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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
 
 
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