Full text data of FAM213B
FAM213B
(C1orf93)
[Confidence: low (only semi-automatic identification from reviews)]
Prostamide/prostaglandin F synthase; Prostamide/PG F synthase; Prostamide/PGF synthase; 1.11.1.20 (Protein FAM213B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prostamide/prostaglandin F synthase; Prostamide/PG F synthase; Prostamide/PGF synthase; 1.11.1.20 (Protein FAM213B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TBF2
ID PGFS_HUMAN Reviewed; 198 AA.
AC Q8TBF2; A8K793; B3KPY3; B4DQR9; B4E0S5; B7ZAC8; B9DI90; B9DI92;
read moreAC Q8N2H0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Prostamide/prostaglandin F synthase;
DE Short=Prostamide/PG F synthase;
DE Short=Prostamide/PGF synthase;
DE EC=1.11.1.20;
DE AltName: Full=Protein FAM213B;
GN Name=FAM213B; Synonyms=C1orf93;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide
CC H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as
CC proton donor. Also able to reduce prostaglandin H(2) to
CC prostaglandin F(2alpha) (By similarity).
CC -!- CATALYTIC ACTIVITY: Thioredoxin + prostaglandin H(2) = thioredoxin
CC disulfide + prostaglandin F(2-alpha).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8TBF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBF2-2; Sequence=VSP_024581;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8TBF2-3; Sequence=VSP_040901;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q8TBF2-4; Sequence=VSP_040903;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q8TBF2-5; Sequence=VSP_040900, VSP_040902;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q8TBF2-6; Sequence=VSP_040900, VSP_040904;
CC Note=No experimental confirmation available;
CC Name=7;
CC IsoId=Q8TBF2-7; Sequence=VSP_040901, VSP_024581;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the peroxiredoxin-like FAM213 family.
CC Prostamide/prostaglandin F synthase subfamily.
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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; CAX30825.1; -; Genomic_DNA.
DR EMBL; AL139246; CAX30826.1; -; Genomic_DNA.
DR EMBL; AL139246; CAX30827.1; -; 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 RefSeq; NP_001182665.1; NM_001195736.1.
DR RefSeq; NP_001182666.1; NM_001195737.1.
DR RefSeq; NP_001182667.1; NM_001195738.1.
DR RefSeq; NP_001182669.1; NM_001195740.1.
DR RefSeq; NP_001182670.1; NM_001195741.1.
DR RefSeq; NP_689584.2; NM_152371.3.
DR UniGene; Hs.462033; -.
DR ProteinModelPortal; Q8TBF2; -.
DR IntAct; Q8TBF2; 2.
DR MINT; MINT-8247583; -.
DR STRING; 9606.ENSP00000367682; -.
DR PhosphoSite; Q8TBF2; -.
DR DMDM; 74760424; -.
DR PaxDb; Q8TBF2; -.
DR PRIDE; Q8TBF2; -.
DR DNASU; 127281; -.
DR Ensembl; ENST00000378425; ENSP00000367682; ENSG00000157870.
DR Ensembl; ENST00000444521; ENSP00000413218; ENSG00000157870.
DR Ensembl; ENST00000537325; ENSP00000443605; ENSG00000157870.
DR GeneID; 127281; -.
DR KEGG; hsa:127281; -.
DR CTD; 127281; -.
DR GeneCards; GC01P002517; -.
DR HGNC; HGNC:28390; FAM213B.
DR HPA; HPA006403; -.
DR neXtProt; NX_Q8TBF2; -.
DR PharmGKB; PA142672477; -.
DR eggNOG; NOG276778; -.
DR HOVERGEN; HBG106494; -.
DR KO; K15717; -.
DR PhylomeDB; Q8TBF2; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 127281; -.
DR NextBio; 82055; -.
DR PRO; PR:Q8TBF2; -.
DR ArrayExpress; Q8TBF2; -.
DR Bgee; Q8TBF2; -.
DR CleanEx; HS_C1orf93; -.
DR Genevestigator; Q8TBF2; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Oxidoreductase; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1 198 Prostamide/prostaglandin F synthase.
FT /FTId=PRO_0000284637.
FT VAR_SEQ 1 1 M -> MSRERGSRSEEPGAGNRESGSREPGLAAAAM (in
FT isoform 5 and isoform 6).
FT /FTId=VSP_040900.
FT VAR_SEQ 106 106 K -> KRLWTQASPEFGQATWCLR (in isoform 3
FT and isoform 7).
FT /FTId=VSP_040901.
FT VAR_SEQ 128 164 Missing (in isoform 5).
FT /FTId=VSP_040902.
FT VAR_SEQ 129 164 Missing (in isoform 4).
FT /FTId=VSP_040903.
FT VAR_SEQ 130 164 KAVGIQGNLSGDLLQSGGLLVVSKGGDKVLLHFVQ -> VP
FT TPDRPRLLASRGTCLGTCCRAEGCWWSAK (in isoform
FT 6).
FT /FTId=VSP_040904.
FT VAR_SEQ 154 198 GGDKVLLHFVQKSPGDYVPKEHILQVLGISAEVCASDPPQC
FT DREV -> EVPRRLRPQGAHPAGPGHLCGGLCQRPASV
FT (in isoform 2 and isoform 7).
