ID   PA2H1_LATCO             Reviewed;         118 AA.
AC   P10117;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Basic phospholipase A2 homolog 1;
DE            Short=svPLA2 homolog;
DE   AltName: Full=Phospholipase A2 homolog I;
DE            Short=PLH-I;
OS   Laticauda colubrina (Yellow-lipped sea krait) (Banded sea krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8628;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=3178739; DOI=10.1042/bj2530869;
RA   Takasaki C., Kimura S., Kokubun Y., Tamiya N.;
RT   "Isolation, properties and amino acid sequences of a phospholipase A2 and
RT   its homologue without activity from the venom of a sea snake, Laticauda
RT   colubrina, from the Solomon Islands.";
RL   Biochem. J. 253:869-875(1988).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3178739}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:3178739}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other phospholipases, it lacks the typical Asp
CC       active site (Asp->Asn in position 75). {ECO:0000305}.
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DR   PIR; S01141; S01141.
DR   AlphaFoldDB; P10117; -.
DR   SMR; P10117; -.
DR   PRIDE; P10117; -.
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:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   CHAIN           1..118
FT                   /note="Basic phospholipase A2 homolog 1"
FT                   /evidence="ECO:0000269|PubMed:3178739"
FT                   /id="PRO_0000161652"
FT   REGION          106..118
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        11..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..117
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        44..98
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        51..91
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        60..84
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        78..89
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   118 AA;  13024 MW;  AB09CEA2B065E2B0 CRC64;
     NLIQFSQLIQ CANKGKRPTL HYMDYGCYCG PGGSGTPVDD LDRCCKTNDD CYGQAEKKGC
     SPLSTNYNFD CFPGGPQCGK GTTCQRFVCD CDLKAALCFA KSPYNNKNFN IDTKKRCK