PG12B_MOUSE
ID PG12B_MOUSE Reviewed; 195 AA.
AC Q99P27;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Group XIIB secretory phospholipase A2-like protein;
DE AltName: Full=Group XIII secretory phospholipase A2-like protein;
DE Short=GXIII sPLA2-like;
DE AltName: Full=sPLA2-GXIIB;
DE Short=GXIIB;
DE Flags: Precursor;
GN Name=Pla2g12b; Synonyms=Pla2g13; ORFNames=Fksg71;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X DBA;
RA Wang Y.-G., Gong L.;
RT "Cloning and characterization of FKSG71, a novel gene encoding group XIII
RT secreted phospholipase A2.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Not known; does not seem to have catalytic activity.
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.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF339738; AAK01739.1; -; mRNA.
DR CCDS; CCDS23864.1; -.
DR AlphaFoldDB; Q99P27; -.
DR IntAct; Q99P27; 1.
DR STRING; 10090.ENSMUSP00000009790; -.
DR jPOST; Q99P27; -.
DR MaxQB; Q99P27; -.
DR PaxDb; Q99P27; -.
DR PRIDE; Q99P27; -.
DR ProteomicsDB; 288177; -.
DR MGI; MGI:1917086; Pla2g12b.
DR eggNOG; ENOG502QQU1; Eukaryota.
DR InParanoid; Q99P27; -.
DR PhylomeDB; Q99P27; -.
DR PRO; PR:Q99P27; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99P27; protein.
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:InterPro.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:MGI.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR010711; PLA2G12.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR PANTHER; PTHR12824; PTHR12824; 1.
DR Pfam; PF06951; PLA2G12; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Calcium; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..195
FT /note="Group XIIB secretory phospholipase A2-like protein"
FT /id="PRO_0000022773"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21736 MW; 86F8E653BD08DA24 CRC64;
MKLLCGFFLL WLGLVGNLAQ SDPSPKEEES YSDWGLRQLR GSFESVNSYV DSFMELLGGK
NGVCQYRCRY GKAPMPRPGY KAQEPNGCSS YFLGIKVPGS MDLGIPAMTK CCNQLDVCYD
TCGANKYRCD AKFRWCLHSI CSDLKRTLGF VSNVEAACDS LADTVFNTVW TLGCRPFMNS
QRAACICAEE EKEEL