LG3BP_RAT
ID LG3BP_RAT Reviewed; 574 AA.
AC O70513; Q66HR4; Q6Q8R9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Galectin-3-binding protein;
DE AltName: Full=Cyp-C-associated protein;
DE Short=CyCAP;
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=Protein 90K;
DE Flags: Precursor;
GN Name=Lgals3bp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Fischer; TISSUE=Fibroblast;
RX PubMed=12650929; DOI=10.1016/s0014-5793(03)00200-x;
RA Shimizu T., Kawakita S., Li Q.-H., Fukuhara S., Fujisawa J.;
RT "Human T-cell leukemia virus type 1 Tax protein stimulates the interferon-
RT responsive enhancer element via NF-kappaB activity.";
RL FEBS Lett. 539:73-77(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Thyroid;
RX PubMed=15231701; DOI=10.1210/en.2004-0506;
RA Grassadonia A., Tinari N., Fiorentino B., Suzuki K., Nakazato M.,
RA De Tursi M., Giuliani C., Napolitano G., Singer D.S., Iacobelli S.,
RA Kohn L.D.;
RT "The 90K protein increases major histocompatibility complex class I
RT expression and is regulated by hormones, gamma-interferon, and double-
RT strand polynucleotides.";
RL Endocrinology 145:4728-4736(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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|UniProtKB:Q08380}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15231701}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q08380}.
CC -!- TISSUE SPECIFICITY: Detected in thyroid (at protein level).
CC {ECO:0000269|PubMed:15231701}.
CC -!- INDUCTION: Up-regulated by virus infection, double-stranded DNA, IFNG
CC and insulin. Down-regulated by hydrocortisone.
CC {ECO:0000269|PubMed:12650929, ECO:0000269|PubMed:15231701}.
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DR EMBL; AF065438; AAC17177.1; -; mRNA.
DR EMBL; AY552591; AAS58489.1; -; mRNA.
DR EMBL; CH473948; EDM06756.1; -; Genomic_DNA.
DR EMBL; BC081724; AAH81724.1; -; mRNA.
DR RefSeq; NP_620796.1; NM_139096.1.
DR AlphaFoldDB; O70513; -.
DR SMR; O70513; -.
DR BioGRID; 251451; 1.
DR IntAct; O70513; 1.
DR STRING; 10116.ENSRNOP00000004320; -.
DR GlyGen; O70513; 8 sites.
DR jPOST; O70513; -.
DR PaxDb; O70513; -.
DR PRIDE; O70513; -.
DR GeneID; 245955; -.
DR KEGG; rno:245955; -.
DR UCSC; RGD:620837; rat.
DR CTD; 3959; -.
DR RGD; 620837; Lgals3bp.
DR VEuPathDB; HostDB:ENSRNOG00000003217; -.
DR eggNOG; ENOG502QU48; Eukaryota.
DR HOGENOM; CLU_032646_0_0_1; -.
DR InParanoid; O70513; -.
DR OMA; FPMMLPQ; -.
DR OrthoDB; 1174057at2759; -.
DR PhylomeDB; O70513; -.
DR TreeFam; TF331368; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:O70513; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000003217; Expressed in ovary and 19 other tissues.
DR Genevisible; O70513; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
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 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..574
FT /note="Galectin-3-binding protein"
FT /id="PRO_0000357037"
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 96
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 125
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 CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
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"
FT CONFLICT 32
FT /note="A -> P (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="V -> L (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="V -> F (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="Q -> P (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..77
FT /note="SRA -> NRV (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> S (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> S (in Ref. 2; AAS58489)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="V -> E (in Ref. 1; AAC17177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63742 MW; 9F0F2F0B828ABD24 CRC64;
MALLWLLSVF LLVPGTQGAK DGDMRLVNGA SASEGRVEIF YRGRWGTVCD NLWNLLDAHV
VCRALGYENA TQALSRAAFG PGKGPIMLDE VECTGNESSL ANCSSLGWMV SHCGHEKDAG
VVCSNDSRGI HILDLSGELP DALGQIFDSQ QDCDLFIQVT GQGHGDLSLC AHTLILRTNP
EAQALWQVVG SSVIMRVDAE CMPVVRDFLR YFYSRRIEVS MSSVKCLHKL ASAYGATELQ
GYCGRLFVTL LPQDPTFHTP LELYEYAQAT GDSVLEDLCV QFLAWNFEPL TQAEAWLSVP
NALIQALLPK SELAVSSELD LLKAVDQWST ATGASHGDVE RLVEQIRFPM MLPQELFELQ
FNLSLYQGHQ ALFQRKTMEA LEFHTVPLKV LAKYRSLNLT EDVYKPRLYT SSTWSSLLMA
GAWSTQSYKY RQFYTYNYGS QSRYSSYQNF QTPQHPSFLF KDKLISWSAT YLPTIQSCWN
YGFSCTSDEL PVLGLTTSSY SDPTIGYENK ALILCGGYSV VDVTTFIGSK APIPGTQETN
SSKTPSLFPC ASGAFSSFRV VIRPFYLTNS TDTE
