ID   LG3BP_PONAB             Reviewed;         584 AA.
AC   Q5RDA4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Galectin-3-binding protein;
DE   AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE   Flags: Precursor;
GN   Name=LGALS3BP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. Interacts with the gamma-
CC       tubulin ring complex (gamma-TuRC), composed of gamma-tubulin, TUBGCP2,
CC       TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. The unglycosylated form
CC       interacts with PDE4DIP; this interaction, which is PDE4DIP isoform-
CC       specific, may connect a pericentrosomal complex, made of AKAP9,
CC       CDK5RAP2, EB1/MAPRE1 and PDE4DIP, to the gamma-tubulin ring complex
CC       (gamma-TuRC) to promote microtubule assembly and acetylation.
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; CR858011; CAH90253.1; -; mRNA.
DR   AlphaFoldDB; Q5RDA4; -.
DR   SMR; Q5RDA4; -.
DR   PRIDE; Q5RDA4; -.
DR   InParanoid; Q5RDA4; -.
DR   Proteomes; UP000001595; 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; SM00202; SR; 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..584
FT                   /note="Galectin-3-binding protein"
FT                   /id="PRO_0000357036"
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..359
FT                   /note="BACK"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        579
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"
SQ   SEQUENCE   584 AA;  65267 MW;  A2BB542325D5982D CRC64;
     MTPPRLFWVW LLVAGTQGVN DGDMRLADGG ATNQGRVEIF YRGQWGTVCD NLWDLTDASV
     VCRALGFENA TQALGRAAFG QGSGPIMLDE VQCTGTEASL ADCKSLGWLK SNCRHERDAG
     VVCTNETRST HTLDLSRELS EALGQIFDSQ RGCDLSISVN VQGEDALGFC GHTVILTANL
     EAQALWKEPG SNVTMSVDAE CVPMVRDLLR YFYSRRIDIT LSSVKCFHKL ASAYGARQLQ
     GYCATLFAIL LPQDPSFHMP LDLYAYAVAT GDALLEKLCL QFLAWNFEAL TQAEAWPSVP
     TDLLQLLLPR SDLAVPSELA LLKAVDTWWG ERASHEEVEG LVEKIRFPMM LPEELFELQF
     NLSLYWSHEA LFQKKTLQAL EFHTVPFQLL ARYKGLNLTE DTYKPRIYTS PTWSAFVTDS
     SWSARKSQLV YQSRRGPLVK YSSDYFQAPS DYRYYPYQSF QTPQHPSFLF QDKRVSWSLV
     YLPTIQSCWN YGFSCSSDEL PVLGLTKSGG SDRTIAYENK ALMLCEGLFV ADVTDFEGWK
     AAIPSALDTN SSKSTSSFPC PAGHFNGFRT VIRPFYLTNS SGVD