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Q8WEW3

- COX1_SEPOF

UniProt

Q8WEW3 - COX1_SEPOF

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Protein

Cytochrome c oxidase subunit 1

Gene

COI

Organism
Sepia officinalis (Common cuttlefish)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Iron (heme A axial ligand)Curated

GO - Molecular functioni

  1. cytochrome-c oxidase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. aerobic respiration Source: InterPro
  2. oxidative phosphorylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00705.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene namesi
Name:COI
Encoded oniMitochondrion
OrganismiSepia officinalis (Common cuttlefish)
Taxonomic identifieri6610 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesSepiidaSepiinaSepiidaeSepia

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 4›4Mitochondrial matrixSequence Analysis
Transmembranei5 – 2723Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini28 – 4619Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei47 – 6923Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini70 – 8819Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei89 – 11123Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini112 – 13019Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei131 – 15323Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini154 – 17320Mitochondrial matrixSequence AnalysisAdd
BLAST
Transmembranei174 – 19623Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini197 – 22327Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-KW
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›223›223Cytochrome c oxidase subunit 1PRO_0000183416Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8WEW3.
SMRiQ8WEW3. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q8WEW3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
IGTLYFIFGI WSGLLGTSLS LMIRTELGKP GSLLNDDQLY NVVVTAHGFV
60 70 80 90 100
MIFFLVMPIM IGGFGNWLVP LMLGAPDMAF PRMNNMSFWL LPPSLTLLLA
110 120 130 140 150
SSAVESGAGT GWTVYPPLSS NISHAGPSVD LAIFSLHLAG VSSILGAINF
160 170 180 190 200
ITTIMNMRWE GLQMERLPLF VWSVFITAIL LLLSLPVLAG AITMLLTDRN
210 220
FNTTFFDPSG GGDPILYQHL FWF
Length:223
Mass (Da):24,364
Last modified:July 19, 2003 - v2
Checksum:i2C48081196B6CDF4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti25 – 251T → S in AAC95107. 1 PublicationCurated
Sequence conflicti32 – 321S → T in AAC95107. 1 PublicationCurated
Sequence conflicti50 – 501V → I in AAC95107. 1 PublicationCurated
Sequence conflicti100 – 1001A → S in AAC95107. 1 PublicationCurated
Sequence conflicti122 – 1221I → L in AAC95107. 1 PublicationCurated
Sequence conflicti155 – 1551M → L in AAC95107. 1 PublicationCurated
Sequence conflicti171 – 1711V → A in AAC95107. 1 PublicationCurated
Non-terminal residuei223 – 2231

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120630 Genomic DNA. Translation: AAL55480.1.
AF000062 Genomic DNA. Translation: AAC95107.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120630 Genomic DNA. Translation: AAL55480.1 .
AF000062 Genomic DNA. Translation: AAC95107.1 .

3D structure databases

ProteinModelPortali Q8WEW3.
SMRi Q8WEW3. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00705 .

Family and domain databases

Gene3Di 1.20.210.10. 1 hit.
InterProi IPR000883. COX1.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view ]
PANTHERi PTHR10422. PTHR10422. 1 hit.
Pfami PF00115. COX1. 1 hit.
[Graphical view ]
PRINTSi PR01165. CYCOXIDASEI.
SUPFAMi SSF81442. SSF81442. 1 hit.
PROSITEi PS50855. COX1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "On bivalve phylogeny: a high-level phylogeny of the mollusk class Bivalvia based on a combined analysis of morphology and DNA sequence data."
    Giribet G., Wheeler W.C.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Phylogenetic analysis of cytochrome c oxidase I sequences to determine higher-level relationships within the coleoid cephalopods."
    Carlini D.B., Graves J.E.
    Bull. Mar. Sci. 64:57-76(1999)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-221.

Entry informationi

Entry nameiCOX1_SEPOF
AccessioniPrimary (citable) accession number: Q8WEW3
Secondary accession number(s): Q9ZYY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 19, 2003
Last modified: October 29, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3