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LEG4_CHICK
ID   LEG4_CHICK              Reviewed;         135 AA.
AC   P07583;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Beta-galactoside-binding lectin;
DE   AltName: Full=14 kDa lectin;
DE   AltName: Full=C-14;
DE   AltName: Full=Galectin CG-1B;
GN   Name=CG-1B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3004444; DOI=10.1016/0006-291x(86)90525-5;
RA   Ohyama Y., Hirabayashi J., Oda Y., Ohno S., Kawasaki H., Suzuki K.,
RA   Kasai K.;
RT   "Nucleotide sequence of chick 14K beta-galactoside-binding lectin mRNA.";
RL   Biochem. Biophys. Res. Commun. 134:51-56(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3182759; DOI=10.1093/oxfordjournals.jbchem.a122436;
RA   Ohyama Y., Kasai K.;
RT   "Isolation and characterization of the chick 14K beta-galactoside-binding
RT   lectin gene.";
RL   J. Biochem. 104:173-177(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-135, AND ACETYLATION AT SER-2.
RC   TISSUE=Embryo;
RX   PubMed=3597352; DOI=10.1093/jb/101.3.775;
RA   Hirabayashi J., Kawasaki H., Suzuki K., Kasai K.;
RT   "Complete amino acid sequence of 14 kDa beta-galactoside-binding lectin of
RT   chick embryo.";
RL   J. Biochem. 101:775-787(1987).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, MUTAGENESIS OF CYS-8, AND
RP   DISULFIDE BOND.
RC   STRAIN=Bantam;
RX   PubMed=18848566; DOI=10.1016/j.jmb.2008.09.054;
RA   Lopez-Lucendo M.F., Solis D., Saiz J.L., Kaltner H., Russwurm R., Andre S.,
RA   Gabius H.J., Romero A.;
RT   "Homodimeric chicken galectin CG-1B (C-14): Crystal structure and detection
RT   of unique redox-dependent shape changes involving inter- and intrasubunit
RT   disulfide bridges by gel filtration, ultracentrifugation, site-directed
RT   mutagenesis, and peptide mass fingerprinting.";
RL   J. Mol. Biol. 386:366-378(2009).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NEWCASTLE DISEASE VIRUS PROTEIN HN
RP   (MICROBIAL INFECTION).
RX   PubMed=28978647; DOI=10.1074/jbc.m116.772897;
RA   Sun J., Han Z., Qi T., Zhao R., Liu S.;
RT   "Chicken galectin-1B inhibits Newcastle disease virus adsorption and
RT   replication through binding to hemagglutinin-neuraminidase (HN)
RT   glycoprotein.";
RL   J. Biol. Chem. 292:20141-20161(2017).
CC   -!- FUNCTION: This protein binds beta-galactoside. May participate in host
CC       antiviral defense through specific interaction with glycans on the
CC       viral envelope glycoproteins. {ECO:0000269|PubMed:28978647}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:18848566}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with newcastle disease virus
CC       protein HN; this interaction inhibits viral adsorption rather than
CC       internalization. {ECO:0000269|PubMed:28978647}.
CC   -!- TISSUE SPECIFICITY: Mainly in the intestine (adult), mainly in the skin
CC       (embryo).
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DR   EMBL; M11674; AAA48779.1; -; mRNA.
DR   EMBL; D00311; BAA00214.1; -; Genomic_DNA.
DR   PIR; JX0042; LNCH14.
DR   RefSeq; NP_990826.1; NM_205495.1.
DR   PDB; 3DUI; X-ray; 2.10 A; A/B=1-135.
DR   PDBsum; 3DUI; -.
DR   AlphaFoldDB; P07583; -.
DR   SMR; P07583; -.
DR   STRING; 9031.ENSGALP00000020275; -.
DR   BindingDB; P07583; -.
DR   ChEMBL; CHEMBL2189155; -.
DR   UniLectin; P07583; -.
DR   iPTMnet; P07583; -.
DR   PaxDb; P07583; -.
DR   Ensembl; ENSGALT00000020302; ENSGALP00000020275; ENSGALG00000012420.
DR   GeneID; 396491; -.
DR   KEGG; gga:396491; -.
DR   CTD; 396491; -.
DR   VEuPathDB; HostDB:geneid_396491; -.
DR   eggNOG; KOG3587; Eukaryota.
DR   GeneTree; ENSGT00940000155534; -.
DR   HOGENOM; CLU_037794_5_0_1; -.
DR   InParanoid; P07583; -.
DR   OMA; CNSKKME; -.
DR   OrthoDB; 1429018at2759; -.
DR   PhylomeDB; P07583; -.
DR   TreeFam; TF315551; -.
DR   Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR   EvolutionaryTrace; P07583; -.
DR   PRO; PR:P07583; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000012420; Expressed in lung and 13 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0043236; F:laminin binding; IBA:GO_Central.
DR   CDD; cd00070; GLECT; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR044156; Galectin-like.
DR   InterPro; IPR001079; Galectin_CRD.
DR   PANTHER; PTHR11346; PTHR11346; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW   Lectin; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3597352"
FT   CHAIN           2..135
FT                   /note="Beta-galactoside-binding lectin"
FT                   /id="PRO_0000076951"
FT   DOMAIN          5..135
FT                   /note="Galectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         46..50
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..76
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000255"
FT   BINDING         70..73
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:3597352"
FT   DISULFID        3..8
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:18848566"
FT   DISULFID        8
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000269|PubMed:18848566"
FT   MUTAGEN         8
FT                   /note="C->V: No redox-dependent shape changes."
FT                   /evidence="ECO:0000269|PubMed:18848566"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          42..53
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          56..68
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:3DUI"
FT   STRAND          120..135
FT                   /evidence="ECO:0007829|PDB:3DUI"
SQ   SEQUENCE   135 AA;  15063 MW;  5059E30CC51F899A CRC64;
     MSCQGPVCTN LGLKPGQRLT VKGIIAPNAK SFVMNLGKDS THLGLHFNPR FDAHGDVNLI
     VCNSKKMEEW GTEQRETVFP FQKGAPIEIT FSINPSDLTV HLPGHQFSFP NRLGLSVFDY
     FDTHGDFTLR SVSWE
 
 
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