ID H3BF68_LATCH Unreviewed; 817 AA.
AC H3BF68;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
GN Name=LOC102351206 {ECO:0000313|Ensembl:ENSLACP00000020539.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020539.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000020539.1}
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|RuleBase:RU362102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC calcium binding. {ECO:0000256|RuleBase:RU362102}.
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DR EMBL; AFYH01029298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01029304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BF68; -.
DR STRING; 7897.ENSLACP00000020539; -.
DR Ensembl; ENSLACT00000020679.1; ENSLACP00000020539.1; ENSLACG00000018051.1.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; H3BF68; -.
DR OMA; FMRGFFL; -.
DR TreeFam; TF325228; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR040723; cPLA2_C2.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF32; CYTOSOLIC PHOSPHOLIPASE A2 BETA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF18695; cPLA2_C2; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|RuleBase:RU362102};
KW Cytoplasm {ECO:0000256|RuleBase:RU362102};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362102};
KW Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362102};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362102};
KW Metal-binding {ECO:0000256|RuleBase:RU362102};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 1..103
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 269..817
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 817 AA; 93109 MW; D21FF983B48B6779 CRC64;
YYNLSVRIIR GRNISGKDLL SKPDCYISLS LPTATAKGDK TKVINNSCNP VWNEAFHYRI
QSQIKNVLDL SMYDNDVLHD DLFSQISIDV NQIKAGEKFQ HTFHVGKKKD EVLEVELVME
KSPDPPTEVI TNGVLVACPI LCTEVTVNRE KASPNQKVAS DESLVLKVNG AFEEEQKNTY
KAGLGLLGGR ESFIFHRTKD IDTQLEVERM CLTTNPHETG LFTQVSQNTA KLKTAIIYKV
SSLTALNDQE RKVPLGKGRN VDIEVQNKVC SKDLDVRLNF DLSEDEKNFL EKRLAQVACA
MTKSLGLNGS LDHEEVPVVA VVGSGGGTRA MTSLYGSLLG LQKLDLLDCI TYINGVSGST
WCMSTLYEDA DWSHKQLQDP VFSAQNCVSR KKAGAFSPEH LYYYYNEKTS KKLQRQKMTI
ADLWGLIIEY MLYGKKNPEK LSNQKEAVLH GQNPYPIYTA VNIRDHMDGQ NFAEWCEFTP
HEIGFPKYGA FIRTENFNSE FFMGRMIRKC PEPRICYLLG LWSSIFSMNL IEAWTVTTKS
SNKWLNWLKK AKENSDDDHL PYIMDNTESK YQLISPPGVT SYFKDFFTDR PAIGEYYNFL
HGLQIHRTYK KWNAFVRSKA DHPDNYPNQL TPSERKLHLV DSGFACNNGI PLVVRPVRNV
DVILSYNYTW GSQFKALKLA EKHCVECQIP FPKIDVSEIN EANLKECYMF MDKDDPRVPI
VLHFPLVNDT FRHFKAPVWG GRVGIQRCSA EENAEGKVDV RSRNSPYRTR NITYTPQDFD
QLVSLQCYNV TNNRDSILEA FRLAVDRRRL RLASSGA
//
