ADTRP_RAT
ID ADTRP_RAT Reviewed; 230 AA.
AC Q5M828; Q7TP74;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
DE AltName: Full=Liver regeneration-related protein LRRG140;
GN Name=Adtrp; ORFNames=Aa2-020;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5M828-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5M828-2; Sequence=VSP_013635, VSP_013636, VSP_013637;
CC -!- SIMILARITY: Belongs to the AIG1 family. {ECO:0000305}.
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DR EMBL; AY325171; AAP92572.1; -; mRNA.
DR EMBL; BC088287; AAH88287.1; -; mRNA.
DR RefSeq; NP_001014166.1; NM_001014144.1. [Q5M828-1]
DR RefSeq; XP_006253895.1; XM_006253833.3. [Q5M828-1]
DR AlphaFoldDB; Q5M828; -.
DR STRING; 10116.ENSRNOP00000057148; -.
DR PaxDb; Q5M828; -.
DR PRIDE; Q5M828; -.
DR Ensembl; ENSRNOT00000019478; ENSRNOP00000019478; ENSRNOG00000014481. [Q5M828-2]
DR Ensembl; ENSRNOT00000115307; ENSRNOP00000076653; ENSRNOG00000014481. [Q5M828-1]
DR GeneID; 361228; -.
DR KEGG; rno:361228; -.
DR UCSC; RGD:1305679; rat. [Q5M828-1]
DR CTD; 84830; -.
DR RGD; 1305679; Adtrp.
DR eggNOG; KOG3989; Eukaryota.
DR GeneTree; ENSGT00940000158284; -.
DR HOGENOM; CLU_073346_2_0_1; -.
DR InParanoid; Q5M828; -.
DR OrthoDB; 1482757at2759; -.
DR PhylomeDB; Q5M828; -.
DR TreeFam; TF318170; -.
DR PRO; PR:Q5M828; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000014481; Expressed in liver and 17 other tissues.
DR ExpressionAtlas; Q5M828; baseline and differential.
DR Genevisible; Q5M828; RN.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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:RGD.
DR GO; GO:0016787; F:hydrolase activity; ISO:RGD.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISO:RGD.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:RGD.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; ISO:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:RGD.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; ISO:RGD.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; ISO:RGD.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; ISO:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
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..230
FT /note="Androgen-dependent TFPI-regulating protein"
FT /id="PRO_0000190103"
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..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96IZ2"
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..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"
FT VAR_SEQ 52..54
FT /note="LLQ -> APESECVNPSESSEPQSSFCDQSRSMVRKDGE (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013635"
FT VAR_SEQ 131..140
FT /note="HTSIFPFSLA -> NNCSISTTFS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013636"
FT VAR_SEQ 141..230
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013637"
SQ SEQUENCE 230 AA; 26904 MW; E3C36DED2E175021 CRC64;
MTKTTTCLYH FVVLNWYIFL NYYIPQIGKD EEKLKEFHDG GRSKYLTLLN LLLQAVFFGV
ACLDDVLKRV IGRKDIKFIT YFRDLLFTTL AFPLSTFVFL VFWSLFHYDR SLVYPKGLDD
FFPAWVNHAM HTSIFPFSLA ETVLRPHNYP SKKLGLSLLG ACNFAYIIRI LWRYVQTGNW
VYPVFASLSP LGIILFFSAS YILSASLYLF GEKINHWKWG ATVKPRMKKN
