ID   PXL2A_XENTR             Reviewed;         227 AA.
AC   A0JPD7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Peroxiredoxin-like 2A;
DE   AltName: Full=Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes;
DE            Short=Protein PAMM;
DE   AltName: Full=Redox-regulatory protein FAM213A;
GN   Name=prxl2a; Synonyms=fam213a, pamm;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in redox regulation of the cell. Acts as an
CC       antioxidant (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family. PRXL2A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC127374; AAI27375.1; -; mRNA.
DR   RefSeq; NP_001090691.1; NM_001097222.2.
DR   AlphaFoldDB; A0JPD7; -.
DR   SMR; A0JPD7; -.
DR   STRING; 8364.ENSXETP00000020353; -.
DR   PaxDb; A0JPD7; -.
DR   GeneID; 100036669; -.
DR   KEGG; xtr:100036669; -.
DR   CTD; 84293; -.
DR   Xenbase; XB-GENE-962667; prxl2a.
DR   eggNOG; KOG4498; Eukaryota.
DR   HOGENOM; CLU_086062_0_0_1; -.
DR   InParanoid; A0JPD7; -.
DR   OMA; KFYGPQK; -.
DR   OrthoDB; 1442607at2759; -.
DR   PhylomeDB; A0JPD7; -.
DR   TreeFam; TF313804; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003529; Expressed in testis and 13 other tissues.
DR   ExpressionAtlas; A0JPD7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016209; F:antioxidant activity; IBA:GO_Central.
DR   InterPro; IPR032802; PRXL2A.
DR   InterPro; IPR032801; PXL2A/B/C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR28630; PTHR28630; 1.
DR   PANTHER; PTHR28630:SF3; PTHR28630:SF3; 1.
DR   Pfam; PF13911; AhpC-TSA_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Redox-active center; Reference proteome.
FT   CHAIN           1..227
FT                   /note="Peroxiredoxin-like 2A"
FT                   /id="PRO_0000398785"
FT   REGION          13..111
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        84
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        87
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  25230 MW;  309A6C095567F3DB CRC64;
     MFDLSDQLIA MGLWSISIGA FGAAVAGILL ANTDLFLTQT EEATLDYLEE TELKAIGDEP
     KSFKAKDLWE KNGAVVMAVR RPGCFLCREE ASDLSSLKSQ LDQLGVPLYA VVKENIGNEV
     EQFQPYFNGK IFLDEKGKFY GPQKRKMMFL GLVRLGVWQN FRRAWKGGFE GNLEGEGLIL
     GGMFVIGSGK QGILLEHREK EFGDKANLTA VLDAARKINK QRAQNDN