ID   PLIA_ATRNM              Reviewed;         166 AA.
AC   A1XRN2; A1XRN3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Phospholipase A2 inhibitor anMIP;
DE            Short=alpha-PLI;
DE   AltName: Full=Myotoxic phospholipase A2 inhibitory protein;
DE            Short=MIP;
DE   Flags: Precursor;
OS   Atropoides nummifer (Jumping pit viper) (Porthidium nummifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Atropoides.
OX   NCBI_TaxID=44730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-29, SUBCELLULAR
RP   LOCATION, SUBUNIT, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Liver, and Plasma;
RX   PubMed=17071122; DOI=10.1016/j.cbpb.2006.09.003;
RA   Quiros S., Alape-Giron A., Angulo Y., Lomonte B.;
RT   "Isolation, characterization and molecular cloning of AnMIP, a new alpha-
RT   type phospholipase A2 myotoxin inhibitor from the plasma of the snake
RT   Atropoides nummifer (Viperidae: Crotalinae).";
RL   Comp. Biochem. Physiol. 146B:60-68(2007).
CC   -!- FUNCTION: This phospholipase A2 inhibitor neutralizes the activity of
CC       basic PLA2 myotoxins of its own and related venoms. The inhibitory
CC       profile shows specificity towards group II PLA2, either belonging to
CC       the catalytically-active (D49) or -inactive (K49) subtypes.
CC   -!- SUBUNIT: Homotrimer; non-covalently linked.
CC       {ECO:0000269|PubMed:17071122}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17071122}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:17071122}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17071122}.
CC   -!- MASS SPECTROMETRY: Mass=22247; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17071122};
CC   -!- MASS SPECTROMETRY: Mass=22301; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17071122};
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; DQ657241; ABG37909.1; -; mRNA.
DR   EMBL; DQ657242; ABG37910.1; -; mRNA.
DR   AlphaFoldDB; A1XRN2; -.
DR   SMR; A1XRN2; -.
DR   iPTMnet; A1XRN2; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW   Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:17071122"
FT   CHAIN           20..166
FT                   /note="Phospholipase A2 inhibitor anMIP"
FT                   /id="PRO_0000355228"
FT   DOMAIN          46..161
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:17071122"
FT   DISULFID        83..160
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        138..152
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   VARIANT         48..50
FT                   /note="HAL -> YAF"
FT   VARIANT         61
FT                   /note="R -> G"
FT   VARIANT         128
FT                   /note="A -> V"
SQ   SEQUENCE   166 AA;  18376 MW;  20E55E75DA6A82E6 CRC64;
     MRLILLSGLL LLGTFLANGD EKDSDVQMLN SMIEAVMILQ RDFANLRHAL MTVHNARSFG
     RGSERLYVTN KEVSKFEGLE EICSQAGGHI PSPQLENQNK AFEDVLERHN KAAYLVVGDS
     ANFTNWAAGQ PNEADGTCVK ADTHGSWHSA SCDDNLLVVC EFYFIL