ADTRP_HUMAN
ID ADTRP_HUMAN Reviewed; 230 AA.
AC Q96IZ2; B2R7T9; B4DV39; Q5THW1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Androgen-dependent TFPI-regulating protein;
DE AltName: Full=Fatty acid esters of hydroxy fatty acids hydrolase ADTRP {ECO:0000303|PubMed:27018888};
DE Short=FAHFA hydrolase ADTRP {ECO:0000303|PubMed:27018888};
DE EC=3.1.-.- {ECO:0000269|PubMed:27018888};
GN Name=ADTRP; Synonyms=C6orf105;
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 1 AND 2).
RC TISSUE=Colon, and Small intestine;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21868574; DOI=10.1182/blood-2011-05-355370;
RA Lupu C., Zhu H., Popescu N.I., Wren J.D., Lupu F.;
RT "Novel protein ADTRP regulates TFPI expression and function in human
RT endothelial cells in normal conditions and in response to androgen.";
RL Blood 118:4463-4471(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TOPOLOGY MODEL, SITE, AND MUTAGENESIS OF THR-47 AND HIS-131.
RX PubMed=27018888; DOI=10.1038/nchembio.2051;
RA Parsons W.H., Kolar M.J., Kamat S.S., Cognetta A.B. III, Hulce J.J.,
RA Saez E., Kahn B.B., Saghatelian A., Cravatt B.F.;
RT "AIG1 and ADTRP are atypical integral membrane hydrolases that degrade
RT bioactive FAHFAs.";
RL Nat. Chem. Biol. 12:367-372(2016).
CC -!- FUNCTION: Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids
CC (FAHFAs), but not other major classes of lipids (PubMed:27018888). Show
CC a preference for FAHFAs with branching distal from the carboxylate head
CC group of the lipids (PubMed:27018888). Regulates the expression and the
CC cell-associated anticoagulant activity of the inhibitor TFPI in
CC endothelial cells (in vitro) (PubMed:21868574).
CC {ECO:0000269|PubMed:21868574, ECO:0000269|PubMed:27018888}.
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000305|PubMed:27018888};
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:0000269|PubMed:27018888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52101;
CC Evidence={ECO:0000305|PubMed:27018888};
CC -!- ACTIVITY REGULATION: Inhibited by N-hydroxyhydantoin carbamate JJH260
CC and beta-lactone KC01. {ECO:0000269|PubMed:27018888}.
CC -!- INTERACTION:
CC Q96IZ2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-3921528, EBI-2807956;
CC Q96IZ2; Q6PL24: TMED8; NbExp=3; IntAct=EBI-3921528, EBI-11603430;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21868574,
CC ECO:0000269|PubMed:27018888}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalized with TFPI and CAV1 in lipid rafts.
CC {ECO:0000269|PubMed:21868574}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96IZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IZ2-2; Sequence=VSP_041965;
CC Name=3;
CC IsoId=Q96IZ2-3; Sequence=VSP_042868;
CC -!- TISSUE SPECIFICITY: Expressed in cultured endothelial cells and in
CC placenta. {ECO:0000269|PubMed:21868574}.
CC -!- INDUCTION: By androgens. {ECO:0000269|PubMed:21868574}.
CC -!- SIMILARITY: Belongs to the AIG1 family. {ECO:0000305}.
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DR EMBL; AK313114; BAG35936.1; -; mRNA.
DR EMBL; AK300919; BAG62551.1; -; mRNA.
DR EMBL; AL022724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55304.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55306.1; -; Genomic_DNA.
DR EMBL; BC007011; AAH07011.1; -; mRNA.
DR CCDS; CCDS4521.1; -. [Q96IZ2-1]
DR CCDS; CCDS47374.1; -. [Q96IZ2-2]
DR RefSeq; NP_001137420.1; NM_001143948.1. [Q96IZ2-2]
DR RefSeq; NP_116133.1; NM_032744.3. [Q96IZ2-1]
DR RefSeq; XP_005249511.1; XM_005249454.3. [Q96IZ2-1]
DR RefSeq; XP_011513258.1; XM_011514956.1. [Q96IZ2-3]
DR AlphaFoldDB; Q96IZ2; -.
DR BioGRID; 124285; 5.
DR IntAct; Q96IZ2; 5.
DR MINT; Q96IZ2; -.
DR STRING; 9606.ENSP00000229583; -.
DR BindingDB; Q96IZ2; -.
DR SwissLipids; SLP:000001683; -.
DR iPTMnet; Q96IZ2; -.
