PXL2A_BOVIN
ID PXL2A_BOVIN Reviewed; 218 AA.
AC Q3ZBK2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Acts as a negative regulator of macrophage-mediated
CC inflammation by inhibiting macrophage production of inflammatory
CC cytokines, probably through suppression of the MAPK signaling pathway.
CC {ECO:0000250|UniProtKB:Q9BRX8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRX8}.
CC Secreted {ECO:0000250|UniProtKB:Q9BRX8}. Note=Secreted from mature
CC adipocytes but not from preadipocytes. {ECO:0000250|UniProtKB:Q9BRX8}.
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}.
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DR EMBL; BC103249; AAI03250.1; -; mRNA.
DR RefSeq; NP_001029771.1; NM_001034599.2.
DR RefSeq; XP_005226485.1; XM_005226428.3.
DR AlphaFoldDB; Q3ZBK2; -.
DR SMR; Q3ZBK2; -.
DR STRING; 9913.ENSBTAP00000028551; -.
DR PaxDb; Q3ZBK2; -.
DR PeptideAtlas; Q3ZBK2; -.
DR PRIDE; Q3ZBK2; -.
DR Ensembl; ENSBTAT00000028551; ENSBTAP00000028551; ENSBTAG00000021416.
DR GeneID; 534049; -.
DR KEGG; bta:534049; -.
DR CTD; 84293; -.
DR VEuPathDB; HostDB:ENSBTAG00000021416; -.
DR VGNC; VGNC:28791; PRXL2A.
DR eggNOG; KOG4498; Eukaryota.
DR GeneTree; ENSGT00940000161199; -.
DR HOGENOM; CLU_086062_0_0_1; -.
DR InParanoid; Q3ZBK2; -.
DR OMA; KFYGPQK; -.
DR OrthoDB; 1442607at2759; -.
DR TreeFam; TF313804; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000021416; Expressed in oviduct epithelium and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IBA:GO_Central.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
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; Secreted.
FT CHAIN 1..218
FT /note="Peroxiredoxin-like 2A"
FT /id="PRO_0000271444"
FT REGION 3..101
FT /note="Thioredoxin fold"
FT ACT_SITE 74
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT ACT_SITE 77
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 24355 MW; D2AFACA207770D86 CRC64;
MGMWSIGAGA IGVAALALLL ANTDMFLAKP EKAALEYLED IDLKTLEKDA VTFKAKALWE
KNGAVIMAVR RPGCFLCREE ATDLSSLKPK LDELGVPLYA VVKEHIKNEV KDFQPYFKGE
IFLDENKKFY GPQRRKMMFM GFVRLGVWQN FFRAWNGGFS GNLDGEGFIL GGVFVMGPGK
QGILLEHREK EFGDKVNLTS VLEAARKIRP QTSASEKQ
