AIG1_HUMAN
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 03-AUG-2022, entry version 150.
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 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 BioMuta; AIG1; -.
DR DMDM; 56748615; -.
DR EPD; Q9NVV5; -.
DR jPOST; Q9NVV5; -.
DR MassIVE; Q9NVV5; -.
DR MaxQB; Q9NVV5; -.
DR PaxDb; Q9NVV5; -.
DR PeptideAtlas; Q9NVV5; -.
DR PRIDE; 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 TopDownProteomics; Q9NVV5-4; -. [Q9NVV5-4]
DR Antibodypedia; 53852; 153 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 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; 1482757at2759; -.
DR PhylomeDB; Q9NVV5; -.
DR TreeFam; TF318170; -.
DR PathwayCommons; Q9NVV5; -.
DR SignaLink; Q9NVV5; -.
DR BioGRID-ORCS; 51390; 6 hits in 1072 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 186 other tissues.
DR ExpressionAtlas; Q9NVV5; baseline and differential.
DR Genevisible; Q9NVV5; HS.
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: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; 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..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
