAP-Rule:MF_00642,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:25006873}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|HAMAP-Rule:MF_00642,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16049768,
ECO:0000269|PubMed:16172937, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3};
Note=With its partner (PsbF) binds heme. PSII binds additional
chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
Rule:MF_00642, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3};
-!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit.
Cyanobacterial PSII is composed of 1 copy each of membrane
proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ,
PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3
peripheral proteins PsbO, PsbU, PsbV and a large number of
cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
Rule:MF_00642, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}; Single-pass
membrane protein {ECO:0000255|HAMAP-Rule:MF_00642,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16049768,
ECO:0000269|PubMed:16172937, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3}.
-!- MASS SPECTROMETRY: Mass=9446; Mass_error=6; Method=MALDI; Range=2-
84; Evidence={ECO:0000269|PubMed:19219048};
-!- MASS SPECTROMETRY: Mass=9440; Method=MALDI; Range=2-84;
Evidence={ECO:0000269|PubMed:20558739};
-!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
Rule:MF_00642}.
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EMBL; BA000039; BAC09093.1; -; Genomic_DNA.
RefSeq; NP_682331.1; NC_004113.1.
RefSeq; WP_011057381.1; NC_004113.1.
PDB; 1S5L; X-ray; 3.50 A; E/e=1-84.
PDB; 1W5C; X-ray; 3.20 A; E/K=1-84.
PDB; 2AXT; X-ray; 3.00 A; E/e=1-84.
PDB; 3KZI; X-ray; 3.60 A; E=2-84.
PDB; 4FBY; X-ray; 6.56 A; E/R=2-84.
PDB; 4IXQ; X-ray; 5.70 A; E/e=1-84.
PDB; 4IXR; X-ray; 5.90 A; E/e=1-84.
PDB; 4PBU; X-ray; 5.00 A; E/e=4-84.
PDB; 4PJ0; X-ray; 2.44 A; E/e=1-84.
PDB; 4RVY; X-ray; 5.50 A; E/e=4-84.
PDB; 4TNH; X-ray; 4.90 A; E/e=1-84.
PDB; 4TNI; X-ray; 4.60 A; E/e=1-84.
PDB; 4TNJ; X-ray; 4.50 A; E/e=1-84.
PDB; 4TNK; X-ray; 5.20 A; E/e=1-84.
PDB; 4V62; X-ray; 2.90 A; AE/BE=1-84.
PDB; 4V82; X-ray; 3.20 A; AE/BE=1-84.
PDB; 5E79; X-ray; 3.50 A; E/e=4-84.
PDB; 5E7C; X-ray; 4.50 A; E/e=4-84.
PDB; 5H2F; X-ray; 2.20 A; E/e=5-84.
PDB; 5KAF; X-ray; 3.00 A; E/e=1-84.
PDB; 5KAI; X-ray; 2.80 A; E/e=1-84.
PDB; 5MX2; X-ray; 2.20 A; E/e=1-84.
PDB; 5TIS; X-ray; 2.25 A; E/e=1-84.
PDBsum; 1S5L; -.
PDBsum; 1W5C; -.
PDBsum; 2AXT; -.
PDBsum; 3KZI; -.
PDBsum; 4FBY; -.
PDBsum; 4IXQ; -.
PDBsum; 4IXR; -.
PDBsum; 4PBU; -.
PDBsum; 4PJ0; -.
PDBsum; 4RVY; -.
PDBsum; 4TNH; -.
PDBsum; 4TNI; -.
PDBsum; 4TNJ; -.
PDBsum; 4TNK; -.
PDBsum; 4V62; -.
PDBsum; 4V82; -.
PDBsum; 5E79; -.
PDBsum; 5E7C; -.
PDBsum; 5H2F; -.
PDBsum; 5KAF; -.
PDBsum; 5KAI; -.
PDBsum; 5MX2; -.
PDBsum; 5TIS; -.
ProteinModelPortal; Q8DIP0; -.
SMR; Q8DIP0; -.
DIP; DIP-48491N; -.
IntAct; Q8DIP0; 1.
STRING; 197221.tsr1541; -.
EnsemblBacteria; BAC09093; BAC09093; BAC09093.
GeneID; 1011075; -.
KEGG; tel:tsr1541; -.
PATRIC; fig|197221.4.peg.1617; -.
