COX41_BOVIN
ID COX41_BOVIN Reviewed; 169 AA.
AC P00423; Q3SZS0; Q5E991;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide IV;
DE AltName: Full=Cytochrome c oxidase subunit IV isoform 1;
DE Short=COX IV-1;
DE Flags: Precursor;
GN Name=COX4I1; Synonyms=COX4;
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 [GENOMIC DNA].
RX PubMed=7557450; DOI=10.1016/0378-1119(95)00329-5;
RA Bachman N.J.;
RT "Isolation and characterization of the functional gene encoding bovine
RT cytochrome c oxidase subunit IV.";
RL Gene 162:313-318(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-104.
RX PubMed=6093095; DOI=10.1073/pnas.81.20.6295;
RA Lomax M.I., Bachman N.J., Nasoff M.S., Caruthers M.H., Grossman L.I.;
RT "Isolation and characterization of a cDNA clone for bovine cytochrome c
RT oxidase subunit IV.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6295-6299(1984).
RN [5]
RP PROTEIN SEQUENCE OF 23-109.
RC TISSUE=Heart;
RX PubMed=227780; DOI=10.1515/bchm2.1979.360.2.1385;
RA Sacher R., Steffens G.J., Buse G.;
RT "Studies on cytochrome c oxidase, VI. Polypeptide IV: the complete primary
RT structure.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1385-1392(1979).
RN [6]
RP PROTEIN SEQUENCE OF 23-109.
RC TISSUE=Heart;
RX PubMed=227779; DOI=10.1515/bchm2.1979.360.2.1377;
RA Sacher R., Buse G., Steffens G.J.;
RT "Studies on cytochrome c oxidase, V. Polypeptide IV: alignment and amino
RT acid sequences on cyanogen bromide fragments.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1377-1383(1979).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=19164527; DOI=10.1073/pnas.0806391106;
RA Aoyama H., Muramoto K., Shinzawa-Itoh K., Hirata K., Yamashita E.,
RA Tsukihara T., Ogura T., Yoshikawa S.;
RT "A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully
RT oxidized cytochrome c oxidase could suppress the proton pump.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2165-2169(2009).
RN [12]
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 [13]
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 [14]
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:P00424}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00424}.
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 PHB2; the interaction decreases in
CC absence of SPHK2 (By similarity). Interacts with AFG1L (By similarity).
CC Interacts with ABCB7; this interaction allows the regulation of
CC cellular iron homeostasis and cellular reactive oxygen species (ROS)
CC levels in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:P10888, ECO:0000250|UniProtKB:P13073,
CC ECO:0000250|UniProtKB:P19783, 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 -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC {ECO:0000305}.
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DR EMBL; L34015; AAA30461.1; -; Genomic_DNA.
DR EMBL; L34012; AAA30461.1; JOINED; Genomic_DNA.
DR EMBL; L34013; AAA30461.1; JOINED; Genomic_DNA.
DR EMBL; L34014; AAA30461.1; JOINED; Genomic_DNA.
DR EMBL; U11070; AAA93149.1; -; Genomic_DNA.
DR EMBL; U11067; AAA93149.1; JOINED; Genomic_DNA.
DR EMBL; U11068; AAA93149.1; JOINED; Genomic_DNA.
DR EMBL; U11069; AAA93149.1; JOINED; Genomic_DNA.
DR EMBL; BT021029; AAX09046.1; -; mRNA.
DR EMBL; BC102733; AAI02734.1; -; mRNA.
DR EMBL; K02064; AAA30463.1; -; mRNA.
DR PIR; A30618; OLBO4.
DR RefSeq; NP_001001439.1; NM_001001439.3.
DR RefSeq; XP_005218495.1; XM_005218438.1.
DR PDB; 1OCC; X-ray; 2.80 A; D/Q=23-169.
DR PDB; 1OCO; X-ray; 2.80 A; D/Q=23-169.