FT /FTId=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
//
ID PGFS_HUMAN Reviewed; 198 AA.
AC Q8TBF2; A8K793; B3KPY3; B4DQR9; B4E0S5; B7ZAC8; B9DI90; B9DI92;
read moreAC Q8N2H0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Prostamide/prostaglandin F synthase;
DE Short=Prostamide/PG F synthase;
DE Short=Prostamide/PGF synthase;
DE EC=1.11.1.20;
DE AltName: Full=Protein FAM213B;
GN Name=FAM213B; Synonyms=C1orf93;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide
CC H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as
CC proton donor. Also able to reduce prostaglandin H(2) to
CC prostaglandin F(2alpha) (By similarity).
CC -!- CATALYTIC ACTIVITY: Thioredoxin + prostaglandin H(2) = thioredoxin
CC disulfide + prostaglandin F(2-alpha).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8TBF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBF2-2; Sequence=VSP_024581;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8TBF2-3; Sequence=VSP_040901;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q8TBF2-4; Sequence=VSP_040903;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q8TBF2-5; Sequence=VSP_040900, VSP_040902;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q8TBF2-6; Sequence=VSP_040900, VSP_040904;
CC Note=No experimental confirmation available;
CC Name=7;
CC IsoId=Q8TBF2-7; Sequence=VSP_040901, VSP_024581;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the peroxiredoxin-like FAM213 family.
CC Prostamide/prostaglandin F synthase subfamily.
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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; CAX30825.1; -; Genomic_DNA.
DR EMBL; AL139246; CAX30826.1; -; Genomic_DNA.
DR EMBL; AL139246; CAX30827.1; -; 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 RefSeq; NP_001182665.1; NM_001195736.1.
DR RefSeq; NP_001182666.1; NM_001195737.1.
DR RefSeq; NP_001182667.1; NM_001195738.1.
DR RefSeq; NP_001182669.1; NM_001195740.1.
DR RefSeq; NP_001182670.1; NM_001195741.1.
DR RefSeq; NP_689584.2; NM_152371.3.
DR UniGene; Hs.462033; -.
DR ProteinModelPortal; Q8TBF2; -.
DR IntAct; Q8TBF2; 2.
DR MINT; MINT-8247583; -.
DR STRING; 9606.ENSP00000367682; -.
DR PhosphoSite; Q8TBF2; -.
DR DMDM; 74760424; -.
DR PaxDb; Q8TBF2; -.
DR PRIDE; Q8TBF2; -.
DR DNASU; 127281; -.
DR Ensembl; ENST00000378425; ENSP00000367682; ENSG00000157870.
DR Ensembl; ENST00000444521; ENSP00000413218; ENSG00000157870.
DR Ensembl; ENST00000537325; ENSP00000443605; ENSG00000157870.
DR GeneID; 127281; -.
DR KEGG; hsa:127281; -.
DR CTD; 127281; -.
DR GeneCards; GC01P002517; -.
DR HGNC; HGNC:28390; FAM213B.
DR HPA; HPA006403; -.
DR neXtProt; NX_Q8TBF2; -.
DR PharmGKB; PA142672477; -.
DR eggNOG; NOG276778; -.
DR HOVERGEN; HBG106494; -.
DR KO; K15717; -.
DR PhylomeDB; Q8TBF2; -.
DR Reactome; REACT_111217; Metabolism.
DR GenomeRNAi; 127281; -.
DR NextBio; 82055; -.
DR PRO; PR:Q8TBF2; -.
DR ArrayExpress; Q8TBF2; -.
DR Bgee; Q8TBF2; -.
DR CleanEx; HS_C1orf93; -.
DR Genevestigator; Q8TBF2; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0019371; P:cyclooxygenase pathway; TAS:Reactome.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Oxidoreductase; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1 198 Prostamide/prostaglandin F synthase.
FT /FTId=PRO_0000284637.
FT VAR_SEQ 1 1 M -> MSRERGSRSEEPGAGNRESGSREPGLAAAAM (in
FT isoform 5 and isoform 6).
FT /FTId=VSP_040900.
FT VAR_SEQ 106 106 K -> KRLWTQASPEFGQATWCLR (in isoform 3
FT and isoform 7).
FT /FTId=VSP_040901.
FT VAR_SEQ 128 164 Missing (in isoform 5).
FT /FTId=VSP_040902.
FT VAR_SEQ 129 164 Missing (in isoform 4).
FT /FTId=VSP_040903.
FT VAR_SEQ 130 164 KAVGIQGNLSGDLLQSGGLLVVSKGGDKVLLHFVQ -> VP
FT TPDRPRLLASRGTCLGTCCRAEGCWWSAK (in isoform
FT 6).
FT /FTId=VSP_040904.
FT VAR_SEQ 154 198 GGDKVLLHFVQKSPGDYVPKEHILQVLGISAEVCASDPPQC
FT DREV -> EVPRRLRPQGAHPAGPGHLCGGLCQRPASV
FT (in isoform 2 and isoform 7).
FT /FTId=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
//