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Database: UniProt
Entry: C3ZUN9_BRAFL
LinkDB: C3ZUN9_BRAFL
Original site: C3ZUN9_BRAFL 
ID   C3ZUN9_BRAFL            Unreviewed;       687 AA.
AC   C3ZUN9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase {ECO:0000256|ARBA:ARBA00013201};
DE            EC=3.1.1.47 {ECO:0000256|ARBA:ARBA00013201};
GN   ORFNames=BRAFLDRAFT_94644 {ECO:0000313|EMBL:EEN43751.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN43751.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN43751.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN43751.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-
CC         hexadecyl-sn-glycero-3-phosphate + acetate + H(+);
CC         Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385;
CC         Evidence={ECO:0000256|ARBA:ARBA00035804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705;
CC         Evidence={ECO:0000256|ARBA:ARBA00035804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC         Evidence={ECO:0000256|ARBA:ARBA00023721};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC         Evidence={ECO:0000256|ARBA:ARBA00023721};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC         Evidence={ECO:0000256|ARBA:ARBA00023737};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC         Evidence={ECO:0000256|ARBA:ARBA00023737};
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DR   EMBL; GG666684; EEN43751.1; -; Genomic_DNA.
DR   RefSeq; XP_002587740.1; XM_002587694.1.
DR   AlphaFoldDB; C3ZUN9; -.
DR   InParanoid; C3ZUN9; -.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR24401:SF29; DUF6729 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24401; SI:CH211-243P7.3-RELATED; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   4: Predicted;
FT   DOMAIN          230..352
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
FT   REGION          383..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  72808 MW;  8AF25817FD65F6E2 CRC64;
     MKYWLAHSWL RRFAEGYGDK MPDKDAINLP SSMTRTGSCN LLPLANGNDV VHIFALPEEQ
     LSRSQSWPVG EAPTVLGADV FEIKTVGDLE DIHYHLKENG RINGLNINTA CAKCLQTVSD
     IILREKTAGR TFVVLSPYIS FMNDGDTDVT DVAIKECEIV YARIIGDGKP KNLLVGHVEV
     VGHVQPSLGS LFPCPEESCV KIILAFTDSI CKYVSNHATF SSDILFSLNA HPGASVYDLT
     SDISRHPFVE PDLVFLHAGT NCLPMHRPLS RTLDDFSYLI SVTKSRFPSA SVVISSILPR
     FDSEVYDRRR SELNSHLLRL CSSQGVFLLD NGSRARRAMF SVDGLHLSRA GNISYAKYLS
     FSLSHYLQLH RRSCQHRFTL RGEEWPGLGT DGRSGKKDKE HPGEEQKSGE YQGQVEWARV
     VRQGGPVARP APGKVEGKGP SQPRGVPVAR AAPGKVEGGN AGKGPSQPRG VPVARAAPGK
     VEGKGPSQPR GVPVARAAPG KVEGGNAGKG PSQPRGVPVA RAAPGKVEGG NAGKGPSRPR
     EVAVASAAPG KVVGCSVGKG PSRPRGVPVA RAAPGKVVGG NAGKGPSRPR GVPVPQPRLP
     PGKVEGGSAG KGPSRPRGGP VPKPRVASGK VEGGSVGKGP SRPRGGPVPK PRVASGKVPR
     GVQHGTWVWC RPVVSEVWKS SVSTAGC
//
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