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ABHGA_PONAB
ID   ABHGA_PONAB             Reviewed;         558 AA.
AC   Q5R6S0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Phosphatidylserine lipase ABHD16A {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q9Z1Q2};
DE   AltName: Full=Alpha/beta hydrolase domain-containing protein 16A {ECO:0000305};
DE            Short=Abhydrolase domain-containing protein 16A {ECO:0000305};
DE   AltName: Full=HLA-B-associated transcript 5 homolog {ECO:0000250|UniProtKB:O95870};
DE   AltName: Full=Monoacylglycerol lipase ABHD16A {ECO:0000305};
DE            EC=3.1.1.23 {ECO:0000250|UniProtKB:O95870};
GN   Name=ABHD16A {ECO:0000250|UniProtKB:O95870};
GN   Synonyms=BAT5 {ECO:0000250|UniProtKB:O95870};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis
CC       of phosphatidylserine to generate lysophosphatidylserine (LPS). LPS
CC       constitutes a class of signaling lipids that regulates immunological
CC       and neurological processes (By similarity). Has no activity towards
CC       diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (By
CC       similarity). Also has monoacylglycerol lipase activity, with preference
CC       for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-
CC       Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (By similarity).
CC       {ECO:0000250|UniProtKB:O95870, ECO:0000250|UniProtKB:Q9Z1Q2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         heptadecanoyl-sn-glycero-3-phosphoserine + H(+);
CC         Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC         serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC         ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC         phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-
CC         glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:84466, ChEBI:CHEBI:84467;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         heptadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC         glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC         phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC         ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC         myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC         3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72833, ChEBI:CHEBI:72837;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC         heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC         Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC         sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC         3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC         EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC         tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC         octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC         Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC         Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC         Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC         Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC         Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) +
CC         prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406,
CC         ChEBI:CHEBI:85232; Evidence={ECO:0000250|UniProtKB:O95870};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy-
CC         Delta(12,14)-prostaglandin J2 + glycerol + H(+);
CC         Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC         octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family.
CC       {ECO:0000305}.
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DR   EMBL; CR860415; CAH92540.1; -; mRNA.
DR   RefSeq; NP_001126487.1; NM_001133015.1.
DR   AlphaFoldDB; Q5R6S0; -.
DR   SMR; Q5R6S0; -.
DR   STRING; 9601.ENSPPYP00000018394; -.
DR   ESTHER; ponpy-q5r6s0; ABHD16.
DR   MEROPS; S09.065; -.
DR   GeneID; 100173474; -.
DR   KEGG; pon:100173474; -.
DR   CTD; 7920; -.
DR   eggNOG; KOG1553; Eukaryota.
DR   HOGENOM; CLU_040705_2_0_1; -.
DR   InParanoid; Q5R6S0; -.
DR   OMA; THCTQLP; -.
DR   OrthoDB; 580247at2759; -.
DR   TreeFam; TF314267; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR   GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR   GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR   GO; GO:0006660; P:phosphatidylserine catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR026604; ABHD16A.
DR   PANTHER; PTHR12277:SF54; PTHR12277:SF54; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..558
FT                   /note="Phosphatidylserine lipase ABHD16A"
FT                   /id="PRO_0000333743"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..558
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1Q2"
FT   DOMAIN          281..407
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        355
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT   ACT_SITE        430
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT   ACT_SITE        507
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N2K0"
SQ   SEQUENCE   558 AA;  63183 MW;  B3B07346BD64D521 CRC64;
     MAKLLSCVLG PRLYKIYRER DSERAPASVP ETPTAVTAPH SSSWDTYYQP RALEKHADSI
     LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT
     NPQYRQFITI LEATHRNQSS ENKRQLANYN FDFRSWPVDF HWEEPSSRKE SRGGPSRQGV
     ALLRPEPLHR GTADTLLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
     QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP
     LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDII IYAWSIGGFT
     ATWAAMSYPD VSAVILDASF DDLVPLALKV MPDSWRGLVT RTVRQHLNLN NAEQLCRYQG
     PVLLIRRTKD EIITTTVPED IMSNRGNDLL LKLLQHRYPR VMAEEGLRVV RQWLEASSQL
     EEASIYSRWE VEEDWCLSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE
     ATHCTPLPAQ NFQMPWHL
 
 
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