PA2GC_HUMAN
ID PA2GC_HUMAN Reviewed; 149 AA.
AC Q5R387; Q7M4M6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative inactive group IIC secretory phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase-like protein GIIC;
DE Flags: Precursor;
GN Name=PLA2G2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-60.
RX PubMed=2708461; DOI=10.1002/jcb.240390312;
RA Seilhamer J.J., Randall T.L., Johnson L.K., Heinzmann C., Klisak I.,
RA Sparkes R.S., Lusis A.J.;
RT "Novel gene exon homologous to pancreatic phospholipase A2: sequence and
RT chromosomal mapping of both human genes.";
RL J. Cell. Biochem. 39:327-337(1989).
CC -!- FUNCTION: Inactive phospholipase. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- CAUTION: Ser-67 is present instead of the conserved His which is one of
CC the active site residues. It is therefore expected that this protein
CC lacks catalytic activity. {ECO:0000305}.
CC -!- CAUTION: The N-terminal region is predicted based on cross-species
CC conservation and limited EST data. Exact gene structure in this region
CC is unclear. {ECO:0000305}.
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DR EMBL; Z98257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A60718; A60718.
DR RefSeq; NP_001354898.1; NM_001367969.2.
DR AlphaFoldDB; Q5R387; -.
DR SMR; Q5R387; -.
DR STRING; 9606.ENSP00000247992; -.
DR BindingDB; Q5R387; -.
DR ChEMBL; CHEMBL2097; -.
DR BioMuta; PLA2G2C; -.
DR DMDM; 300669681; -.
DR PRIDE; Q5R387; -.
DR TopDownProteomics; Q5R387; -.
DR Antibodypedia; 57806; 54 antibodies from 7 providers.
DR Ensembl; ENST00000429261.2; ENSP00000389335.2; ENSG00000187980.7.
DR Ensembl; ENST00000679259.1; ENSP00000504292.1; ENSG00000187980.7.
DR GeneID; 391013; -.
DR KEGG; hsa:391013; -.
DR MANE-Select; ENST00000679259.1; ENSP00000504292.1; NM_001367969.2; NP_001354898.1.
DR UCSC; uc057cyp.1; human.
DR CTD; 391013; -.
DR GeneCards; PLA2G2C; -.
DR HGNC; HGNC:9032; PLA2G2C.
DR HPA; ENSG00000187980; Not detected.
DR neXtProt; NX_Q5R387; -.
DR OpenTargets; ENSG00000187980; -.
DR VEuPathDB; HostDB:ENSG00000187980; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00910000144349; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; Q5R387; -.
DR OMA; CECDRQS; -.
DR PhylomeDB; Q5R387; -.
DR TreeFam; TF319283; -.
DR PathwayCommons; Q5R387; -.
DR Pharos; Q5R387; Tchem.
DR PRO; PR:Q5R387; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5R387; protein.
DR Bgee; ENSG00000187980; Expressed in muscle layer of sigmoid colon and 117 other tissues.
DR ExpressionAtlas; Q5R387; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:UniProt.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
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; Disulfide bond; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..149
FT /note="Putative inactive group IIC secretory phospholipase
FT A2"
FT /id="PRO_0000319946"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 44..142
FT /evidence="ECO:0000250"
FT DISULFID 77..107
FT /evidence="ECO:0000250"
FT DISULFID 95..112
FT /evidence="ECO:0000250"
FT DISULFID 97..105
FT /evidence="ECO:0000255"
FT VARIANT 139
FT /note="Q -> R (in dbSNP:rs6426616)"
FT /id="VAR_039057"
SQ SEQUENCE 149 AA; 16844 MW; EB386EF6DF86AA8B CRC64;
MKVIAILTLL LFCSPTHSSF WQFQRRVKHI TGRSAFFSYY GYGCYCGLGD KGIPVDDTDR
HSPSSPSPYE KLKEFSCQPV LNSYQFHIVN GAVVCGCTLG PGASCHCRLK ACECDKQSVH
CFKESLPTYE KNFKQFSSQP RCGRHKPWC
