ID   PXL2A_RAT               Reviewed;         229 AA.
AC   Q6AXX6; P85300;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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;
DE   AltName: Full=Sperm head protein 1;
GN   Name=Prxl2a {ECO:0000312|RGD:1309676}; Synonyms=Fam213a, Pamm, Shp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   STRAIN=Holtzman; TISSUE=Epididymis, and Sperm;
RX   PubMed=19423663; DOI=10.1530/rep-09-0052;
RA   Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT   "Identification of novel immunodominant epididymal sperm proteins using
RT   combinatorial approach.";
RL   Reproduction 138:81-93(2009).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19951071; DOI=10.1089/ars.2009.2886;
RA   Xu Y., Morse L.R., da Silva R.A., Odgren P.R., Sasaki H., Stashenko P.,
RA   Battaglino R.A.;
RT   "PAMM: a redox regulatory protein that modulates osteoclast
RT   differentiation.";
RL   Antioxid. Redox Signal. 13:27-37(2010).
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   -!- TISSUE SPECIFICITY: Expressed by the principal cells of the epididymis.
CC       Detected in the head region of epididymal sperm (at protein level).
CC       Expressed in bone marrow. {ECO:0000269|PubMed:19423663,
CC       ECO:0000269|PubMed:19951071}.
CC   -!- INDUCTION: Up-regulated on CSF1 treatment.
CC       {ECO:0000269|PubMed:19951071}.
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; BC079275; AAH79275.1; -; mRNA.
DR   RefSeq; NP_001014162.1; NM_001014140.1.
DR   RefSeq; XP_006252853.1; XM_006252791.3.
DR   AlphaFoldDB; Q6AXX6; -.
DR   SMR; Q6AXX6; -.
DR   BioGRID; 262452; 1.
DR   IntAct; Q6AXX6; 1.
DR   MINT; Q6AXX6; -.
DR   STRING; 10116.ENSRNOP00000014819; -.
DR   iPTMnet; Q6AXX6; -.
DR   PhosphoSitePlus; Q6AXX6; -.
DR   jPOST; Q6AXX6; -.
DR   PaxDb; Q6AXX6; -.
DR   PRIDE; Q6AXX6; -.
DR   GeneID; 361118; -.
DR   KEGG; rno:361118; -.
DR   UCSC; RGD:1309676; rat.
DR   CTD; 84293; -.
DR   RGD; 1309676; Prxl2a.
DR   VEuPathDB; HostDB:ENSRNOG00000011140; -.
DR   eggNOG; KOG4498; Eukaryota.
DR   HOGENOM; CLU_086062_0_0_1; -.
DR   InParanoid; Q6AXX6; -.
DR   OMA; KFYGPQK; -.
DR   OrthoDB; 1442607at2759; -.
DR   PhylomeDB; Q6AXX6; -.
DR   TreeFam; TF313804; -.
DR   PRO; PR:Q6AXX6; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000011140; Expressed in testis and 20 other tissues.
DR   Genevisible; Q6AXX6; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
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   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Redox-active center; Reference proteome; Secreted.
FT   CHAIN           1..229
FT                   /note="Peroxiredoxin-like 2A"
FT                   /id="PRO_0000019552"
FT   REGION          14..112
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        85
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  25763 MW;  176B1E95FD8285A6 CRC64;
     MSFLQDSSFF SMGMWSIGVG AFGAAALALL LANTDMFLSK PQKAALEYLE DIDLKTLEKE
     PRTFKAKELW EKNGAVIMAV RRPGCFLCRA EAADLMSLKP KLDELGVPLY AVVKEKVKRE
     VEDFQPYFKG EIFLDEKKKF YGPERRKMML MGLVRLGVWY NSFRAWKGGF SGNFEGEGFI
     LGGVFVIGSG KQGVLLEHRE KEFGDRVNLL SVLEAVKKIK PQTPASRQS