LG3BP_BOVIN
ID LG3BP_BOVIN Reviewed; 555 AA.
AC A7E3W2; Q2KJF4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Galectin-3-binding protein;
DE AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE Flags: Precursor;
GN Name=LGALS3BP;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host
CC defense against viruses and tumor cells (By similarity).
CC {ECO:0000250|UniProtKB:Q08380}.
CC -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-like
CC structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds
CC ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By similarity). Interacts
CC with the gamma-tubulin ring complex (gamma-TuRC), composed of gamma-
CC tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. The
CC unglycosylated form interacts with PDE4DIP; this interaction, which is
CC PDE4DIP isoform-specific, may connect a pericentrosomal complex, made
CC of AKAP9, CDK5RAP2, EB1/MAPRE1 and PDE4DIP, to the gamma-tubulin ring
CC complex (gamma-TuRC) to promote microtubule assembly and acetylation
CC (By similarity). {ECO:0000250|UniProtKB:Q08380}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q08380}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT030733; ABS45049.1; -; mRNA.
DR EMBL; BC105367; AAI05368.1; -; mRNA.
DR RefSeq; NP_001039781.1; NM_001046316.2.
DR RefSeq; XP_005221293.1; XM_005221236.1.
DR AlphaFoldDB; A7E3W2; -.
DR SMR; A7E3W2; -.
DR STRING; 9913.ENSBTAP00000001802; -.
DR PaxDb; A7E3W2; -.
DR PRIDE; A7E3W2; -.
DR Ensembl; ENSBTAT00000001802; ENSBTAP00000001802; ENSBTAG00000001368.
DR GeneID; 531137; -.
DR KEGG; bta:531137; -.
DR CTD; 3959; -.
DR VEuPathDB; HostDB:ENSBTAG00000001368; -.
DR VGNC; VGNC:30853; LGALS3BP.
DR eggNOG; ENOG502QU48; Eukaryota.
DR GeneTree; ENSGT00940000162516; -.
DR HOGENOM; CLU_032646_0_0_1; -.
DR InParanoid; A7E3W2; -.
DR OMA; FPMMLPQ; -.
DR OrthoDB; 1174057at2759; -.
DR TreeFam; TF331368; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000001368; Expressed in granulosa cell and 102 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..555
FT /note="Galectin-3-binding protein"
FT /id="PRO_0000357033"
FT DOMAIN 24..124
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 153..221
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 260..360
FT /note="BACK"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 49..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 62..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 93..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 230
FT /note="L -> F (in Ref. 2; AAI05368)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="P -> T (in Ref. 2; AAI05368)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> H (in Ref. 2; AAI05368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 62127 MW; 062B125EAF13018D CRC64;
MAPLRLFWIW LLVVGTRGVK DGDMRLADGG SANQGRVEIY YNGQWGTVCE NMWDLTDASV
VCRALGFQNA TEALGGAAFG PGYGPIMLDE VRCTGTEPSL ANCSSLGWMR SNCRHDKDAS
VICTNETRGV YTLDLSGELP AALEQIFESQ KGCDLFITVK VREEDEIAMC AHKLILSTNP
EAHGLWKEPG SRVTMEVDAE CVPVVKDFIR YLYSRRIDVS LSSVKCLHKL ASAYQAKQLQ
SYCGHLFAIL IPQDPSFWTP LELYAYALAT RDPVLEEICV QFLAWNFGAL TQAEAWPSVP
PALLQGLLSR TELVVPSELV LLLAVDKWSQ ERRTSHKEVE ALVGQVRFPM MPPQDLFSLQ
FNLSLYWSHE ALFQKKILQA LEFHTVPFEL LAQYWGLNLT EGTYQPRLYT SPTWSQSVMS
SSYNPSRSFQ TPQHPSFLFH DSSVSWSFVY LPTLQSCWNY GFSCSSDDPP LLALSKSSYS
KSNPTIGYEN RALLHCEGSF VVDVIDFKGW KALVPSALAT NSSRSTSLFP CPSGVFSRFQ
VVIRPFYLTN STDMD
