PXL2A_MOUSE
ID PXL2A_MOUSE Reviewed; 218 AA.
AC Q9CYH2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Peroxiredoxin-like 2A {ECO:0000305};
DE AltName: Full=Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes {ECO:0000303|PubMed:19951071, ECO:0000303|PubMed:26438880};
DE Short=Protein PAMM {ECO:0000303|PubMed:19951071, ECO:0000303|PubMed:26438880};
DE AltName: Full=Redox-regulatory protein FAM213A;
GN Name=Prxl2a;
GN Synonyms=Fam213a {ECO:0000312|MGI:MGI:1917814},
GN Pamm {ECO:0000303|PubMed:19951071, ECO:0000303|PubMed:26438880};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 91-103 AND 196-206, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26438880; DOI=10.1042/bj20150019;
RA Guo F., He H., Fu Z.C., Huang S., Chen T., Papasian C.J., Morse L.R.,
RA Xu Y., Battaglino R.A., Yang X.F., Jiang Z., Xin H.B., Fu M.;
RT "Adipocyte-derived PAMM suppresses macrophage inflammation by inhibiting
RT MAPK signalling.";
RL Biochem. J. 472:309-318(2015).
CC -!- FUNCTION: Involved in redox regulation of the cell (By similarity).
CC Acts as an antioxidant (By similarity). Inhibits TNFSF11-induced NFKB1
CC and JUN activation and osteoclast differentiation (By similarity). May
CC affect bone resorption and help to maintain bone mass (By similarity).
CC Acts as a negative regulator of macrophage-mediated inflammation by
CC inhibiting macrophage production of inflammatory cytokines, probably
CC through suppression of the MAPK signaling pathway (PubMed:26438880).
CC {ECO:0000250|UniProtKB:Q9BRX8, ECO:0000269|PubMed:26438880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRX8}.
CC Secreted {ECO:0000269|PubMed:26438880}. Note=Secreted from mature
CC adipocytes but not from preadipocytes. {ECO:0000250|UniProtKB:Q9BRX8}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, skin, and brain
CC (PubMed:19951071). Widely expressed with highest levels detected in
CC adipose tissue (PubMed:26438880). {ECO:0000269|PubMed:19951071,
CC ECO:0000269|PubMed:26438880}.
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; AK017688; BAB30875.2; -; mRNA.
DR EMBL; BC056635; AAH56635.1; -; mRNA.
DR CCDS; CCDS26957.1; -.
DR RefSeq; NP_001303661.1; NM_001316732.1.
DR RefSeq; NP_001303662.1; NM_001316733.1.
DR RefSeq; NP_001303663.1; NM_001316734.1.
DR RefSeq; NP_001303664.1; NM_001316735.1.
DR RefSeq; NP_001303665.1; NM_001316736.1.
DR RefSeq; NP_001303666.1; NM_001316737.1.
DR RefSeq; NP_001303668.1; NM_001316739.1.
DR RefSeq; NP_001303669.1; NM_001316740.1.
DR RefSeq; NP_081740.2; NM_027464.4.
DR AlphaFoldDB; Q9CYH2; -.
DR SMR; Q9CYH2; -.
DR BioGRID; 214138; 4.
DR STRING; 10090.ENSMUSP00000022317; -.
DR iPTMnet; Q9CYH2; -.
DR PhosphoSitePlus; Q9CYH2; -.
DR SwissPalm; Q9CYH2; -.
DR EPD; Q9CYH2; -.
DR jPOST; Q9CYH2; -.
DR MaxQB; Q9CYH2; -.
DR PaxDb; Q9CYH2; -.
DR PRIDE; Q9CYH2; -.
DR ProteomicsDB; 275514; -.
DR Antibodypedia; 2394; 75 antibodies from 17 providers.
DR DNASU; 70564; -.
DR Ensembl; ENSMUST00000022317; ENSMUSP00000022317; ENSMUSG00000021792.
DR GeneID; 70564; -.
DR KEGG; mmu:70564; -.
DR UCSC; uc007tci.1; mouse.
DR CTD; 84293; -.
DR MGI; MGI:1917814; Prxl2a.
DR VEuPathDB; HostDB:ENSMUSG00000021792; -.
DR eggNOG; KOG4498; Eukaryota.
DR GeneTree; ENSGT00940000161199; -.
DR InParanoid; Q9CYH2; -.
DR OrthoDB; 1442607at2759; -.
DR PhylomeDB; Q9CYH2; -.
DR TreeFam; TF313804; -.
DR BioGRID-ORCS; 70564; 1 hit in 27 CRISPR screens.
DR ChiTaRS; Fam213a; mouse.
DR PRO; PR:Q9CYH2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CYH2; protein.
DR Bgee; ENSMUSG00000021792; Expressed in pigmented layer of retina and 292 other tissues.
DR ExpressionAtlas; Q9CYH2; baseline and differential.
DR Genevisible; Q9CYH2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:MGI.
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; Direct protein sequencing; Redox-active center;
KW Reference proteome; Secreted.
FT CHAIN 1..218
FT /note="Peroxiredoxin-like 2A"
FT /id="PRO_0000019551"
FT REGION 3..101
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000250"
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; 24395 MW; A59CC8F53FACBC4C CRC64;
MGMWSIGVGA VGAAAVALLL ANTDMFLSKP RKAALEYLED IDLKTLEKEP RTFKAKELWE
KNGAVIMAVR RPGCFLCRAE AADLMSLKPK LDELGVPLYA VVKEQVKREV EDFQPYFKGE
IFLDEKKKFY GPERRKMMFM GLIRLGVWYN SFRAWNGGFS GNLEGEGFIL GGVFVIGSGK
QGILLEHREK EFGDRVNPLS VLEAVKKIKL QTPASGRS
