ID   AIG1_HUMAN              Reviewed;         238 AA.
AC   Q9NVV5; B4DPX2; C9J569; Q5T2H2; Q6N047; Q7Z378; Q8TB14; Q9Y3A9; Q9Y5B4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 3.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Androgen-induced gene 1 protein;
DE            Short=AIG-1;
DE   AltName: Full=Fatty acid esters of hydroxy fatty acids hydrolase AIG1 {ECO:0000303|PubMed:27018888};
DE            Short=FAHFA hydrolase AIG1 {ECO:0000303|PubMed:27018888};
DE            EC=3.1.-.- {ECO:0000269|PubMed:27018888};
GN   Name=AIG1; ORFNames=CGI-103;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Hair follicle dermal papilla;
RX   PubMed=11266118;
RA   Seo J., Kim J., Kim M.;
RT   "Cloning of androgen-inducible gene 1 (AIG1) from human dermal papilla
RT   cells.";
RL   Mol. Cells 11:35-40(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC   TISSUE=Prostate, and Rectum tumor;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP   TOPOLOGY MODEL, SITE, AND MUTAGENESIS OF THR-43 AND HIS-134.
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). {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-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC         hexadecenoate + 5-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52092,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC         ChEBI:CHEBI:136369, ChEBI:CHEBI:136370;
CC         Evidence={ECO:0000269|PubMed:27018888};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093;
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       Q9NVV5; Q96PM5: RCHY1; NbExp=4; IntAct=EBI-3942989, EBI-947779;
CC       Q9NVV5-2; P05090: APOD; NbExp=3; IntAct=EBI-11957045, EBI-715495;
CC       Q9NVV5-2; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-11957045, EBI-4290634;
CC       Q9NVV5-2; Q13520: AQP6; NbExp=3; IntAct=EBI-11957045, EBI-13059134;
CC       Q9NVV5-2; O43315: AQP9; NbExp=3; IntAct=EBI-11957045, EBI-17444777;
CC       Q9NVV5-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-11957045, EBI-11343438;
CC       Q9NVV5-2; P07307-3: ASGR2; NbExp=3; IntAct=EBI-11957045, EBI-12808270;
CC       Q9NVV5-2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-11957045, EBI-747430;
CC       Q9NVV5-2; Q13323: BIK; NbExp=3; IntAct=EBI-11957045, EBI-700794;
CC       Q9NVV5-2; P19397: CD53; NbExp=3; IntAct=EBI-11957045, EBI-6657396;
CC       Q9NVV5-2; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-11957045, EBI-1045797;
CC       Q9NVV5-2; O95471: CLDN7; NbExp=3; IntAct=EBI-11957045, EBI-740744;
CC       Q9NVV5-2; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-11957045, EBI-18013275;
CC       Q9NVV5-2; P00387: CYB5R3; NbExp=3; IntAct=EBI-11957045, EBI-1046040;
CC       Q9NVV5-2; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-11957045, EBI-2680384;
CC       Q9NVV5-2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11957045, EBI-781551;
CC       Q9NVV5-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11957045, EBI-18304435;
CC       Q9NVV5-2; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-11957045, EBI-12142257;
CC       Q9NVV5-2; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-11957045, EBI-712073;
CC       Q9NVV5-2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11957045, EBI-13345167;
CC       Q9NVV5-2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11957045, EBI-11721746;
CC       Q9NVV5-2; P31937: HIBADH; NbExp=3; IntAct=EBI-11957045, EBI-11427100;
CC       Q9NVV5-2; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-11957045, EBI-18053395;
CC       Q9NVV5-2; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-11957045, EBI-725665;
CC       Q9NVV5-2; P48051: KCNJ6; NbExp=3; IntAct=EBI-11957045, EBI-12017638;
CC       Q9NVV5-2; P43628: KIR2DL3; NbExp=3; IntAct=EBI-11957045, EBI-8632435;
CC       Q9NVV5-2; Q13571: LAPTM5; NbExp=3; IntAct=EBI-11957045, EBI-2865663;
CC       Q9NVV5-2; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-11957045, EBI-17490413;
CC       Q9NVV5-2; Q9H400: LIME1; NbExp=3; IntAct=EBI-11957045, EBI-2830566;
CC       Q9NVV5-2; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-11957045, EBI-10329546;
CC       Q9NVV5-2; Q9GZY8-5: MFF; NbExp=6; IntAct=EBI-11957045, EBI-11956541;
