ID   PXL2A_CHICK             Reviewed;         224 AA.
AC   Q5ZI34;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 84.
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; ORFNames=RCJMB04_30m16;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   SELENOCYSTEINE AT SEC-85.
RX   PubMed=14710190; DOI=10.1038/sj.embor.7400036;
RA   Castellano S., Novoselov S.V., Kryukov G.V., Lescure A., Blanco E.,
RA   Krol A., Gladyshev V.N., Guigo R.;
RT   "Reconsidering the evolution of eukaryotic selenoproteins: a novel
RT   nonmammalian family with scattered phylogenetic distribution.";
RL   EMBO Rep. 5:71-77(2004).
CC   -!- FUNCTION: Involved in redox regulation of the cell. Acts as an
CC       antioxidant. Inhibits TNFSF11-induced NFKB1 and JUN activation and
CC       osteoclast differentiation. May affect bone resorption and help to
CC       maintain bone mass (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: The active site Cys-88 corresponds to one of the redox-
CC       active cysteines of peroxiredoxins.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family. PRXL2A
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG32609.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ720950; CAG32609.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001180448.1; NM_001193519.2.
DR   STRING; 9031.ENSGALP00000003802; -.
DR   PaxDb; Q5ZI34; -.
DR   GeneID; 423625; -.
DR   KEGG; gga:423625; -.
DR   CTD; 84293; -.
DR   VEuPathDB; HostDB:geneid_423625; -.
DR   eggNOG; KOG4498; Eukaryota.
DR   InParanoid; Q5ZI34; -.
DR   PhylomeDB; Q5ZI34; -.
DR   PRO; PR:Q5ZI34; -.
DR   Proteomes; UP000000539; Unplaced.
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;
KW   Selenocysteine.
FT   CHAIN           1..224
FT                   /note="Peroxiredoxin-like 2A"
FT                   /id="PRO_0000398782"
FT   REGION          14..112
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   NON_STD         85
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000269|PubMed:14710190"
SQ   SEQUENCE   224 AA;  24948 MW;  FE057DF563CDB24D CRC64;
     MSFLPDFGIF TMGMWSVGLG AVGAAITGIV LANTDLFLSK PEKATLEFLE AIELKTLGSE
     PRTFKASELW KKNGAVIMAV RRPGUFLCRE EASELSSLKP QLSKLGVPLY AVVKEKIGTE
     VEDFQHYFQG EIFLDEKRSF YGPRKRKMML SGFFRIGVWQ NFFRAWKNGY SGNLEGEGFT
     LGGVYVIGAG RQGILLEHRE KEFGDKVSLP SVLEAAEKIK PQAS