PLIA_BOTAL
ID PLIA_BOTAL Reviewed; 166 AA.
AC B1A4M7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Phospholipase A2 inhibitor;
DE Short=alpha-PLI;
DE Flags: Precursor;
OS Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=64174;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Estevao-Costa M.I., Costa M.A.F., Mudado M.A., Franco G.R.,
RA Fortes-Dias C.L.;
RT "A profile of the phospholipase A2 inhibitors of the alpha class prospected
RT in Brazilian Crotalidae snakes: structural and phylogenetic analysis.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This phospholipase A2 inhibitor binds directly phospholipase
CC A2 in the presence or absence of calcium. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:A1XRN2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}. Note=Secreted in
CC plasma. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver. {ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC family. {ECO:0000305}.
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DR EMBL; EU421901; ABZ82318.1; -; mRNA.
DR EMBL; EU421902; ABZ82319.1; -; mRNA.
DR EMBL; EU421903; ABZ82320.1; -; mRNA.
DR EMBL; EU421904; ABZ82321.1; -; mRNA.
DR EMBL; EU421905; ABZ82322.1; -; mRNA.
DR AlphaFoldDB; B1A4M7; -.
DR SMR; B1A4M7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Lectin; Phospholipase A2 inhibitor;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..166
FT /note="Phospholipase A2 inhibitor"
FT /id="PRO_5000311718"
FT DOMAIN 46..161
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..160
FT /evidence="ECO:0000250|UniProtKB:P21755"
FT DISULFID 138..152
FT /evidence="ECO:0000250|UniProtKB:P21755"
SQ SEQUENCE 166 AA; 18406 MW; 33AD523A0BA540CF CRC64;
MRLILLSGLL LLGIFLANGH EQDPDGKLLN SLIDALMHLQ REFAKLRGAF LTVYKARSFG
NGSERLYVTN KEIKNFEALR QICEQAGGHI PSPQLENQNK AFANVLERHN KEAYLVVGDS
ANFTNWAAGE PNKAAGACVK ADTHGSWHST SCDDNLLVVC EFYFIL