ID   LG3BP_MESAU             Reviewed;         578 AA.
AC   P70117;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Galectin-3-binding protein;
DE   AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE   AltName: Full=Mac-2-binding protein;
DE            Short=MAC2BP;
DE            Short=Mac-2 BP;
DE   AltName: Full=Pancreas cancer-associated protein 4;
DE   Flags: Precursor;
GN   Name=LGALS3BP; Synonyms=M2BP;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schaffert C., Pour P.M., MacDonald R.G., Chaney W.G.;
RT   "Identification of blood group A-modified glycoproteins in hamster
RT   pancreatic cancer and cloning of hamster Mac-2-BP.";
RL   Submitted (OCT-1996) 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). The
CC       unglycosylated form interacts with PDE4DIP; this interaction, which is
CC       PDE4DIP isoform-specific, may connect a pericentrosomal complex to the
CC       gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly
CC       and acetylation (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q08380}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q08380}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:Q08380}.
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DR   EMBL; U73375; AAB18745.1; -; mRNA.
DR   RefSeq; NP_001268610.1; NM_001281681.1.
DR   AlphaFoldDB; P70117; -.
DR   SMR; P70117; -.
DR   STRING; 10036.XP_005069906.1; -.
DR   GeneID; 101825995; -.
DR   CTD; 3959; -.
DR   eggNOG; ENOG502QU48; Eukaryota.
DR   OrthoDB; 1174057at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; SM00225; BTB; 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   2: Evidence at transcript 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..578
FT                   /note="Galectin-3-binding protein"
FT                   /id="PRO_0000357034"
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                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   578 AA;  64399 MW;  45BF22796BE79EE6 CRC64;
     MAFLWLFSLW LLVPGTQGTK DGDMRLVNGA SANEGRVEIF YRGQWGTVCD NLWNILDANV
     VCRALGYENA TQALGRAAFG PGRGPVMLDE VECTGTEPSL ANCSSLGWLK SRCGHEKDAG
     VVCSNETGGV HILDLSGDLP NALGQIFDSQ QGCDLFIQVT GQGHGDLTIC AHKLILNTNP
     EAQALWQVVG SSVIMRVDAE CMPVVRDFLR YFYSRRIEVT MSSVKCLHKL ASAYGATQLQ
     DYCGRLFATL LPQDPTFRTP LELYAYAQAT RDSVLEDLCV QFLAWNFEPL TQAEAWLSVP
     TALLQALLSK SDLAVSSELD LLKAVDQWSM ESSASHAEVE RLLEQVRFPM VLPQELFELQ
     FNLSLYEGHR ELFQRKTMEA LEFHTVPFRV LAKYRGLNLT EDTYQPRLYT SSTWSTLVTE
     SSSRSRAAVQ VYGYAQYYPY GYDSRRWYYP YQSFQTPQHP SFLFVDKLIS WSATYLPTVQ
     SCWNYGFSCT PEELPVLGLT KSSYSEPAIG YENKALMLCG GYSVVDVANF AGSKAPIPSA
     LDTNSSKISS LFPCSSGAFS GFRVVIRPFY LTNSTDLD