PLIAB_PROFL
ID PLIAB_PROFL Reviewed; 147 AA.
AC P21756;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Phospholipase A2 inhibitor subunit B;
DE Short=alpha-PLI B;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-103.
RC TISSUE=Blood;
RX PubMed=1985928; DOI=10.1016/s0021-9258(17)35274-2;
RA Inoue S., Kogaki H., Ikeda K., Samejima Y., Omori-Satoh T.;
RT "Amino acid sequences of the two subunits of a phospholipase A2 inhibitor
RT from the blood plasma of Trimeresurus flavoviridis. Sequence homologies
RT with pulmonary surfactant apoprotein and animal lectins.";
RL J. Biol. Chem. 266:1001-1007(1991).
RN [2]
RP SUBUNIT.
RX PubMed=18243268; DOI=10.1016/j.toxicon.2007.12.014;
RA Shimada A., Ohkura N., Hayashi K., Samejima Y., Omori-Satoh T., Inoue S.,
RA Ikeda K.;
RT "Subunit structure and inhibition specificity of alpha-type phospholipase
RT A2 inhibitor from Protobothrops flavoviridis.";
RL Toxicon 51:787-796(2008).
CC -!- FUNCTION: PLI binds directly phospholipase A2 in the presence or
CC absence of calcium. Inhibitory activity of the PLI-B homotrimer is less
CC specific than that of the PLI-A homotrimer.
CC {ECO:0000269|PubMed:1985928}.
CC -!- SUBUNIT: Homo- or heterotrimer; homotrimer of PLI-A chains, two PLI-A
CC and one PLI-B chains, one PLI-A and two PLI-B chains, and homotrimer of
CC PLI-B chains (with a ratio of 1:3:3:1). {ECO:0000269|PubMed:18243268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1985928}.
CC Note=Secreted in plasma. {ECO:0000269|PubMed:1985928}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver.
CC -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC family. {ECO:0000305}.
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DR PIR; B39091; B39091.
DR AlphaFoldDB; P21756; -.
DR SMR; P21756; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW Phospholipase A2 inhibitor; Secreted.
FT CHAIN 1..147
FT /note="Phospholipase A2 inhibitor subunit B"
FT /id="PRO_0000046695"
FT DOMAIN 62..143
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1985928"
FT DISULFID 64..141
FT /evidence="ECO:0000269|PubMed:1985928"
FT DISULFID 119..133
FT /evidence="ECO:0000269|PubMed:1985928"
SQ SEQUENCE 147 AA; 16412 MW; 911F9B0FBBA8A53B CRC64;
HETDSDGQVM NSMIEALTEL QEMIVNLRYA FLTVHKARSF GSGSERLYVS NKEIKTFEPL
KEICEEAGGH IPSPQLENQN KAFANVLERH NKAAYLVVGD SANFTNWAAG QPNEADGTCV
KADTHGFWHS ASCDEKLLVV CEFYFIL
