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Q37677 (COX2_SALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 2

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene names
Name:mt-co2
Synonyms:coii, coxii, mtco2
Encoded onMitochondrion
OrganismSalmo salar (Atlantic salmon)
Taxonomic identifier8030 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceInferred 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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactor

Copper A.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Cytochrome c oxidase subunit 2
PRO_0000183683

Regions

Topological domain1 – 2626Mitochondrial intermembrane Potential
Transmembrane27 – 4822Helical; Probable
Topological domain49 – 6214Mitochondrial matrix Potential
Transmembrane63 – 8220Helical; Probable
Topological domain83 – 230148Mitochondrial intermembrane Potential

Sites

Metal binding1611Copper A Probable
Metal binding1961Copper A Probable
Metal binding2001Copper A Probable
Metal binding2041Copper A Probable

Experimental info

Sequence conflict1751S → V in AAD04736. Ref.1
Sequence conflict2091I → V in AAB08524. Ref.3
Sequence conflict227 – 2304LEDA → TW in AAB08524. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q37677 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 405C95AA58112AF4

FASTA23026,016
        10         20         30         40         50         60 
MAHPSQLGFQ DAASPVMEEL LHFHDHALMI VLLISTLVLY IIVAMVSTKL TNKYILDSQE 

        70         80         90        100        110        120 
IEIVWTVLPA VILILIALPS LRILYLMDEI NDPHLTIKAM GHQWYWSYEY TDYEDLGFDS 

       130        140        150        160        170        180 
YMVPTQDLTP GQFRLLETDH RMVVPVESPI RVLVSAEDVL HSWAVPSLGV KMDASPGRLN 

       190        200        210        220        230 
QTAFIASRPG VFYGQCSEIC GANHSFMPIV VEAVPLEHFE KWSTMMLEDA 

« Hide

References

[1]"The complete mitochondrial DNA sequence of the Atlantic salmon, Salmo salar."
Hurst C.D., Bartlett S.E., Davidson W.S., Bruce I.J.
Gene 239:237-242(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"The complete mitochondrial genome sequence of a teleost, Salmo salar, and comparisons with other salmoniformes."
Arnason U., Johnsson E., Rasmussen A.S.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation of Atlantic Salmon (Salmo salar) cytochrome c oxidase subunit II gene (coxII)."
Hardiman G.T., Wolff J., Peden J., Gannon F.
J. Appl. Ichthyol. 10:64-68(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-230.
Tissue: Kidney.
[4]Hardiman G.T.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12143 Genomic DNA. Translation: AAD04736.1.
AF133701 Genomic DNA. Translation: AAF61381.1.
L04501 Genomic DNA. Translation: AAB08524.1.
PIRT09950.
RefSeqNP_008448.1. NC_001960.1.

3D structure databases

ProteinModelPortalQ37677.
SMRQ37677. Positions 1-227.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID808315.

Organism-specific databases

CTD4513.

Phylogenomic databases

HOVERGENHBG012727.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_SALSA
AccessionPrimary (citable) accession number: Q37677
Secondary accession number(s): Q9MPG8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: June 11, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families