ID   J3KMZ3_HUMAN            Unreviewed;       150 AA.
AC   J3KMZ3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   16-JAN-2019, entry version 51.
DE   RecName: Full=Phospholipase A(2) {ECO:0000256|RuleBase:RU361236};
DE            EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236};
GN   Name=PLA2G2C {ECO:0000313|Ensembl:ENSP00000247992};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000247992, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000247992, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S.,
RA   Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J.,
RA   James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K.,
RA   Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G.,
RA   Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J.,
RA   Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L.,
RA   Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J.,
RA   Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A.,
RA   Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K.,
RA   Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N.,
RA   Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S.,
RA   Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L.,
RA   Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.,
RA   Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T.,
RA   Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R.,
RA   Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P.,
RA   Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D.,
RA   Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000247992}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2012) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-
CC         acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC         Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168;
CC         EC=3.1.1.4; Evidence={ECO:0000256|RuleBase:RU361236};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU361236};
CC       Note=Binds 1 Ca(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU361236};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361236,
CC       ECO:0000256|SAAS:SAAS00331951}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
CC       {ECO:0000256|RuleBase:RU003654, ECO:0000256|SAAS:SAAS00587348}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; Z98257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; J3KMZ3; -.
DR   STRING; 9606.ENSP00000247992; -.
DR   iPTMnet; J3KMZ3; -.
DR   PaxDb; J3KMZ3; -.
DR   PRIDE; J3KMZ3; -.
DR   Ensembl; ENST00000247992; ENSP00000247992; ENSG00000187980.
DR   UCSC; uc009vpq.1; human.
DR   EuPathDB; HostDB:ENSG00000187980.6; -.
DR   HGNC; HGNC:9032; PLA2G2C.
DR   OpenTargets; ENSG00000187980; -.
DR   eggNOG; KOG4087; Eukaryota.
DR   eggNOG; ENOG411283D; LUCA.
DR   GeneTree; ENSGT00910000144349; -.
DR   OrthoDB; 1422829at2759; -.
DR   PhylomeDB; J3KMZ3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000187980; Expressed in 52 organ(s), highest expression level in muscle layer of sigmoid colon.
DR   ExpressionAtlas; J3KMZ3; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
DR   GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU361236};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00479786};
KW   Hydrolase {ECO:0000256|RuleBase:RU361236};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361236};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Secreted {ECO:0000256|RuleBase:RU361236,
KW   ECO:0000256|SAAS:SAAS00479782};
KW   Signal {ECO:0000256|RuleBase:RU361236}.
FT   SIGNAL        1     16       {ECO:0000256|RuleBase:RU361236}.
FT   CHAIN        17    150       Phospholipase A(2).
FT                                {ECO:0000256|RuleBase:RU361236}.
FT                                /FTId=PRO_5001390687.
FT   DOMAIN       22    144       PA2c. {ECO:0000259|SMART:SM00085}.
SQ   SEQUENCE   150 AA;  16837 MW;  40E9357EAB9B1C58 CRC64;
     MLIATSFFLF FSSVVAAPTH SSFWQFQRRV KHITGRSAFF SYYGYGCYCG LGDKGIPVDD
     TDSPSSPSPY EKLKEFSCQP VLNSYQFHIV NGAVVCGCTL GPGASCHCRL KACECDKQSV
     HCFKESLPTY EKNFKQFSSQ PRCGRHKPWC
//