DR PDB; 1OCR; X-ray; 2.35 A; D/Q=23-169.
DR PDB; 1OCZ; X-ray; 2.90 A; D/Q=23-169.
DR PDB; 1V54; X-ray; 1.80 A; D/Q=23-169.
DR PDB; 1V55; X-ray; 1.90 A; D/Q=23-169.
DR PDB; 2DYR; X-ray; 1.80 A; D/Q=23-169.
DR PDB; 2DYS; X-ray; 2.20 A; D/Q=23-169.
DR PDB; 2EIJ; X-ray; 1.90 A; D/Q=23-169.
DR PDB; 2EIK; X-ray; 2.10 A; D/Q=23-169.
DR PDB; 2EIL; X-ray; 2.10 A; D/Q=23-169.
DR PDB; 2EIM; X-ray; 2.60 A; D/Q=23-169.
DR PDB; 2EIN; X-ray; 2.70 A; D/Q=23-169.
DR PDB; 2OCC; X-ray; 2.30 A; D/Q=23-169.
DR PDB; 2Y69; X-ray; 1.95 A; D/Q=1-169.
DR PDB; 2YBB; EM; 19.00 A; O=23-169.
DR PDB; 2ZXW; X-ray; 2.50 A; D/Q=23-169.
DR PDB; 3ABK; X-ray; 2.00 A; D/Q=23-169.
DR PDB; 3ABL; X-ray; 2.10 A; D/Q=23-169.
DR PDB; 3ABM; X-ray; 1.95 A; D/Q=23-169.
DR PDB; 3AG1; X-ray; 2.20 A; D/Q=23-169.
DR PDB; 3AG2; X-ray; 1.80 A; D/Q=23-169.
DR PDB; 3AG3; X-ray; 1.80 A; D/Q=23-169.
DR PDB; 3AG4; X-ray; 2.05 A; D/Q=23-169.
DR PDB; 3ASN; X-ray; 3.00 A; D/Q=23-169.
DR PDB; 3ASO; X-ray; 2.30 A; D/Q=23-169.
DR PDB; 3WG7; X-ray; 1.90 A; D/Q=23-169.
DR PDB; 3X2Q; X-ray; 2.00 A; D/Q=23-169.
DR PDB; 5B1A; X-ray; 1.50 A; D/Q=23-169.
DR PDB; 5B1B; X-ray; 1.60 A; D/Q=23-169.
DR PDB; 5B3S; X-ray; 1.68 A; D/Q=23-169.
DR PDB; 5GPN; EM; 5.40 A; 1=23-169.
DR PDB; 5IY5; X-ray; 2.00 A; D/Q=26-169.
DR PDB; 5LUF; EM; 9.10 A; 1=23-169.
DR PDB; 5W97; X-ray; 2.30 A; D/d=23-169.
DR PDB; 5WAU; X-ray; 1.95 A; D/d=23-169.
DR PDB; 5X19; X-ray; 2.20 A; D/Q=23-169.
DR PDB; 5X1B; X-ray; 2.40 A; D/Q=23-169.
DR PDB; 5X1F; X-ray; 2.20 A; D/Q=23-169.
DR PDB; 5XDQ; X-ray; 1.77 A; D/Q=23-169.
DR PDB; 5XDX; X-ray; 1.99 A; D/Q=23-169.
DR PDB; 5XTH; EM; 3.90 A; 0=26-169.
DR PDB; 5XTI; EM; 17.40 A; 0/B0=26-169.
DR PDB; 5Z84; X-ray; 1.85 A; D/Q=23-169.
DR PDB; 5Z85; X-ray; 1.85 A; D/Q=23-169.
DR PDB; 5Z86; X-ray; 1.85 A; D/Q=23-169.
DR PDB; 5ZCO; X-ray; 1.90 A; D/Q=23-169.
DR PDB; 5ZCP; X-ray; 1.65 A; D/Q=23-169.
