ID F7HN22_MACMU Unreviewed; 935 AA.
AC F7HN22;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=PLA2G6 {ECO:0000313|VGNC:VGNC:76157};
GN Synonyms=TMEM184B {ECO:0000313|Ensembl:ENSMMUP00000003633.4};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000003633.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000003633.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000003633.4};
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; F7HN22; -.
DR SMR; F7HN22; -.
DR STRING; 9544.ENSMMUP00000003633; -.
DR Ensembl; ENSMMUT00000003843.4; ENSMMUP00000003633.4; ENSMMUG00000002701.4.
DR VEuPathDB; HostDB:ENSMMUG00000002701; -.
DR VGNC; VGNC:76157; PLA2G6.
DR eggNOG; KOG0513; Eukaryota.
DR GeneTree; ENSGT00940000158756; -.
DR InParanoid; F7HN22; -.
DR TreeFam; TF319230; -.
DR Proteomes; UP000006718; Chromosome 10.
DR Bgee; ENSMMUG00000002701; Expressed in cerebellar cortex and 21 other cell types or tissues.
DR ExpressionAtlas; F7HN22; baseline.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IBA:GO_Central.
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; 1.
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; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
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:UP000006718};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 250..283
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 318..350
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 415..447
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 448..480
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 580..764
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 935 AA; 102618 MW; 72CC3419B5F40A10 CRC64;
MGDQEGDQSG SRHPCLLIQA CSWPSWRSVG PSPKSTRPAC RWVRALWLLA TRTSSSVWRC
SLQPWPCGTP SPTRSMLTRD WTHKTEGEGG GASPPAPQKM QFFGRLVNTL SGVTNLFSNP
FRVKEVAVAD YTSSDRVREE GQLILFQNTP NRTWDCVLVN PRSPQSGFRL FQLGLEADAL
VNFQQYSSQL LPFYESSPQV LHTEVLQHLT DLIRNHPSWS VAHLAVELGI RECFHHSRVI
SCANCTENEE GCTPLHLACR KGDGEILVEL VQYCHAQMDV TDNKGETVFH YAVQGDNSQV
LQLLGKNAVA GLNQVNNQGL TPLHLACQLG KQEMVRVLLL CNARCNIMGP NGYPIHSAMK
FSQKGCAEMI ISMDSSQIHS KDPRYGASPL HWAKNAEMAR MLLKRGCNVN STSSAGNTAL
HVAVMRNRFD CAIVLLTHGA NADAHGEHGN TPLHLAMSKD NVEMIKALIV FGAEVDTPND
FGETPTFLAS KISRLDTRKA ILTLLRTVGA EYCSPPIHGV PAEQGFAAPH HPFSLERAQP
PPISLNNLEL QDLMHISRAR KPAFILGSMR DEKRTHDHLL CLDGGGVKGL IIIQLLIAIE
KASGVATKDL FDWVAGTSTG GILALAILHG KSMAYMRGVY FRMKDEVFRG SRPYESGPLE
EFLKREFGEH TKMTDVKKPK VMLTGTLSDR QPAELHLFRN YDAPETVREP RFNQNVNLRP
PAQPSDQLVW RAARSSGAAP TYFRPNGRFL DGGLLANNPT LDAMTEIHEY NQDLIRKGQA
NKVKKLSIVV SLGTGRSPQV PVTCVDVFRP SNPWELAKTV FGAKELGKMV VDCVSMGPSP
RPLPSGSAAQ VDGFPSSCGA FGVGGDSRAV SIAFSQLEGE RVPNSESQGR VGTLSDHQQG
GFQTLFSCRS LSANIAQCRS PEWTKAPEWA GHSPL
//
