PXL2B_HUMAN
ID PXL2B_HUMAN Reviewed; 198 AA.
AC Q8TBF2; A8K793; B3KPY3; B4DQR9; B4E0S5; B7ZAC8; B9DI90; B9DI92; J3KQD0;
AC Q8N2H0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Prostamide/prostaglandin F synthase {ECO:0000305};
DE Short=Prostamide/PG F synthase;
DE Short=Prostamide/PGF synthase;
DE EC=1.11.1.20 {ECO:0000250|UniProtKB:Q9DB60};
DE AltName: Full=Peroxiredoxin-like 2B {ECO:0000305};
DE AltName: Full=Protein FAM213B;
GN Name=PRXL2B {ECO:0000312|HGNC:HGNC:28390};
GN Synonyms=C1orf93, FAM213B {ECO:0000312|HGNC:HGNC:28390};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
RC TISSUE=Neuroepithelioma, Teratocarcinoma, Thymus, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Guo J.H., She X.Y., Yu L.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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) (By
CC similarity). {ECO:0000250|UniProtKB:Q9DB60}.
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:0000250|UniProtKB:Q9DB60};
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:0000250|UniProtKB:Q9DB60};
CC -!- INTERACTION:
CC Q8TBF2; Q9UNS2: COPS3; NbExp=5; IntAct=EBI-7280826, EBI-350590;
CC Q8TBF2; Q9NUJ3: TCP11L1; NbExp=6; IntAct=EBI-7280826, EBI-2555179;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9DB60}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8TBF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBF2-2; Sequence=VSP_024581;
CC Name=3;
CC IsoId=Q8TBF2-3; Sequence=VSP_040901;
CC Name=4;
CC IsoId=Q8TBF2-4; Sequence=VSP_040903;
CC Name=5;
CC IsoId=Q8TBF2-6; Sequence=VSP_040904;
CC Name=6;
CC IsoId=Q8TBF2-7; Sequence=VSP_040901, VSP_024581;
CC -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family.
CC Prostamide/prostaglandin F synthase subfamily. {ECO:0000305}.
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DR EMBL; AK057027; BAG51845.1; -; mRNA.
DR EMBL; AK075273; BAC11511.1; -; mRNA.
DR EMBL; AK291908; BAF84597.1; -; mRNA.
DR EMBL; AK298926; BAG61031.1; -; mRNA.
DR EMBL; AK303504; BAG64537.1; -; mRNA.
DR EMBL; AK316243; BAH14614.1; -; mRNA.
DR EMBL; AF425266; AAP97295.1; -; mRNA.
DR EMBL; AL139246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56086.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56087.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56088.1; -; Genomic_DNA.
DR EMBL; BC022547; AAH22547.1; -; mRNA.
DR CCDS; CCDS44.2; -. [Q8TBF2-1]
DR CCDS; CCDS72690.1; -. [Q8TBF2-3]
DR CCDS; CCDS72691.1; -. [Q8TBF2-4]
DR RefSeq; NP_001182665.1; NM_001195736.1. [Q8TBF2-3]
DR RefSeq; NP_001182666.1; NM_001195737.1. [Q8TBF2-6]
DR RefSeq; NP_001182667.1; NM_001195738.1. [Q8TBF2-2]
DR RefSeq; NP_001182669.1; NM_001195740.1. [Q8TBF2-4]
DR RefSeq; NP_001182670.1; NM_001195741.1.
DR RefSeq; NP_689584.2; NM_152371.3. [Q8TBF2-1]
DR AlphaFoldDB; Q8TBF2; -.
DR BioGRID; 126049; 20.
DR IntAct; Q8TBF2; 8.
DR MINT; Q8TBF2; -.
DR STRING; 9606.ENSP00000413218; -.
DR iPTMnet; Q8TBF2; -.
DR PhosphoSitePlus; Q8TBF2; -.
DR BioMuta; FAM213B; -.
DR DMDM; 74760424; -.
DR EPD; Q8TBF2; -.
DR jPOST; Q8TBF2; -.
DR MassIVE; Q8TBF2; -.
DR MaxQB; Q8TBF2; -.
DR PaxDb; Q8TBF2; -.
DR PeptideAtlas; Q8TBF2; -.
