ADTRP_MOUSE
ID ADTRP_MOUSE Reviewed; 230 AA.
AC Q8C138; D3Z6U0; Q3UXS3; Q8K180;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Androgen-dependent TFPI-regulating protein;
DE AltName: Full=Fatty acid esters of hydroxy fatty acids hydrolase ADTRP {ECO:0000250|UniProtKB:Q96IZ2};
DE Short=FAHFA hydrolase ADTRP {ECO:0000250|UniProtKB:Q96IZ2};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q96IZ2};
GN Name=Adtrp;
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=Skin, and Wolffian duct;
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 STRAIN=FVB/N; TISSUE=Liver;
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).
CC -!- FUNCTION: Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids
CC (FAHFAs), but not other major classes of lipids (By similarity). Shows
CC a preference for FAHFAs with branching distal from the carboxylate head
CC group of the lipids (By similarity). Regulates the expression and the
CC cell-associated anticoagulant activity of the inhibitor TFPI in
CC endothelial cells (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:Q96IZ2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52052,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83670, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hexadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52056,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83677, ChEBI:CHEBI:84201;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136309;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136312;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:136304, ChEBI:CHEBI:136315;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52096,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136373;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-octadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136330;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136304, ChEBI:CHEBI:136335;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52048,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:136282, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52060,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136302;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:136303, ChEBI:CHEBI:136304;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 5-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52100,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:136370, ChEBI:CHEBI:136389;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52101;
CC Evidence={ECO:0000250|UniProtKB:Q96IZ2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96IZ2};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalized with TFPI
CC and CAV1 in lipid rafts. {ECO:0000250|UniProtKB:Q96IZ2}.
CC -!- SIMILARITY: Belongs to the AIG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AC165263; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC26250.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK029025; BAC26250.1; ALT_INIT; mRNA.
DR EMBL; AK135327; BAE22490.1; -; mRNA.
DR EMBL; AC165263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027755; AAH27755.1; -; mRNA.
DR CCDS; CCDS49250.1; -.
DR RefSeq; NP_001139347.1; NM_001145875.1.
DR RefSeq; NP_780626.1; NM_175417.4.
DR AlphaFoldDB; Q8C138; -.
DR STRING; 10090.ENSMUSP00000071899; -.
DR iPTMnet; Q8C138; -.
DR PhosphoSitePlus; Q8C138; -.
DR PaxDb; Q8C138; -.
DR PRIDE; Q8C138; -.
DR Antibodypedia; 63585; 4 antibodies from 4 providers.
DR DNASU; 109254; -.
DR Ensembl; ENSMUST00000121404; ENSMUSP00000113661; ENSMUSG00000058022.
DR Ensembl; ENSMUST00000179758; ENSMUSP00000137365; ENSMUSG00000058022.
DR GeneID; 109254; -.
DR KEGG; mmu:109254; -.
DR UCSC; uc007qfh.1; mouse.
DR CTD; 84830; -.
DR MGI; MGI:1924596; Adtrp.
DR VEuPathDB; HostDB:ENSMUSG00000058022; -.
DR eggNOG; KOG3989; Eukaryota.
DR GeneTree; ENSGT00940000158284; -.
DR HOGENOM; CLU_073346_2_0_1; -.
DR InParanoid; Q8C138; -.
DR OMA; TRTSTCI; -.
DR OrthoDB; 1482757at2759; -.
DR PhylomeDB; Q8C138; -.
DR TreeFam; TF318170; -.
DR BioGRID-ORCS; 109254; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Adtrp; mouse.
DR PRO; PR:Q8C138; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8C138; protein.
DR Bgee; ENSMUSG00000058022; Expressed in left lobe of liver and 102 other tissues.
DR ExpressionAtlas; Q8C138; baseline and differential.
DR Genevisible; Q8C138; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; ISO:MGI.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:MGI.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; ISO:MGI.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; ISO:MGI.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; ISO:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:MGI.
DR InterPro; IPR006838; Far-17a_AIG1.
DR PANTHER; PTHR10989; PTHR10989; 1.
DR Pfam; PF04750; Far-17a_AIG1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Androgen-dependent TFPI-regulating protein"
FT /id="PRO_0000190102"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..45
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..120
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..190
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT SITE 47
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT SITE 131
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
SQ SEQUENCE 230 AA; 27003 MW; 0AAEFC74F1555F9D CRC64;
MTKTTTCVYH FLVLNWYIFL NYHIPQIGRN EEKLREFHDG GRSKYLTLLN LLLQAIFFGV
ACLDDVLKRV IGRKDIKFVT SFRDLLFTTM AFPISTFVFL VFWTLFHYDR SLVYPKGLDD
FFPAWVNHAM HTSIFPFSLF ETILRPHNYP SKKLGLTLLG AFNFAYIIRI LWRYVQTGNW
VYPVFDSLSP LGIIIFFSAA YILVAGIYLF GEKINHWKWG AIAKPQMKKN
