ID   PLIAL_ELACL             Reviewed;         167 AA.
AC   C0STK6;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Phospholipase A2 inhibitor alpha-like protein {ECO:0000303|PubMed:19673083};
DE            Short=PLI-alpha-LP {ECO:0000303|PubMed:19673083};
DE   Flags: Precursor;
OS   Elaphe climacophora (Japanese rat snake) (Coluber climacophorus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe.
OX   NCBI_TaxID=31143;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-39, FUNCTION,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RC   TISSUE=Liver, and Serum;
RX   PubMed=19673083; DOI=10.1016/j.toxicon.2009.02.001;
RA   Shirai R., Toriba M., Hayashi K., Ikeda K., Inoue S.;
RT   "Identification and characterization of phospholipase A2 inhibitors from
RT   the serum of the Japanese rat snake, Elaphe climacophora.";
RL   Toxicon 53:685-692(2009).
CC   -!- FUNCTION: Has no PLA2 inhibitory activity.
CC       {ECO:0000269|PubMed:19673083}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19673083}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19673083}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:19673083}.
CC   -!- MISCELLANEOUS: Concentration of this protein in the serum is 8-fold
CC       lower than in the E.quadrivirgata (another non-venomous snake) serum.
CC       This difference may reflect the difference in the food habits of these
CC       snakes. E.quadrivirgata preys upon snakes including the venomous
CC       snakes, whereas E.climacophora only preys upon small mammals and birds.
CC       {ECO:0000269|PubMed:19673083}.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; AB462510; BAH47548.1; -; mRNA.
DR   AlphaFoldDB; C0STK6; -.
DR   SMR; C0STK6; -.
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   Direct protein sequencing; Disulfide bond; Lectin; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:19673083"
FT   CHAIN           20..167
FT                   /note="Phospholipase A2 inhibitor alpha-like protein"
FT                   /evidence="ECO:0000305|PubMed:19673083"
FT                   /id="PRO_5002903376"
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;  18201 MW;  6B598855DE01D9B1 CRC64;
     MQLILLSSLL LLGLSLANGH ETDPEGQILN SLVETVSRLE KKIDKVENAF LTVHRARSFG
     SGSERLYVTN KQVGNFEAVR NTCVQAGGRI PSPQLLNENK AFASVLERHN KAAYLVVQNS
     AKFTNWAAGE PNNADGNKLC VKADAQGAWH SASCDEDLLV VCEFSFI