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REG1B_HUMAN
ID   REG1B_HUMAN             Reviewed;         166 AA.
AC   P48304;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Lithostathine-1-beta;
DE   AltName: Full=Pancreatic stone protein 2;
DE            Short=PSP-2;
DE   AltName: Full=Regenerating islet-derived protein 1-beta;
DE            Short=REG-1-beta;
DE   AltName: Full=Regenerating protein I beta;
DE   Flags: Precursor;
GN   Name=REG1B; Synonyms=PSPS2, REGL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8348956; DOI=10.1016/0014-5793(93)81006-l;
RA   Bartoli C., Gharib B., Giorgi D., Sansonetti A., Dagorn J.-C.,
RA   Berge-Lefranc U.;
RT   "A gene homologous to the reg gene is expressed in the human pancreas.";
RL   FEBS Lett. 327:289-293(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=8110835; DOI=10.1016/0167-4781(94)90035-3;
RA   Moriizumi S., Watanabe T., Unno M., Nakagawara K., Suzuki Y., Miyashita H.,
RA   Yonekura H., Okamoto H.;
RT   "Isolation, structural determination and expression of a novel reg gene,
RT   human regI beta.";
RL   Biochim. Biophys. Acta 1217:199-202(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION AT THR-27.
RX   PubMed=7607222; DOI=10.1111/j.1432-1033.1995.tb20589.x;
RA   De Reggi M., Capon C., Gharib B., Wieruszeski J.-M., Michel R., Fournet B.;
RT   "The glycan moiety of human pancreatic lithostathine. Structure
RT   characterization and possible pathophysiological implications.";
RL   Eur. J. Biochem. 230:503-510(1995).
CC   -!- FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate
CC       precipitation. May be associated with neuronal sprouting in brain, and
CC       with brain and pancreas regeneration.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: All O-linked glycans consist of Gal-GlcNAc-Gal-GalNAc
CC       tetrasaccharide core and get elongated (microheterogeneity).
CC       {ECO:0000269|PubMed:7607222}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Lithostathine A;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_255";
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DR   EMBL; L08010; AAA18204.1; -; Genomic_DNA.
DR   EMBL; D17291; BAA04124.1; -; Genomic_DNA.
DR   EMBL; D16816; BAA04091.1; -; mRNA.
DR   EMBL; BC027895; AAH27895.1; -; mRNA.
DR   CCDS; CCDS1963.1; -.
DR   PIR; S34591; RGHU1B.
DR   RefSeq; NP_006498.1; NM_006507.3.
DR   AlphaFoldDB; P48304; -.
DR   SMR; P48304; -.
DR   BioGRID; 111900; 6.
DR   IntAct; P48304; 3.
DR   MINT; P48304; -.
DR   STRING; 9606.ENSP00000303206; -.
DR   MEROPS; I63.002; -.
DR   GlyGen; P48304; 1 site.
DR   iPTMnet; P48304; -.
DR   PhosphoSitePlus; P48304; -.
DR   BioMuta; REG1B; -.
DR   DMDM; 1346460; -.
DR   jPOST; P48304; -.
DR   MassIVE; P48304; -.
DR   PaxDb; P48304; -.
DR   PeptideAtlas; P48304; -.
DR   PRIDE; P48304; -.
DR   ProteomicsDB; 55874; -.
DR   Antibodypedia; 47486; 182 antibodies from 22 providers.
DR   DNASU; 5968; -.
DR   Ensembl; ENST00000305089.8; ENSP00000303206.3; ENSG00000172023.8.
DR   GeneID; 5968; -.
DR   KEGG; hsa:5968; -.
DR   MANE-Select; ENST00000305089.8; ENSP00000303206.3; NM_006507.4; NP_006498.1.
DR   CTD; 5968; -.
DR   DisGeNET; 5968; -.
DR   GeneCards; REG1B; -.
DR   HGNC; HGNC:9952; REG1B.
DR   HPA; ENSG00000172023; Tissue enriched (pancreas).
DR   MIM; 167771; gene.
DR   neXtProt; NX_P48304; -.
DR   OpenTargets; ENSG00000172023; -.
DR   PharmGKB; PA34319; -.
DR   VEuPathDB; HostDB:ENSG00000172023; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000163728; -.
DR   HOGENOM; CLU_049894_18_0_1; -.
DR   InParanoid; P48304; -.
DR   OMA; QTNSFFM; -.
DR   OrthoDB; 1509611at2759; -.
DR   PhylomeDB; P48304; -.
DR   PathwayCommons; P48304; -.
DR   SignaLink; P48304; -.
DR   BioGRID-ORCS; 5968; 8 hits in 1022 CRISPR screens.
DR   ChiTaRS; REG1B; human.
DR   GeneWiki; REG1B; -.
DR   GenomeRNAi; 5968; -.
DR   Pharos; P48304; Tbio.
DR   PRO; PR:P48304; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P48304; protein.
DR   Bgee; ENSG00000172023; Expressed in body of pancreas and 87 other tissues.
DR   ExpressionAtlas; P48304; baseline and differential.
DR   Genevisible; P48304; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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   Disulfide bond; Glycoprotein; Lectin; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..166
FT                   /note="Lithostathine-1-beta"
FT                   /id="PRO_0000017425"
FT   DOMAIN          34..164
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        27
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7607222"
FT   DISULFID        36..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        64..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        137..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VARIANT         109
FT                   /note="R -> H (in dbSNP:rs7586984)"
FT                   /id="VAR_050121"
SQ   SEQUENCE   166 AA;  18665 MW;  D1DC20E11AE5DDE8 CRC64;
     MAQTNSFFML ISSLMFLSLS QGQESQTELP NPRISCPEGT NAYRSYCYYF NEDPETWVDA
     DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SSTDDSNVWI GLHDPKKNRR WHWSSGSLVS
     YKSWDTGSPS SANAGYCASL TSCSGFKKWK DESCEKKFSF VCKFKN
 
 
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