LITH_BOVIN
ID LITH_BOVIN Reviewed; 175 AA.
AC P23132;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Lithostathine;
DE AltName: Full=Islet cells regeneration factor;
DE Short=ICRF;
DE AltName: Full=Islet of Langerhans regenerating protein;
DE Short=REG;
DE AltName: Full=Pancreatic stone protein;
DE Short=PSP;
DE AltName: Full=Pancreatic thread protein;
DE Short=PTP;
DE Contains:
DE RecName: Full=Lithostathine A chain;
DE Contains:
DE RecName: Full=Lithostathine B chain;
DE Flags: Precursor;
GN Name=PTP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2394826; DOI=10.1172/jci114762;
RA de la Monte S.M., Ozturk M., Wands J.R.;
RT "Enhanced expression of an exocrine pancreatic protein in Alzheimer's
RT disease and the developing human brain.";
RL J. Clin. Invest. 86:1004-1013(1990).
RN [2]
RP PROTEIN SEQUENCE OF 38-138 AND 141-175.
RX PubMed=2085387; DOI=10.1007/bf01025016;
RA Cai L., Harris W.R., Marshak D.R., Gross J., Crabb J.W.;
RT "Structural analysis of bovine pancreatic thread protein.";
RL J. Protein Chem. 9:623-632(1990).
RN [3]
RP PROTEIN SEQUENCE OF 38-85 AND 141-175.
RX PubMed=3862086; DOI=10.1073/pnas.82.17.5627;
RA Gross J., Brauer A.W., Bringhurst R.F., Corbett C., Margolies M.N.;
RT "An unusual bovine pancreatic protein exhibiting pH-dependent globule-
RT fibril transformation and unique amino acid sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5627-5631(1985).
CC -!- FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate
CC precipitation.
CC -!- SUBUNIT: Cleaved to give an A chain and a B chain joined by a disulfide
CC bond.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In pancreatic acinar cells.
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DR EMBL; M59794; AAA30750.1; -; mRNA.
DR PIR; A37194; A37194.
DR RefSeq; NP_991356.1; NM_205787.1.
DR RefSeq; XP_005212802.1; XM_005212745.2.
DR AlphaFoldDB; P23132; -.
DR SMR; P23132; -.
DR STRING; 9913.ENSBTAP00000015040; -.
DR PaxDb; P23132; -.
DR Ensembl; ENSBTAT00000015040; ENSBTAP00000015040; ENSBTAG00000011314.
DR Ensembl; ENSBTAT00000086119; ENSBTAP00000073451; ENSBTAG00000011314.
DR GeneID; 404114; -.
DR KEGG; bta:404114; -.
DR CTD; 5068; -.
DR VEuPathDB; HostDB:ENSBTAG00000011314; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154447; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; P23132; -.
DR OMA; WEWSNAD; -.
DR OrthoDB; 1509611at2759; -.
DR Reactome; R-BTA-6803157; Antimicrobial peptides.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000011314; Expressed in urinary bladder and 21 other tissues.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..37
FT /evidence="ECO:0000255"
FT /id="PRO_0000017417"
FT CHAIN 38..175
FT /note="Lithostathine"
FT /id="PRO_0000017418"
FT CHAIN 38..138
FT /note="Lithostathine A chain"
FT /id="PRO_0000017419"
FT CHAIN 141..175
FT /note="Lithostathine B chain"
FT /id="PRO_0000017420"
FT DOMAIN 38..173
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 68..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 146..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 84..85
FT /note="EE -> FF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19334 MW; C270EE70B7E91D6A CRC64;
MLPSLGLPRL SWMLLSCLML LSQIQGENSQ KELPSARISC PSGSMAYRSH CYALFKTPKT
WMDADIACQK RPSGHLVSVL SGAEESFVAS LVRNNLNTQS DIWIGLHDPT EGSEANAGGW
EWISNDVLNY VAWETDPAAI SSPGYCGSLS RSSGYLKWRD HNCNLNLPYV CKFTD
