AIG1_MOUSE
ID AIG1_MOUSE Reviewed; 238 AA.
AC Q9D8B1; Q8CI90; Q9CW23;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 125.
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:0000250|UniProtKB:Q9NVV5};
DE Short=FAHFA hydrolase AIG1 {ECO:0000250|UniProtKB:Q9NVV5};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9NVV5};
GN Name=Aig1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Small intestine;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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). {ECO:0000250|UniProtKB:Q9NVV5}.
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
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:0000250|UniProtKB:Q9NVV5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NVV5};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8B1-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8B1-1; Sequence=VSP_060696;
CC -!- INDUCTION: By dihydrotestosterone (DHT). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AIG1 family. {ECO:0000305}.
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DR EMBL; AK005332; BAB23957.1; -; mRNA.
DR EMBL; AK008210; BAB25534.1; -; mRNA.
DR EMBL; BC035305; AAH35305.1; -; mRNA.
DR CCDS; CCDS23703.1; -. [Q9D8B1-1]
DR CCDS; CCDS83682.1; -. [Q9D8B1-2]
DR RefSeq; NP_001334291.1; NM_001347362.1. [Q9D8B1-2]
DR RefSeq; NP_079722.1; NM_025446.4. [Q9D8B1-1]
DR AlphaFoldDB; Q9D8B1; -.
DR STRING; 10090.ENSMUSP00000019942; -.
DR PhosphoSitePlus; Q9D8B1; -.
DR SwissPalm; Q9D8B1; -.
DR MaxQB; Q9D8B1; -.
DR PaxDb; Q9D8B1; -.
DR PRIDE; Q9D8B1; -.
DR ProteomicsDB; 296347; -. [Q9D8B1-2]
DR ProteomicsDB; 296348; -. [Q9D8B1-2]
DR Antibodypedia; 53852; 153 antibodies from 30 providers.
DR DNASU; 66253; -.
DR Ensembl; ENSMUST00000019942; ENSMUSP00000019942; ENSMUSG00000019806. [Q9D8B1-1]
DR Ensembl; ENSMUST00000162610; ENSMUSP00000125366; ENSMUSG00000019806. [Q9D8B1-2]
DR GeneID; 66253; -.
DR KEGG; mmu:66253; -.
DR UCSC; uc007elc.1; mouse. [Q9D8B1-2]
DR CTD; 51390; -.
DR MGI; MGI:1913503; Aig1.
DR VEuPathDB; HostDB:ENSMUSG00000019806; -.
DR eggNOG; KOG3989; Eukaryota.
DR GeneTree; ENSGT00940000158696; -.
DR HOGENOM; CLU_073346_0_0_1; -.
DR InParanoid; Q9D8B1; -.
DR OMA; MRTTHHK; -.
DR OrthoDB; 1482757at2759; -.
DR PhylomeDB; Q9D8B1; -.
DR TreeFam; TF318170; -.
DR BioGRID-ORCS; 66253; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Aig1; mouse.
DR PRO; PR:Q9D8B1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D8B1; protein.
DR Bgee; ENSMUSG00000019806; Expressed in olfactory epithelium and 233 other tissues.
DR ExpressionAtlas; Q9D8B1; baseline and differential.
DR Genevisible; Q9D8B1; MM.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; 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 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_0000190099"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 13..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..44
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..124
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 157..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..193
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT SITE 43
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT SITE 134
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV5"
FT VAR_SEQ 227..238
FT /note="SIEEEKEKPKLE -> TKAPSCQDTQSSLSCAKPVQNLCKDTFMLEGGKARA
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060696"
FT CONFLICT 134
FT /note="H -> N (in Ref. 1; BAB23957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 27397 MW; 23BAE63F35E0CF05 CRC64;
MALVPCQVLR VAILLSYCSI LCNYKAIEMP SHQTYGGSWK FLTFIDLVIQ AVFFGICVLT
DLSSLLTRGS GNQEQERQLR KLISLRDWTL AVLAFPVGVF VVAVFWTIYA YDREMIYPRL
LDNFIPGWLN HGMHTTVLPF ILIEMRTSHH QYPSRSSGLA AICTFSVGYI LWVCWIHHVT
GMWVYPFLEH IGSGARIIFF GSTTILMNFL YLLGEVLNSY IWDTQRSIEE EKEKPKLE
