ID H2YWX8_CIOSA Unreviewed; 240 AA.
AC H2YWX8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Peroxiredoxin-6 {ECO:0000256|ARBA:ARBA00026214, ECO:0000256|PIRNR:PIRNR000239};
DE EC=1.11.1.27 {ECO:0000256|PIRNR:PIRNR000239};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000009839.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000009839.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000256|ARBA:ARBA00001479};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000256|ARBA:ARBA00001479};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000256|ARBA:ARBA00024460};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000256|ARBA:ARBA00024460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00024623};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; EC=1.11.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00024523,
CC ECO:0000256|PIRNR:PIRNR000239};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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DR AlphaFoldDB; H2YWX8; -.
DR STRING; 51511.ENSCSAVP00000009839; -.
DR Ensembl; ENSCSAVT00000009957.1; ENSCSAVP00000009839.1; ENSCSAVG00000005782.1.
DR eggNOG; KOG0854; Eukaryota.
DR GeneTree; ENSGT00550000074794; -.
DR HOGENOM; CLU_042529_4_1_1; -.
DR InParanoid; H2YWX8; -.
DR OMA; RLTMLYP; -.
DR TreeFam; TF105183; -.
DR Proteomes; UP000007875; Unassembled WGS sequence.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:RHEA.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000007875}.
FT DOMAIN 3..185
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 45
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 240 AA; 26528 MW; D9CDE84748F54C2E CRC64;
MPVNLGQVFP DFDCVTTQGN FKLLSYLAGS WGILFSHPAD FTPVCTTELG MAAAMKPEFD
KRQVKMLGLS IDSVKSHNDW MKVDYNSSSI TIYRHCLNLV ILQDIQSYSK LEGAFPYPII
AGDRKLALDL GMLDPDELDA TGMPLTARCV FIIGPDQKLK LSLLYPATTG RNFNEIIRVI
DSLQLTANKK VATPANWKSG EKCMVIPSLS DAQAKDLFPK GFETTQVPSG KCYIRLTPDP
//