CC       Q9NVV5-2; Q9HC36: MRM3; NbExp=3; IntAct=EBI-11957045, EBI-1045440;
CC       Q9NVV5-2; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-11957045, EBI-716063;
CC       Q9NVV5-2; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-11957045, EBI-3920694;
CC       Q9NVV5-2; O75396: SEC22B; NbExp=3; IntAct=EBI-11957045, EBI-1058865;
CC       Q9NVV5-2; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-11957045, EBI-12811757;
CC       Q9NVV5-2; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-11957045, EBI-5235586;
CC       Q9NVV5-2; P27105: STOM; NbExp=3; IntAct=EBI-11957045, EBI-1211440;
CC       Q9NVV5-2; Q16623: STX1A; NbExp=3; IntAct=EBI-11957045, EBI-712466;
CC       Q9NVV5-2; Q8WY91: THAP4; NbExp=3; IntAct=EBI-11957045, EBI-726691;
CC       Q9NVV5-2; P07204: THBD; NbExp=3; IntAct=EBI-11957045, EBI-941422;
CC       Q9NVV5-2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-11957045, EBI-2821497;
CC       Q9NVV5-2; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-11957045, EBI-11742770;
CC       Q9NVV5-2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11957045, EBI-6447886;
CC       Q9NVV5-2; Q15836: VAMP3; NbExp=3; IntAct=EBI-11957045, EBI-722343;
CC       Q9NVV5-2; O95292: VAPB; NbExp=3; IntAct=EBI-11957045, EBI-1188298;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27018888};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q9NVV5-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVV5-1; Sequence=VSP_060695;
CC       Name=3;
CC         IsoId=Q9NVV5-3; Sequence=VSP_060690;
CC       Name=4;
CC         IsoId=Q9NVV5-4; Sequence=VSP_060689;
CC       Name=5;
CC         IsoId=Q9NVV5-5; Sequence=VSP_060693, VSP_060694;
CC       Name=6;
CC         IsoId=Q9NVV5-6; Sequence=VSP_060691, VSP_060692;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, ovary, testis, liver,
CC       and kidney, at lower levels in spleen, prostate, brain, skeletal
CC       muscle, pancreas, small intestine and colon, and undetected in
CC       peripheral blood leukocytes, thymus, lung and placenta. AIG1 expression
CC       is higher in hair follicles from males than from females.
CC       {ECO:0000269|PubMed:11266118}.
CC   -!- INDUCTION: By dihydrotestosterone (DHT). {ECO:0000269|PubMed:11266118}.
CC   -!- SIMILARITY: Belongs to the AIG1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD34098.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAE45823.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF153605; AAD41087.1; -; mRNA.
DR   EMBL; AF151861; AAD34098.1; ALT_FRAME; mRNA.
DR   EMBL; AK001347; BAA91640.1; -; mRNA.
DR   EMBL; BX538067; CAD97997.1; -; mRNA.
DR   EMBL; BX640703; CAE45823.1; ALT_INIT; mRNA.
DR   EMBL; AK298533; BAG60734.1; -; mRNA.
DR   EMBL; AL023581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL450335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025278; AAH25278.1; -; mRNA.
DR   CCDS; CCDS5198.1; -. [Q9NVV5-2]
DR   CCDS; CCDS69215.1; -. [Q9NVV5-6]
DR   CCDS; CCDS69216.1; -. [Q9NVV5-5]
DR   CCDS; CCDS94014.1; -. [Q9NVV5-1]
DR   RefSeq; NP_001273516.1; NM_001286587.1. [Q9NVV5-4]
DR   RefSeq; NP_001273517.1; NM_001286588.1. [Q9NVV5-6]
DR   RefSeq; NP_001273518.1; NM_001286589.1. [Q9NVV5-5]
DR   RefSeq; NP_057192.2; NM_016108.3. [Q9NVV5-2]
DR   AlphaFoldDB; Q9NVV5; -.
DR   BioGRID; 119519; 60.
DR   IntAct; Q9NVV5; 52.
DR   MINT; Q9NVV5; -.
DR   STRING; 9606.ENSP00000350509; -.
DR   BindingDB; Q9NVV5; -.
DR   SwissLipids; SLP:000001682; -.
DR   TCDB; 9.B.203.1.1; the aig1 lipid hydrolase (aig1) family.
DR   iPTMnet; Q9NVV5; -.
DR   PhosphoSitePlus; Q9NVV5; -.
DR   SwissPalm; Q9NVV5; -.
DR   BioMuta; AIG1; -.
DR   DMDM; 56748615; -.
DR   EPD; Q9NVV5; -.
DR   jPOST; Q9NVV5; -.
DR   MassIVE; Q9NVV5; -.
DR   MaxQB; Q9NVV5; -.
DR   PaxDb; 9606-ENSP00000350509; -.
DR   PeptideAtlas; Q9NVV5; -.
DR   ProteomicsDB; 4823; -.
DR   ProteomicsDB; 82866; -. [Q9NVV5-1]
DR   ProteomicsDB; 82867; -. [Q9NVV5-2]
DR   ProteomicsDB; 82868; -. [Q9NVV5-3]
DR   ProteomicsDB; 82869; -. [Q9NVV5-4]
DR   ProteomicsDB; 82870; -. [Q9NVV5-5]
DR   Pumba; Q9NVV5; -.
DR   TopDownProteomics; Q9NVV5-4; -. [Q9NVV5-4]
DR   Antibodypedia; 53852; 168 antibodies from 30 providers.
DR   DNASU; 51390; -.