DR PhosphoSitePlus; Q96IZ2; -.
DR BioMuta; ADTRP; -.
DR DMDM; 83286865; -.
DR MassIVE; Q96IZ2; -.
DR PeptideAtlas; Q96IZ2; -.
DR PRIDE; Q96IZ2; -.
DR ProteomicsDB; 76871; -. [Q96IZ2-1]
DR ProteomicsDB; 76872; -. [Q96IZ2-2]
DR ProteomicsDB; 76873; -. [Q96IZ2-3]
DR Antibodypedia; 63585; 4 antibodies from 4 providers.
DR DNASU; 84830; -.
DR Ensembl; ENST00000229583.9; ENSP00000229583.5; ENSG00000111863.13. [Q96IZ2-2]
DR Ensembl; ENST00000414691.8; ENSP00000404416.2; ENSG00000111863.13. [Q96IZ2-1]
DR GeneID; 84830; -.
DR KEGG; hsa:84830; -.
DR MANE-Select; ENST00000414691.8; ENSP00000404416.2; NM_032744.4; NP_116133.1.
DR UCSC; uc003nab.4; human. [Q96IZ2-1]
DR CTD; 84830; -.
DR DisGeNET; 84830; -.
DR GeneCards; ADTRP; -.
DR HGNC; HGNC:21214; ADTRP.
DR HPA; ENSG00000111863; Tissue enhanced (intestine, parathyroid gland).
DR MIM; 614348; gene.
DR neXtProt; NX_Q96IZ2; -.
DR OpenTargets; ENSG00000111863; -.
DR PharmGKB; PA134981312; -.
DR VEuPathDB; HostDB:ENSG00000111863; -.
DR eggNOG; KOG3989; Eukaryota.
DR GeneTree; ENSGT00940000158284; -.
DR HOGENOM; CLU_073346_2_0_1; -.
DR InParanoid; Q96IZ2; -.
DR OMA; TRTSTCI; -.
DR OrthoDB; 1482757at2759; -.
DR PhylomeDB; Q96IZ2; -.
DR TreeFam; TF318170; -.
DR PathwayCommons; Q96IZ2; -.
DR SignaLink; Q96IZ2; -.
DR BioGRID-ORCS; 84830; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; ADTRP; human.
DR GenomeRNAi; 84830; -.
DR Pharos; Q96IZ2; Tbio.
DR PRO; PR:Q96IZ2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96IZ2; protein.
DR Bgee; ENSG00000111863; Expressed in sperm and 153 other tissues.
DR ExpressionAtlas; Q96IZ2; baseline and differential.
DR Genevisible; Q96IZ2; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IMP:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:BHF-UCL.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEP:UniProtKB.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IMP:UniProtKB.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; IMP:BHF-UCL.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IMP:BHF-UCL.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IMP:BHF-UCL.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; IMP:BHF-UCL.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:BHF-UCL.
DR InterPro; IPR006838; Far-17a_AIG1.
DR PANTHER; PTHR10989; PTHR10989; 1.
DR Pfam; PF04750; Far-17a_AIG1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Androgen-dependent TFPI-regulating protein"
FT /id="PRO_0000190100"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..46
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..119
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..189
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27018888"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27018888"
FT SITE 47
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:27018888"
FT SITE 131
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:27018888"
FT VAR_SEQ 52
FT /note="L -> LKNRTAGFDIYQPGSFRQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041965"
FT VAR_SEQ 220..230
FT /note="GDMRQPRKKRK -> VSVQILQRWRLESVGICFQWPDWKSPAKHQLVKNIR
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042868"
FT VARIANT 202
FT /note="V -> I (in dbSNP:rs2076185)"
FT /id="VAR_024365"
FT MUTAGEN 47
FT /note="T->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27018888"
FT MUTAGEN 131
FT /note="H->A: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:27018888"
SQ SEQUENCE 230 AA; 26842 MW; 49B964B41C381360 CRC64;
MTKTSTCIYH FLVLSWYTFL NYYISQEGKD EVKPKILANG ARWKYMTLLN LLLQTIFYGV
TCLDDVLKRT KGGKDIKFLT AFRDLLFTTL AFPVSTFVFL AFWILFLYNR DLIYPKVLDT
VIPVWLNHAM HTFIFPITLA EVVLRPHSYP SKKTGLTLLA AASIAYISRI LWLYFETGTW
VYPVFAKLSL LGLAAFFSLS YVFIASIYLL GEKLNHWKWG DMRQPRKKRK
