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Database: UniProt
Entry: V8NZK5_OPHHA
LinkDB: V8NZK5_OPHHA
Original site: V8NZK5_OPHHA 
ID   V8NZK5_OPHHA            Unreviewed;       307 AA.
AC   V8NZK5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Phospholipase A1 member A {ECO:0000256|ARBA:ARBA00040696};
DE   Flags: Fragment;
GN   Name=PLA1A {ECO:0000313|EMBL:ETE67007.1};
GN   ORFNames=L345_07200 {ECO:0000313|EMBL:ETE67007.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE67007.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE67007.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE67007.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC         serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC         ChEBI:CHEBI:77342; Evidence={ECO:0000256|ARBA:ARBA00036960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC         Evidence={ECO:0000256|ARBA:ARBA00036960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC         Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC         Evidence={ECO:0000256|ARBA:ARBA00000834};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC         glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC         Evidence={ECO:0000256|ARBA:ARBA00036542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC         Evidence={ECO:0000256|ARBA:ARBA00036542};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE67007.1}.
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DR   EMBL; AZIM01001413; ETE67007.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8NZK5; -.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   PANTHER; PTHR11610:SF111; PHOSPHOLIPASE A1 MEMBER A; 1.
DR   Pfam; PF00151; Lipase; 2.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          3..129
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   DOMAIN          132..214
FT                   /note="Lipase"
FT                   /evidence="ECO:0000259|Pfam:PF00151"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE67007.1"
SQ   SEQUENCE   307 AA;  33605 MW;  63495E1EF2BD5D57 CRC64;
     ALGTKPSWID ALIQAFLEVA KVNVIAVDWV QGATAAYPTA VENVMKLGLE ISSFIRKLLA
     MGVPESSIHL IGVSLGAHVG GLVGQFYEGH LGRITALDPA GPKYTRASPE ERLDPGDALF
     VEAIHTDSDS YRYLICDHLR AVHFYISVLK DSCPVMAFPC SSYKNFLAGH CLDCSNPFLL
     SCPTIGLLDN GGLNVKTLPR EVKVYLATAA SAPYCVYHTL VKFHLQQRRT SDTNIEITFL
     TSNSSASTSF IIPKHQMLGK GLLIHSAPLC QIESVMLQHL HKFWKRNKDE SPIVGHFCTA
     SLPVDKK
//
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