LITH_PIG
ID LITH_PIG Reviewed; 122 AA.
AC Q29191;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Lithostathine;
DE Contains:
DE RecName: Full=Lithostathine A chain;
DE Flags: Precursor; Fragment;
GN Name=PTP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
CC -!- FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate
CC precipitation. {ECO:0000250}.
CC -!- SUBUNIT: Cleaved to give an A chain and a B chain joined by a disulfide
CC bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In pancreatic acinar cells.
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DR EMBL; F14502; CAA23093.1; -; mRNA.
DR STRING; 9823.ENSSSCP00000030478; -.
DR PaxDb; Q29191; -.
DR PeptideAtlas; Q29191; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q29191; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR GO; GO:0042834; F:peptidoglycan binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0044278; P:cell wall disruption in another organism; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
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; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..37
FT /evidence="ECO:0000255"
FT /id="PRO_0000017421"
FT CHAIN 38..>122
FT /note="Lithostathine"
FT /id="PRO_0000017422"
FT CHAIN 38..>122
FT /note="Lithostathine A chain"
FT /id="PRO_0000017423"
FT DOMAIN 38..>122
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT NON_TER 122
SQ SEQUENCE 122 AA; 13149 MW; FD58FDBE1C5C1FFC CRC64;
MLPSMSLPSL XWMLLSCLML LSQVQGEDSP ADTPSARISC PKGSMAYASY CYALFITPKT
WMGADMACQK RPSGHLVSVL SGAEASFVSS LIKNNLNALS DVWIGLHDPT EGLEPNAGGW
EW