Reviewed, UniProtKB/Swiss-Prot P48866 (COX1_CHOCR)

Names and origin

Protein names

Recommended name:
    Cytochrome c oxidase subunit 1
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I

Gene names

Name:

COX1

Encoded on

Mitochondrion

Organism

Chondrus crispus (Carragheen)

Taxonomic identifier

2769 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Florideophyceae › Gigartinales › Gigartinaceae › Chondrus

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Catalytic activity	4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
Pathway	Energy metabolism; oxidative phosphorylation.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: InterPro respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 532	532	Cytochrome c oxidase subunit 1		PRO_0000183313
Regions
	Transmembrane	23 – 43	21	Potential
	Transmembrane	71 – 91	21	Potential
	Transmembrane	110 – 130	21	Potential
	Transmembrane	153 – 173	21	Potential
	Transmembrane	191 – 211	21	Potential
	Transmembrane	242 – 262	21	Potential
	Transmembrane	274 – 294	21	Potential
	Transmembrane	315 – 335	21	Potential
	Transmembrane	345 – 365	21	Potential
	Transmembrane	384 – 404	21	Potential
	Transmembrane	421 – 441	21	Potential
	Transmembrane	463 – 483	21	Potential
Sites
	Metal binding	69	1	Iron (heme A axial ligand) Probable
	Metal binding	248	1	Copper B Probable
	Metal binding	252	1	Copper B Probable
	Metal binding	297	1	Copper B Probable
	Metal binding	298	1	Copper B Probable
	Metal binding	383	1	Iron (heme A3 axial ligand) Probable
	Metal binding	385	1	Iron (heme A axial ligand) Probable
Amino acid modifications
	Cross-link	248 ↔ 252		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P48866-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: A0F18B4B35BA636F	FASTA	532	59,291
	10 20 30 40 50 60 MQSFFTQWIS RWIFSTNHKD IGTLYLIFGA FSGVLGGCMS MLIRMELAQP SNHLLLGNHQ 70 80 90 100 110 120 IYNVLITAHA FLMIFFMVMP VMIGGFGNWL VPIMIGSPDM AFPRLNNISF WLLPPSLCLL 130 140 150 160 170 180 LMSALVEVGV GTGWTVYPPL SSIQSHSGGA VDLAIFSLHI SGASSILGAV NFISTILNMR 190 200 210 220 230 240 SPGQSMYRIP LFVWSILVTA FLLLLAVPVL AGAITMLLTD RNFNTSFFDA SGGGDPILYQ 250 260 270 280 290 300 HLFWFFGHPE VYILILPGFG MISHIVSTFS RKPVFGYIGM VYAMVSIGVL GFIVWAHHMY 310 320 330 340 350 360 TVGLDVDTRA YFTAATMIIA VPTGIKIFSW IATIWEGSIH LKTPMLFAIG FIFLFTIGGL 370 380 390 400 410 420 TGIVLANSGL DISLHDTYYV VAHFHYVLSM GAVFAIFAGF YYWFGKITGL QYPETLGQIH 430 440 450 460 470 480 FWSTFIGVNL TFMPMHFLGL AGMPRRIPDY PDAYAGWNLI ASYGSYIALF STLFFFYIVF 490 500 510 520 530 VSLTSNNPCT NFPWEFNKSK TYGVSTLEWI VTSPPAYHTF EEMPLIYETK SN

References

[1]

"Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus (Gigartinales). Gene content and genome organization." Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M., Kloareg B. J. Mol. Biol. 250:484-495(1995) [PubMed: 7616569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Apices.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z47547 Genomic DNA. Translation: CAA87603.1.
PIR	S59087.
RefSeq	NP_062482.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
ModBase	Search...
Genome annotation databases
GeneID	809360.
Enzyme and pathway databases
BRENDA	1.9.3.1. 190989.
Family and domain databases
InterPro	IPR000883. Cyt_c_oxidase_su1. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
TIGRFAMs	TIGR02891. CtaD_CoxA. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_CHOCR

Accession

Primary (citable) accession number: P48866

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	October 13, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)