eggNOG; ENOG4105NT3; Bacteria.
eggNOG; ENOG4111X01; LUCA.
HOGENOM; HOG000254797; -.
KO; K02707; -.
OMA; VRYWVIH; -.
OrthoDB; POG091H14HV; -.
BioCyc; TELO197221:G1G3I-1568-MONOMER; -.
EvolutionaryTrace; Q8DIP0; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
Gene3D; 1.20.5.860; -; 1.
HAMAP; MF_00642; PSII_PsbE; 1.
InterPro; IPR006217; PSII_cyt_b559_asu.
InterPro; IPR037025; PSII_cyt_b559_asu_sf.
InterPro; IPR006216; PSII_cyt_b559_CS.
InterPro; IPR013081; PSII_cyt_b559_N.
InterPro; IPR013082; PSII_cytb559_asu_lum.
PANTHER; PTHR33391:SF1; PTHR33391:SF1; 1.
Pfam; PF00283; Cytochrom_B559; 1.
Pfam; PF00284; Cytochrom_B559a; 1.
PIRSF; PIRSF000036; PsbE; 1.
TIGRFAMs; TIGR01332; cyt_b559_alpha; 1.
PROSITE; PS00537; CYTOCHROME_B559; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Electron transport; Heme; Iron; Membrane; Metal-binding;
Photosynthesis; Photosystem II; Reference proteome; Thylakoid;
Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17935689,
ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739}.
CHAIN 2 84 Cytochrome b559 subunit alpha.
/FTId=PRO_0000200343.
TOPO_DOM 2 19 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
TRANSMEM 20 35 Helical. {ECO:0000269|PubMed:19219048}.
TOPO_DOM 36 84 Lumenal. {ECO:0000269|PubMed:19219048}.
METAL 23 23 Iron (heme axial ligand); shared with
beta subunit. {ECO:0000255|HAMAP-
Rule:MF_00642,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
HELIX 10 15 {ECO:0000244|PDB:5H2F}.
HELIX 17 39 {ECO:0000244|PDB:5H2F}.
HELIX 42 47 {ECO:0000244|PDB:5H2F}.
STRAND 54 56 {ECO:0000244|PDB:5H2F}.
STRAND 69 71 {ECO:0000244|PDB:2AXT}.
HELIX 72 81 {ECO:0000244|PDB:5H2F}.
SEQUENCE 84 AA; 9573 MW; 19C7A074624D937F CRC64;
MAGTTGERPF SDIITSVRYW VIHSITIPAL FIAGWLFVST GLAYDVFGTP RPDSYYAQEQ
RSIPLVTDRF EAKQQVETFL EQLK


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E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
EIAAB10217 Complex III subunit 4,Complex III subunit IV,Cyc1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Mouse,Mus musculus,Ubiquinol-cytochrome-c reductase comple
EIAAB08789 COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Oryctolagus cuniculus,Rabb
EIAAB08785 Bos taurus,Bovine,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,IX,VIIIb
EIAAB10236 COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,MTCYB,MT-CYB,Pig,Sus scrofa,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
EIAAB08788 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Rat,Rattus norvegicus
EIAAB10216 Bos taurus,Bovine,Complex III subunit 4,Complex III subunit IV,CYC1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Ubiquinol-cytochrome-c reductase complex
EIAAB08787 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Mouse,Mus musculus
EIAAB10099 Bos taurus,Bovine,COX7A,COX7A1,COX7AH,Cytochrome c oxidase subunit 7A1, mitochondrial,Cytochrome c oxidase subunit VIIa-H,Cytochrome c oxidase subunit VIIa-heart,Cytochrome c oxidase subunit VIIa-M,Cy


 

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