PXL2B_MOUSE
ID PXL2B_MOUSE Reviewed; 201 AA.
AC Q9DB60;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Prostamide/prostaglandin F synthase {ECO:0000303|PubMed:18006499};
DE Short=Prostamide/PG F synthase;
DE Short=Prostamide/PGF synthase;
DE EC=1.11.1.20 {ECO:0000269|PubMed:18006499};
DE AltName: Full=Peroxiredoxin-like 2B {ECO:0000305};
GN Name=Prxl2b; Synonyms=Fam213b {ECO:0000312|MGI:MGI:1913719};
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=Cerebellum;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-44 AND CYS-47.
RX PubMed=18006499; DOI=10.1074/jbc.m705638200;
RA Moriuchi H., Koda N., Okuda-Ashitaka E., Daiyasu H., Ogasawara K., Toh H.,
RA Ito S., Woodward D.F., Watanabe K.;
RT "Molecular characterization of a novel type of prostamide/prostaglandin F
RT synthase, belonging to the thioredoxin-like superfamily.";
RL J. Biol. Chem. 283:792-801(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Spleen;
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 TISSUE SPECIFICITY.
RX PubMed=20950588; DOI=10.1016/j.brainres.2010.10.019;
RA Yoshikawa K., Takei S., Hasegawa-Ishii S., Chiba Y., Furukawa A.,
RA Kawamura N., Hosokawa M., Woodward D.F., Watanabe K., Shimada A.;
RT "Preferential localization of prostamide/prostaglandin F synthase in myelin
RT sheaths of the central nervous system.";
RL Brain Res. 1367:22-32(2011).
CC -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2)
CC (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor.
CC Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha).
CC {ECO:0000269|PubMed:18006499}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + prostaglandin H2 = [thioredoxin]-
CC disulfide + prostaglandin F2alpha; Xref=Rhea:RHEA:28214, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57404, ChEBI:CHEBI:57405;
CC EC=1.11.1.20; Evidence={ECO:0000269|PubMed:18006499};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + prostamide F2alpha = [thioredoxin]-
CC dithiol + prostamide H2; Xref=Rhea:RHEA:26373, Rhea:RHEA-COMP:10698,
CC Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:53081, ChEBI:CHEBI:53082; EC=1.11.1.20;
CC Evidence={ECO:0000269|PubMed:18006499};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18006499}.
CC -!- TISSUE SPECIFICITY: Mainly present in brain and spinal cord. In spinal
CC cord, present in the superficial layer of the dorsal horn, in motor
CC neurons of the ventral horn and in glia of the white matter of the
CC spinal cord. In brain, expressed preferentially in the white matter
CC bundles of the entire CNS of adult with less marked expression in
CC neuronal cell bodies. Colocalizes with MBP in myelin sheaths but not in
CC axons. Localizes to myelin sheaths (at protein level).
CC {ECO:0000269|PubMed:18006499, ECO:0000269|PubMed:20950588}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family.
CC Prostamide/prostaglandin F synthase subfamily. {ECO:0000305}.
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DR EMBL; AK005188; BAB23870.1; -; mRNA.
DR EMBL; AL607032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030453; AAH30453.1; -; mRNA.
DR CCDS; CCDS19016.1; -.
DR RefSeq; NP_079858.2; NM_025582.3.
DR AlphaFoldDB; Q9DB60; -.
DR SMR; Q9DB60; -.
DR BioGRID; 211497; 1.
DR STRING; 10090.ENSMUSP00000030935; -.
DR SwissLipids; SLP:000001101; -.
DR iPTMnet; Q9DB60; -.
DR PhosphoSitePlus; Q9DB60; -.
DR SwissPalm; Q9DB60; -.
DR EPD; Q9DB60; -.
DR MaxQB; Q9DB60; -.
DR PaxDb; Q9DB60; -.
DR PeptideAtlas; Q9DB60; -.
DR PRIDE; Q9DB60; -.
DR ProteomicsDB; 288052; -.
DR Antibodypedia; 1625; 69 antibodies from 17 providers.
DR DNASU; 66469; -.
DR Ensembl; ENSMUST00000030935; ENSMUSP00000030935; ENSMUSG00000029059.
DR GeneID; 66469; -.
DR KEGG; mmu:66469; -.
DR UCSC; uc008wch.1; mouse.
DR CTD; 127281; -.
DR MGI; MGI:1913719; Prxl2b.
DR VEuPathDB; HostDB:ENSMUSG00000029059; -.
DR eggNOG; KOG4498; Eukaryota.
DR GeneTree; ENSGT00940000162566; -.
DR HOGENOM; CLU_094994_0_0_1; -.
DR InParanoid; Q9DB60; -.
DR OMA; QRPVCND; -.
DR OrthoDB; 1255928at2759; -.
DR PhylomeDB; Q9DB60; -.
DR TreeFam; TF313804; -.
DR BRENDA; 1.11.1.20; 3474.
DR SABIO-RK; Q9DB60; -.
DR BioGRID-ORCS; 66469; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fam213b; mouse.
DR PRO; PR:Q9DB60; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DB60; protein.
DR Bgee; ENSMUSG00000029059; Expressed in olfactory epithelium and 241 other tissues.
DR ExpressionAtlas; Q9DB60; baseline and differential.
DR Genevisible; Q9DB60; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0047017; F:prostaglandin-F synthase activity; IMP:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; TAS:Reactome.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR032801; PXL2A/B/C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR28630; PTHR28630; 1.
DR Pfam; PF13911; AhpC-TSA_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome.
FT CHAIN 1..201
FT /note="Prostamide/prostaglandin F synthase"
FT /id="PRO_0000284638"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBF2"
FT MUTAGEN 44
FT /note="C->S: Almost abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18006499"
FT MUTAGEN 47
FT /note="C->S: Decreased enzyme activity to retain 63% of
FT wild type activity."
FT /evidence="ECO:0000269|PubMed:18006499"
SQ SEQUENCE 201 AA; 21670 MW; 4F392EF111AC6B42 CRC64;
MNVVDLGRVG ACVLKHAVTG EAVELRSLWQ EKACVVAGLR RFGCMVCRWI AQDLSNLRSI
LDQHDVRLVG VGPEALGLQE FLDGGYFSGE LYLDESKQIY KELGFKRYNS LSILPAALGK
PVRDVASKAK AVGIQGNLSG DLLQSGGLLV VSKGGDKVLL HFIQKSPGDY VPQENILQAL
GISAEVCSSK PPQCDEEVCG R
