ID Q85AE9_ECHMA Unreviewed; 361 AA. AC Q85AE9; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 11-DEC-2019, entry version 73. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; OS Echinometra mathaei (Rock boring urchin) (Echinus mathaei). OG Mitochondrion {ECO:0000313|EMBL:AAP31634.1}. OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea; OC Euechinoidea; Echinacea; Echinoida; Echinometridae; Echinometra. OX NCBI_TaxID=31178 {ECO:0000313|EMBL:AAP31634.1}; RN [1] {ECO:0000313|EMBL:AAP31634.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MDm2 {ECO:0000313|EMBL:AAP31634.1}, MDm3 RC {ECO:0000313|EMBL:AAP31635.1}, MDm7 {ECO:0000313|EMBL:AAP31637.1}, and RC MDm8 {ECO:0000313|EMBL:AAP31638.1}; RX PubMed=12964987; DOI=10.1098/rspb.2003.2395; RA Landry C., Geyer L.B., Arakaki Y., Uehara T., Palumbi S.R.; RT "Recent speciation in the Indo-West Pacific: rapid evolution of gamete RT recognition and sperm morphology in cryptic species of sea urchin."; RL Proc. R. Soc. B 270:1839-1847(2003). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY262912; AAP31634.1; -; Genomic_DNA. DR EMBL; AY262913; AAP31635.1; -; Genomic_DNA. DR EMBL; AY262915; AAP31637.1; -; Genomic_DNA. DR EMBL; AY262916; AAP31638.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 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; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AAP31634.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 30..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 76..100 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 120..143 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 155..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 215..233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 240..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..298 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 310..331 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 343..360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..361 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAP31634.1" FT NON_TER 361 FT /evidence="ECO:0000313|EMBL:AAP31634.1" SQ SEQUENCE 361 AA; 39192 MW; D1082528B56F0693 CRC64; VGTAMSVIIR AELAQPGSLL NDDQIYNXVV TAHALVMIFF MVMPIMIGGF GNWLIPLMIG APDMAFPRMN NMSFWLVPPS FILLLASAGV ESGAGTGWTI YPPLSSNIAH AGGSVDLAIF SLHLAGASSI LASINFITTI INMRTPGMSF DRLPLFVWSV FVTAFLLLLS LPVLAGAITM LLTDRNINTT FFDPAGGGDP ILFQHLFXXX XHPEVYILIL PGFGMISHVI AHYSGKREPF GYLGMVYAMI AIGVLGFLVW AHHMFTVGMD VDTRAYFTAA TMIIAVPTGI KVFSWMATLQ GSNLQWETPL FWALGFVFLF TLGGLTGIVL ANSSIDVVLH DTYYVVAHFH YVLSMGAVFA I //