DR   Ensembl; ENST00000275235.8; ENSP00000275235.4; ENSG00000146416.19. [Q9NVV5-1]
DR   Ensembl; ENST00000357847.9; ENSP00000350509.4; ENSG00000146416.19. [Q9NVV5-2]
DR   Ensembl; ENST00000494282.6; ENSP00000473952.1; ENSG00000146416.19. [Q9NVV5-5]
DR   Ensembl; ENST00000629020.2; ENSP00000485875.1; ENSG00000146416.19. [Q9NVV5-6]
DR   GeneID; 51390; -.
DR   KEGG; hsa:51390; -.
DR   MANE-Select; ENST00000357847.9; ENSP00000350509.4; NM_016108.4; NP_057192.2.
DR   UCSC; uc003qjg.5; human. [Q9NVV5-2]
DR   AGR; HGNC:21607; -.
DR   CTD; 51390; -.
DR   DisGeNET; 51390; -.
DR   GeneCards; AIG1; -.
DR   HGNC; HGNC:21607; AIG1.
DR   HPA; ENSG00000146416; Tissue enhanced (liver).
DR   MIM; 608514; gene.
DR   neXtProt; NX_Q9NVV5; -.
DR   OpenTargets; ENSG00000146416; -.
DR   PharmGKB; PA134991331; -.
DR   VEuPathDB; HostDB:ENSG00000146416; -.
DR   eggNOG; KOG3989; Eukaryota.
DR   GeneTree; ENSGT00940000158696; -.
DR   HOGENOM; CLU_073346_0_0_1; -.
DR   InParanoid; Q9NVV5; -.
DR   OMA; MRTTHHK; -.
DR   OrthoDB; 5395567at2759; -.
DR   PhylomeDB; Q9NVV5; -.
DR   TreeFam; TF318170; -.
DR   PathwayCommons; Q9NVV5; -.
DR   SignaLink; Q9NVV5; -.
DR   BioGRID-ORCS; 51390; 8 hits in 1150 CRISPR screens.
DR   ChiTaRS; AIG1; human.
DR   GeneWiki; AIG1; -.
DR   GenomeRNAi; 51390; -.
DR   Pharos; Q9NVV5; Tbio.
DR   PRO; PR:Q9NVV5; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9NVV5; Protein.
DR   Bgee; ENSG00000146416; Expressed in buccal mucosa cell and 188 other cell types or tissues.
DR   ExpressionAtlas; Q9NVV5; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IMP:UniProtKB.
DR   GO; GO:0042758; P:long-chain fatty acid catabolic process; IMP:UniProtKB.
DR   InterPro; IPR006838; ADTRP_AIG1.
DR   PANTHER; PTHR10989:SF11; ANDROGEN-INDUCED GENE 1 PROTEIN; 1.
DR   PANTHER; PTHR10989; ANDROGEN-INDUCED PROTEIN 1-RELATED; 1.
DR   Pfam; PF04750; Far-17a_AIG1; 1.
DR   Genevisible; Q9NVV5; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Hydrolase; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..238
FT                   /note="Androgen-induced gene 1 protein"
FT                   /id="PRO_0000190098"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        13..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        45..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..156
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   TRANSMEM        194..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27018888"
FT   SITE            43
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:27018888"
FT   SITE            134
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:27018888"
FT   VAR_SEQ         1..10
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305|PubMed:10810093"
FT                   /id="VSP_060689"
FT   VAR_SEQ         48..99
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060690"
FT   VAR_SEQ         134
FT                   /note="H -> L (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060691"
FT   VAR_SEQ         135..238
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060692"
FT   VAR_SEQ         135..137
FT                   /note="TTV -> FKA (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060693"
FT   VAR_SEQ         138..238
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060694"
FT   VAR_SEQ         227..238
FT                   /note="SMEEEKEKPKLE -> KPPSWQDMKIKFMYLGPSS (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060695"
FT   VARIANT         151
FT                   /note="Q -> E (in dbSNP:rs1053193)"
FT                   /id="VAR_057502"
FT   MUTAGEN         43
FT                   /note="T->A: Loss of hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:27018888"
FT   MUTAGEN         134
FT                   /note="H->A: Loss of hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:27018888"
FT   CONFLICT        70
FT                   /note="S -> I (in Ref. 1; AAD41087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="I -> F (in Ref. 3; BAA91640)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  27458 MW;  DF5D5B8FC41A2C95 CRC64;
     MALVPCQVLR MAILLSYCSI LCNYKAIEMP SHQTYGGSWK FLTFIDLVIQ AVFFGICVLT
     DLSSLLTRGS GNQEQERQLK KLISLRDWML AVLAFPVGVF VVAVFWIIYA YDREMIYPKL
     LDNFIPGWLN HGMHTTVLPF ILIEMRTSHH QYPSRSSGLT AICTFSVGYI LWVCWVHHVT
     GMWVYPFLEH IGPGARIIFF GSTTILMNFL YLLGEVLNNY IWDTQKSMEE EKEKPKLE
//