ID   PXL2A_XENLA             Reviewed;         227 AA.
AC   Q641F0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 63.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) 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   -!- MISCELLANEOUS: The active site cysteines correspond to the redox-active
CC       cysteines of peroxiredoxins.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family. PRXL2A
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH82387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH82387.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC082387; AAH82387.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001087861.1; NM_001094392.1.
DR   AlphaFoldDB; Q641F0; -.
DR   SMR; Q641F0; -.
DR   GeneID; 447722; -.
DR   KEGG; xla:447722; -.
DR   CTD; 447722; -.
DR   Xenbase; XB-GENE-962672; prxl2a.L.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 447722; Expressed in camera-type eye and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   InterPro; IPR032802; PRXL2A.
DR   InterPro; IPR032801; PXL2A/B/C.
DR   PANTHER; PTHR28630; PTHR28630; 1.
DR   PANTHER; PTHR28630:SF3; PTHR28630:SF3; 1.
DR   Pfam; PF13911; AhpC-TSA_2; 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_0000398784"
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;  25221 MW;  C241D04ED2E92F60 CRC64;
     MFDLSDQLIT MGLWSISIGA FGAAVAGILL ANTDFFLSQT EKATLDYLEE TELKTIGEEP
     RLFKAKDLWE RDGAVIMAVR RPGCFLCREE ASGLSTLKPQ LDQLGVPLYA IVKENIGNEV
     EHFQPYFNGK VFLDAKGQFY GPQKRKMMLL GLVRLGVWQN FRRAWKGGFE GNLEGEGLIL
     GGMFVIGSGK QGILLEHREK EFGDKANLTA VLDAARKISK QTAQNDN