COX5B_VULVU
ID COX5B_VULVU Reviewed; 128 AA.
AC Q710D6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial {ECO:0000250|UniProtKB:P00428};
DE AltName: Full=Cytochrome c oxidase polypeptide Vb {ECO:0000303|PubMed:15866998};
DE AltName: Full=Sperm protein 8 {ECO:0000312|EMBL:CAD19164.1};
DE AltName: Full=fSP8 {ECO:0000303|PubMed:15866998};
DE Flags: Precursor;
GN Name=COX5B {ECO:0000250|UniProtKB:P00428};
GN Synonyms=SP8 {ECO:0000312|EMBL:CAD19164.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD19164.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-44, TISSUE SPECIFICITY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Testis {ECO:0000312|EMBL:CAD19164.1};
RX PubMed=15866998; DOI=10.2164/jandrol.04101;
RA Verdier Y., Farre G., Rouet N., Kele Z., Janaky T., Boue F., Borregaard N.,
RA Kjeldsen L.;
RT "Cloning and sequencing of cDNA encoding for the testis-specific fox
RT (Vulpes vulpes) sperm polypeptide Vb of the cytochrome C oxidase.";
RL J. Androl. 26:319-327(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY 2D-PAGE.
RX PubMed=12065460;
RA Verdier Y., Rouet N., Artois M., Boue F.;
RT "Partial characterization of antigenic sperm proteins in foxes (Vulpes
RT vulpes).";
RL J. Androl. 23:529-536(2002).
CC -!- FUNCTION: This protein is one of the nuclear-coded polypeptide chains
CC of cytochrome c oxidase, the terminal oxidase in mitochondrial electron
CC transport. {ECO:0000250|UniProtKB:P00428, ECO:0000255|PROSITE-
CC ProRule:PRU00692}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00428, ECO:0000255|PROSITE-ProRule:PRU00692}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Not expressed in brain, heart,
CC liver, kidney, spleen, lung, duodenum, muscle, epididymis, vagina,
CC uterus and ovary. {ECO:0000269|PubMed:15866998}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 6.0,
CC its MW is: 14.7 kDa. {ECO:0000269|PubMed:12065460}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase 5b family.
CC {ECO:0000255}.
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DR EMBL; AJ421970; CAD19164.1; -; mRNA.
DR AlphaFoldDB; Q710D6; -.
DR SMR; Q710D6; -.
DR STRING; 9627.ENSVVUP00000040325; -.
DR OMA; HVNFMVI; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS00848; COX5B_1; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15866998"
FT CHAIN 31..128
FT /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT /evidence="ECO:0000269|PubMed:15866998"
FT /id="PRO_0000395876"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428,
FT ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428,
FT ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428,
FT ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428,
FT ECO:0000255|PROSITE-ProRule:PRU00692"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT CONFLICT 31
FT /note="F -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="K -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14004 MW; E0A10F260CD61848 CRC64;
MKRGSAALEV RELKMQTPTA SCVLSTQRAN FAKGGVPTDD EQATGLEREV MMAARKGLDP
YNILAPKAAA GTKEDPNLVP SITNKRIVGC ICEEDNSTVI WFWLHKGEAQ RCPSCGTHYK
LVPHQLAH
