ID   COX1_RAT                Reviewed;         514 AA.
AC   P05503;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=Mt-co1 {ECO:0000312|RGD:621871}; Synonyms=Coi, Mtco1;
OS   Rattus norvegicus (Rat).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar;
RX   PubMed=2504926; DOI=10.1007/bf02602930;
RA   Gadaleta G., Pepe G., de Candia G., Quagliariello C., Sbisa E., Saccone C.;
RT   "The complete nucleotide sequence of the Rattus norvegicus mitochondrial
RT   genome: cryptic signals revealed by comparative analysis between
RT   vertebrates.";
RL   J. Mol. Evol. 28:497-516(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Grosskopf R., Feldmann H.;
RT   "Analysis of a DNA segment from rat liver mitochondria containing the genes
RT   for the cytochrome oxidase subunits I, II, II, ATPase subunit 6, and
RT   several tRNA genes.";
RL   Curr. Genet. 4:151-158(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX   PubMed=6300770; DOI=10.1093/nar/11.6.1635;
RA   Taira M., Yoshida E., Kobayashi M., Yaginuma K., Koike K.;
RT   "Tumor-associated mutations of rat mitochondrial transfer RNA genes.";
RL   Nucleic Acids Res. 11:1635-1643(1983).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 216-514.
RC   TISSUE=Sertoli cell;
RX   PubMed=1664046; DOI=10.1210/mend-5-11-1669;
RA   Ku C.Y., Lu Q., Ussuf K.K., Weinstock G.M., Sanborn B.M.;
RT   "Hormonal regulation of cytochrome oxidase subunit messenger RNAs in rat
RT   Sertoli cells.";
RL   Mol. Endocrinol. 5:1669-1676(1991).
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:P00401}.
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:P00401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00396};
CC       Note=Binds 2 heme A groups non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:P00396};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00396};
CC       Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00396};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00401}.
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 COX4I, COX5A,
CC       COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC       are encoded in the nuclear genome. The complex exists as a monomer or a
CC       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)) (By similarity).
CC       As a newly synthesized protein, rapidly incorporates into a multi-
CC       subunit assembly intermediate in the inner membrane, called MITRAC
CC       (mitochondrial translation regulation assembly intermediate of
CC       cytochrome c oxidase) complex, whose core components are COA3/MITRAC12
CC       and COX14. Within the MITRAC complex, interacts with COA3 and with
CC       SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly
CC       synthesized MT-CO1 and prevents its premature turnover. Interacts with
CC       TMEM177 in a COX20-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:P00395, ECO:0000250|UniProtKB:P00396}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00396}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X14848; CAA32956.1; -; Genomic_DNA.
DR   EMBL; J01435; AAD15016.1; -; Genomic_DNA.
DR   EMBL; AY172581; AAN77596.1; -; Genomic_DNA.
DR   EMBL; V00676; CAA24046.1; -; Genomic_DNA.
DR   EMBL; V00678; CAA24050.1; -; Genomic_DNA.
DR   EMBL; S79304; AAB21298.2; -; mRNA.
DR   PIR; S04749; S04749.
DR   RefSeq; AP_004894.1; AC_000022.2.
DR   RefSeq; YP_665631.1; NC_001665.2.
DR   AlphaFoldDB; P05503; -.
DR   SMR; P05503; -.
DR   CORUM; P05503; -.
DR   IntAct; P05503; 1.
DR   MINT; P05503; -.
DR   STRING; 10116.ENSRNOP00000039048; -.
DR   GlyGen; P05503; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; P05503; -.
DR   SwissPalm; P05503; -.
DR   jPOST; P05503; -.
DR   PaxDb; 10116-ENSRNOP00000039048; -.
DR   Ensembl; ENSRNOT00000050156.3; ENSRNOP00000039048.3; ENSRNOG00000034234.3.
DR   GeneID; 26195; -.
DR   KEGG; rno:26195; -.
DR   AGR; RGD:621871; -.
DR   CTD; 4512; -.
DR   RGD; 621871; Mt-co1.
DR   eggNOG; KOG4769; Eukaryota.
DR   GeneTree; ENSGT00390000001518; -.
DR   HOGENOM; CLU_011899_7_3_1; -.
DR   InParanoid; P05503; -.
DR   OMA; WAMMSIG; -.
DR   OrthoDB; 5387269at2759; -.
DR   Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-RNO-611105; Respiratory electron transport.
DR   Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:P05503; -.
DR   Proteomes; UP000002494; Mitochondrion.
DR   Bgee; ENSRNOG00000034234; Expressed in esophagus and 18 other cell types or tissues.
DR   ExpressionAtlas; P05503; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:RGD.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; ISO:RGD.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR   GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
DR   Genevisible; P05503; RN.
PE   2: Evidence at transcript level;
KW   Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Sodium; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183406"
FT   TOPO_DOM        1..11
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        12..40
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        41..50
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        51..86
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        87..94
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        95..117
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        118..140
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        141..170
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        171..182
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        183..212
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        213..227
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        228..261
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        262..269
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        270..286
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        287..298
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        299..327
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        328..335
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        336..357
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        358..370
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        371..400
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        401..406
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        407..433
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        434..446
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        447..478
FT                   /note="Helical; Name=XII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        479..514
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         40
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         45
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         61
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         240
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         244
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         290
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         291
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with MT-CO2"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         369
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with MT-CO2"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         376
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_note="high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         378
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         441
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   CROSSLNK        240..244
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   CONFLICT        2
FT                   /note="L -> F (in Ref. 1; CAA32956, 2; AAD15016 and 4;
FT                   CAA24046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        5
FT                   /note="R -> G (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="H -> P (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="P -> L (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="I -> L (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="A -> V (in Ref. 1; CAA32956 and 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216..218
FT                   /note="NTT -> EFP (in Ref. 5; AAB21298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="D -> G (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="P -> L (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="G -> E (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="A -> T (in Ref. 1; CAA32956 and 2; AAD15016)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="G -> C (in Ref. 2; AAD15016 and 5; AAB21298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="H -> L (in Ref. 2; AAD15016)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  56845 MW;  68FF852A1E7D6D70 CRC64;
     MLVNRWLFST NHKDIGTLYL LFGAWAGMVG TALSILIRAE LGQPGALLGD DQIYNVIVTA
     HAFVMIFFMV MPMMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA
     GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMTQYQ
     TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
     PEVYILILPG FGIISHVVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGLDVD
     TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTV GGLTGIVLSN
     SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF SGYTLNDTWA KAHFAIMFVG
     VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW NTVSSMGSFI SLTAVLVMIF MIWEAFASKR
     EVLSISYSST NLEWLHGCPP PYHTFEEPSY VKVK
//