ID   PLIAL_ELAQU             Reviewed;         167 AA.
AC   Q8AXS4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Phospholipase A2 inhibitor alpha-like protein;
DE            Short=PLI-alpha-LP;
DE            Short=alpha-PLI-like;
DE   Flags: Precursor;
OS   Elaphe quadrivirgata (Japanese four-lined ratsnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe.
OX   NCBI_TaxID=86195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver, and Serum;
RX   PubMed=14658760; DOI=10.1080/15216540310001620995;
RA   Okumura K., Inoue S., Ikeda K., Hayashi K.;
RT   "Identification and characterization of a serum protein homologous to
RT   alpha-type phospholipase A2 inhibitor (PLIalpha) from a nonvenomous snake,
RT   Elaphe quadrivirgata.";
RL   IUBMB Life 55:539-545(2003).
CC   -!- FUNCTION: Does not show any inhibitory activity against various snake
CC       venom PLA2s. Does not inhibit the endogenous PLA2 activities in various
CC       tissue homogenates prepared from this snake.
CC       {ECO:0000269|PubMed:14658760}.
CC   -!- SUBUNIT: Homotrimer (PubMed:14658760); non-covalently linked (By
CC       similarity). {ECO:0000250|UniProtKB:A1XRN2,
CC       ECO:0000269|PubMed:14658760}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14658760}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:14658760}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000269|PubMed:14658760}.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; AB030247; BAC53925.1; -; mRNA.
DR   AlphaFoldDB; Q8AXS4; -.
DR   SMR; Q8AXS4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; 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   1: Evidence at protein level;
KW   Disulfide bond; Lectin; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..167
FT                   /note="Phospholipase A2 inhibitor alpha-like protein"
FT                   /id="PRO_5000049423"
FT   DOMAIN          62..163
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        83..162
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        140..154
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
SQ   SEQUENCE   167 AA;  18152 MW;  E06D4E6BA3C1C55F CRC64;
     MQLILLSSLL LLGLSLANGH ETDPEGQILN SLVETVGRLE KKIDKVENAF LTVHRARSFG
     SGSERLYVTN KQVGNFEAVR NTCVQAGGHI PSPQLLNENK AFASVLERHN KAAYLVVQNS
     AKFTNWAAGE PNNADGNKLC VKADAQGAWH SASCDEDLLV VCEFSFI