DR PRIDE; Q8TBF2; -.
DR ProteomicsDB; 74003; -. [Q8TBF2-1]
DR ProteomicsDB; 74004; -. [Q8TBF2-2]
DR ProteomicsDB; 74005; -. [Q8TBF2-3]
DR ProteomicsDB; 74006; -. [Q8TBF2-4]
DR ProteomicsDB; 74008; -. [Q8TBF2-6]
DR ProteomicsDB; 74009; -. [Q8TBF2-7]
DR Antibodypedia; 1625; 69 antibodies from 17 providers.
DR DNASU; 127281; -.
DR Ensembl; ENST00000378424.9; ENSP00000367681.5; ENSG00000157870.17. [Q8TBF2-7]
DR Ensembl; ENST00000378427.6; ENSP00000367684.2; ENSG00000157870.17. [Q8TBF2-2]
DR Ensembl; ENST00000419916.8; ENSP00000394405.4; ENSG00000157870.17. [Q8TBF2-1]
DR GeneID; 127281; -.
DR KEGG; hsa:127281; -.
DR MANE-Select; ENST00000419916.8; ENSP00000394405.4; NM_152371.5; NP_689584.5.
DR UCSC; uc001aju.4; human. [Q8TBF2-1]
DR CTD; 127281; -.
DR DisGeNET; 127281; -.
DR GeneCards; PRXL2B; -.
DR HGNC; HGNC:28390; PRXL2B.
DR HPA; ENSG00000157870; Low tissue specificity.
DR neXtProt; NX_Q8TBF2; -.
DR OpenTargets; ENSG00000157870; -.
DR PharmGKB; PA142672477; -.
DR VEuPathDB; HostDB:ENSG00000157870; -.
DR eggNOG; KOG4498; Eukaryota.
DR GeneTree; ENSGT00940000162566; -.
DR HOGENOM; CLU_094994_0_0_1; -.
DR InParanoid; Q8TBF2; -.
DR OMA; QRPVCND; -.
DR OrthoDB; 1255928at2759; -.
DR PhylomeDB; Q8TBF2; -.
DR TreeFam; TF313804; -.
DR PathwayCommons; Q8TBF2; -.
DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SignaLink; Q8TBF2; -.
DR BioGRID-ORCS; 127281; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; FAM213B; human.
DR GenomeRNAi; 127281; -.
DR Pharos; Q8TBF2; Tdark.
DR PRO; PR:Q8TBF2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TBF2; protein.
DR Bgee; ENSG00000157870; Expressed in mucosa of transverse colon and 94 other tissues.
DR ExpressionAtlas; Q8TBF2; baseline and differential.
DR Genevisible; Q8TBF2; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; ISS:CAFA.
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; ISS:UniProtKB.
DR GO; GO:0047017; F:prostaglandin-F synthase activity; ISS:CAFA.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS: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 Alternative splicing; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Phosphoprotein; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1..198
FT /note="Prostamide/prostaglandin F synthase"
FT /id="PRO_0000284637"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 106
FT /note="K -> KRLWTQASPEFGQATWCLR (in isoform 3 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040901"
FT VAR_SEQ 129..164
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040903"
FT VAR_SEQ 130..164
FT /note="KAVGIQGNLSGDLLQSGGLLVVSKGGDKVLLHFVQ -> VPTPDRPRLLASR
FT GTCLGTCCRAEGCWWSAK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040904"
FT VAR_SEQ 154..198
FT /note="GGDKVLLHFVQKSPGDYVPKEHILQVLGISAEVCASDPPQCDREV -> EVP
FT RRLRPQGAHPAGPGHLCGGLCQRPASV (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024581"
SQ SEQUENCE 198 AA; 21223 MW; 5E846BAFF44BA7FF CRC64;
MSTVDLARVG ACILKHAVTG EAVELRSLWR EHACVVAGLR RFGCVVCRWI AQDLSSLAGL
LDQHGVRLVG VGPEALGLQE FLDGDYFAGE LYLDESKQLY KELGFKRYNS LSILPAALGK
PVRDVAAKAK AVGIQGNLSG DLLQSGGLLV VSKGGDKVLL HFVQKSPGDY VPKEHILQVL
GISAEVCASD PPQCDREV
