ID H0ZJK1_TAEGU Unreviewed; 805 AA.
AC H0ZJK1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=PLA2G6 {ECO:0000313|Ensembl:ENSTGUP00000010770.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010770.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000010770.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000010770.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
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DR AlphaFoldDB; H0ZJK1; -.
DR STRING; 59729.ENSTGUP00000010770; -.
DR Ensembl; ENSTGUT00000010883.2; ENSTGUP00000010770.2; ENSTGUG00000010433.2.
DR GeneTree; ENSGT00940000158756; -.
DR HOGENOM; CLU_010817_0_0_1; -.
DR InParanoid; H0ZJK1; -.
DR OMA; DYWIPSD; -.
DR OrthoDB; 518048at2759; -.
DR TreeFam; TF319230; -.
DR Proteomes; UP000007754; Chromosome 1A.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:Ensembl.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:Ensembl.
DR GO; GO:0017171; F:serine hydrolase activity; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR CDD; cd07212; Pat_PNPLA9; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047148; PLPL9.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24139:SF34; 85_88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 151..183
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 218..250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 315..347
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 348..380
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 481..665
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 89856 MW; E3A7A5A85F2A694D CRC64;
MQFFGRLLDT FSSVTQIFSN PYRVREVPAA EYGGHACLRE EGRVALYKNS LSRSWDCLLV
NPQSPQVAFR LFQLDNEADA VVYFEQYARQ LRPFYESSSQ PLSLEELQQL SDCIRSYPSW
SPAHIAVEFG RRESFRHNHI LSCVNSTDSE DGCTPLHLAC RKGDVECLLE LLECHARVDI
TDKNGETVFH YAVRGNNPQI IELLGKPPTT GLDHLSHEGL TALHLACQLG KEDMVRSLLK
CHASCSVVGT LGYPIHTALK FSQKGCAQAI LEADASQVCS KDPRYDATPL HWAKKAEMTR
LLLEYGSEVN VSSRTADMAL HIAVQRGRLD CAMVLLTHGA HTNARGHDGN TPLHLAMKHD
HLDLIKAIIV FGGDVEIPND FGETPGLLAA RSSKGANRKV LLDLLQIVGT ERCHPPPNPE
SPSLAPSAAS FLEGQPSSRS NLNSLGYKDL LYISTTLGQL LKAQDVVDMP REARRNQDRL
LCLDGGGIRG LVLIQLLLAI EKAAGRPIRE IFDWIAGTST GGILALAIVH GKSMDYMRCL
YFRMKDMVFR GSRPYESEPL DEFLKKEFGE NTKMTDVRRP KVMVTGTLCD RQPAELHLFR
NYPVPETKRS TEYKTSASFQ PLTRPEEQLV WRAARCSGAA PTYFRPIGRF LDGGLLANNP
TLDAMAEIHE YNKTLIKKGR KQEVRKLGLV VSLGTGKPPQ VPVSSVDVFR PSNPWELAKT
VFGARELGKM VVDCCTDADG PAVDRARAWC EMTDVPYFRL SPQLHTEVML DEVNDAVLVN
ALWDTQLYIY QQREQFEQLV QHLCS
//