DR PDB; 5ZCQ; X-ray; 1.65 A; D/Q=23-169.
DR PDB; 6J8M; X-ray; 1.90 A; D/Q=23-169.
DR PDB; 6JUW; X-ray; 1.80 A; D/Q=26-169.
DR PDB; 6JY3; X-ray; 1.85 A; D=23-169.
DR PDB; 6JY4; X-ray; 1.95 A; D=23-169.
DR PDB; 6NKN; X-ray; 2.50 A; D/Q=23-169.
DR PDB; 6NMF; X-ray; 2.80 A; D/Q=23-169.
DR PDB; 6NMP; X-ray; 2.90 A; D/Q=23-169.
DR PDB; 7COH; X-ray; 1.30 A; D/Q=23-169.
DR PDB; 7CP5; X-ray; 1.76 A; D/Q=26-169.
DR PDB; 7D5W; X-ray; 1.84 A; D/Q=26-169.
DR PDB; 7D5X; X-ray; 1.74 A; D/Q=26-169.
DR PDB; 7EV7; X-ray; 1.70 A; D/Q=23-169.
DR PDB; 7THU; X-ray; 1.93 A; DDD/QQQ=23-169.
DR PDB; 7TIE; X-ray; 1.90 A; DDD/QQQ=23-169.
DR PDB; 7TIH; X-ray; 2.35 A; DDD/QQQ=23-169.
DR PDB; 7TII; X-ray; 2.45 A; DDD/QQQ=23-169.
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; P00423; -.
DR SMR; P00423; -.
DR CORUM; P00423; -.
DR DIP; DIP-38979N; -.
DR IntAct; P00423; 3.
DR STRING; 9913.ENSBTAP00000049613; -.
DR iPTMnet; P00423; -.
DR PaxDb; P00423; -.
DR PeptideAtlas; P00423; -.
DR PRIDE; P00423; -.
DR Ensembl; ENSBTAT00000021397; ENSBTAP00000021397; ENSBTAG00000016079.
DR Ensembl; ENSBTAT00000053881; ENSBTAP00000049613; ENSBTAG00000016079.
DR GeneID; 281090; -.
DR KEGG; bta:281090; -.
DR CTD; 1327; -.
DR VEuPathDB; HostDB:ENSBTAG00000016079; -.
DR VGNC; VGNC:27634; COX4I1.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00390000002407; -.
DR HOGENOM; CLU_117340_1_0_1; -.
DR InParanoid; P00423; -.
DR OMA; ESYAEMN; -.
DR OrthoDB; 1591226at2759; -.
DR TreeFam; TF105061; -.
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; P00423; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000016079; Expressed in cardiac atrium and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IDA:MGI.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR Gene3D; 1.10.442.10; -; 1.
DR InterPro; IPR013288; Cyt_c_oxidase_su4.
DR InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR PANTHER; PTHR10707; PTHR10707; 1.
DR Pfam; PF02936; COX4; 1.
DR PRINTS; PR01873; CYTCOXIDASE4.
DR SUPFAM; SSF81406; SSF81406; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:227779,
FT ECO:0000269|PubMed:227780"
FT CHAIN 23..169
FT /note="Cytochrome c oxidase subunit 4 isoform 1,
FT mitochondrial"
FT /id="PRO_0000006083"
FT TOPO_DOM 23..98
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 125..169
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT MOD_RES 29
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 29
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13073"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10888"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10888"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13073"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19783"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1OCC"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 99..124
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 169 AA; 19572 MW; 76D2B2D15F8D02A1 CRC64;
MLATRVFSLI GRRAISTSVC VRAHGSVVKS EDYALPSYVD RRDYPLPDVA HVKNLSASQK
ALKEKEKASW SSLSIDEKVE LYRLKFKESF AEMNRSTNEW KTVVGAAMFF IGFTALLLIW
EKHYVYGPIP HTFEEEWVAK QTKRMLDMKV APIQGFSAKW DYDKNEWKK
