SDCB1_RAT
ID SDCB1_RAT Reviewed; 300 AA.
AC Q9JI92;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Syntenin-1;
DE AltName: Full=Syndecan-binding protein 1;
GN Name=Sdcbp;
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 INTERACTION WITH SDCBP2 AND NFASC.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11152476; DOI=10.1074/jbc.m010647200;
RA Koroll M., Rathjen F.G., Volkmer H.;
RT "The neural cell recognition molecule neurofascin interacts with syntenin-1
RT but not with syntenin-2, both of which reveal self-associating activity.";
RL J. Biol. Chem. 276:10646-10654(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11179419; DOI=10.1091/mbc.12.2.339;
RA Zimmermann P., Tomatis D., Rosas M., Grootjans J.J., Leenaerts I.,
RA Degeest G., Reekmans G., Coomans C., David G.;
RT "Characterization of syntenin, a syndecan-binding PDZ protein, as a
RT component of cell adhesion sites and microfilaments.";
RL Mol. Biol. Cell 12:339-350(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
RN [4]
RP INTERACTION WITH PTPRJ.
RX PubMed=11434923; DOI=10.1016/s0014-5793(01)02580-7;
RA Iuliano R., Trapasso F., Sama I., Le Pera I., Martelli M.L., Lembo F.,
RA Santoro M., Viglietto G., Chiariotti L., Fusco A.;
RT "Rat protein tyrosine phosphatase eta physically interacts with the PDZ
RT domains of syntenin.";
RL FEBS Lett. 500:41-44(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Multifunctional adapter protein involved in diverse array of
CC functions including trafficking of transmembrane proteins, neuro and
CC immunomodulation, exosome biogenesis, and tumorigenesis. Positively
CC regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced
CC epithelial-to-mesenchymal transition (EMT) and cell migration in
CC various cell types. May increase TGFB1 signaling by enhancing cell-
CC surface expression of TGFR1 by preventing the interaction between TGFR1
CC and CAV1 and subsequent CAV1-dependent internalization and degradation
CC of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome
CC biogenesis. Regulates migration, growth, proliferation, and cell cycle
CC progression in a variety of cancer types. In adherens junctions may
CC function to couple syndecans to cytoskeletal proteins or signaling
CC components. Seems to couple transcription factor SOX4 to the IL-5
CC receptor (IL5RA). May also play a role in vesicular trafficking. Seems
CC to be required for the targeting of TGFA to the cell surface in the
CC early secretory pathway. {ECO:0000250|UniProtKB:O00560}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:11152476). Interacts with NFASC
CC and SDCBP2 (PubMed:11152476). Interacts with PTPRJ (PubMed:11434923).
CC Interacts with SDC1, SDC2, SDC3, SDC4, NRXN2, EPHA7, EPHB1, NF2 isoform
CC 1, TGFA and IL5RA (By similarity). Interacts with PDCD6IP. Forms a
CC complex with PDCD6IP and SDC2. Interacts (via C-terminus) with TGFBR1
CC (By similarity). Binds to FZD7; this interaction is increased by
CC inositol trisphosphate (IP3) (By similarity). Interacts with SMO (By
CC similarity). {ECO:0000250|UniProtKB:O00560,
CC ECO:0000250|UniProtKB:O08992, ECO:0000269|PubMed:11152476,
CC ECO:0000269|PubMed:11434923}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O00560}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O00560}. Cell membrane
CC {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00560}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00560}. Nucleus {ECO:0000250|UniProtKB:O00560}.
CC Melanosome {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O00560}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:O00560}. Membrane raft
CC {ECO:0000250|UniProtKB:O00560}. Note=Mainly membrane-associated.
CC Localized to adherens junctions, focal adhesions and endoplasmic
CC reticulum. Colocalized with actin stress fibers. Also found in the
CC nucleus. Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV. Associated to the plasma membrane in the presence
CC of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) (By
CC similarity). {ECO:0000250|UniProtKB:O00560}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
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; AF248548; AAF86960.1; -; mRNA.
DR EMBL; AJ292243; CAC21602.1; -; mRNA.
DR EMBL; BC064651; AAH64651.1; -; mRNA.
DR RefSeq; NP_114192.1; NM_031986.1.
DR PDB; 5A2P; X-ray; 2.50 A; A/B/C/D=112-274.
DR PDB; 5G1D; X-ray; 2.81 A; A/B=108-300.
DR PDB; 5G1E; X-ray; 1.92 A; A/B=108-300.
DR PDB; 6AK2; X-ray; 1.87 A; A/B=113-193.
DR PDBsum; 5A2P; -.
DR PDBsum; 5G1D; -.
DR PDBsum; 5G1E; -.
DR PDBsum; 6AK2; -.
DR AlphaFoldDB; Q9JI92; -.
DR SMR; Q9JI92; -.
DR BioGRID; 249867; 8.
DR IntAct; Q9JI92; 10.
DR MINT; Q9JI92; -.
DR STRING; 10116.ENSRNOP00000013563; -.
DR iPTMnet; Q9JI92; -.
DR PhosphoSitePlus; Q9JI92; -.
DR jPOST; Q9JI92; -.
DR PaxDb; Q9JI92; -.
DR PRIDE; Q9JI92; -.
DR Ensembl; ENSRNOT00000115856; ENSRNOP00000081603; ENSRNOG00000009683.
DR GeneID; 83841; -.
DR KEGG; rno:83841; -.
DR UCSC; RGD:621497; rat.
DR CTD; 6386; -.
DR RGD; 621497; Sdcbp.
DR eggNOG; KOG0849; Eukaryota.
DR GeneTree; ENSGT00940000154502; -.
DR HOGENOM; CLU_059870_0_0_1; -.
DR InParanoid; Q9JI92; -.
DR OMA; EIKQRIC; -.
DR OrthoDB; 1035679at2759; -.
DR PhylomeDB; Q9JI92; -.
DR TreeFam; TF327131; -.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-447043; Neurofascin interactions.
DR Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9JI92; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009683; Expressed in lung and 20 other tissues.
DR Genevisible; Q9JI92; RN.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005895; C:interleukin-5 receptor complex; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:RGD.
DR GO; GO:0005109; F:frizzled binding; ISO:RGD.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005137; F:interleukin-5 receptor binding; ISS:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0045545; F:syndecan binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:RGD.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:RGD.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030528; SDCBP.
DR PANTHER; PTHR12345:SF10; PTHR12345:SF10; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Endoplasmic reticulum; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT CHAIN 2..300
FT /note="Syntenin-1"
FT /id="PRO_0000184003"
FT DOMAIN 116..195
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 200..274
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 2..104
FT /note="Interaction with PDCD6IP"
FT /evidence="ECO:0000250|UniProtKB:O08992"
FT MOTIF 3..7
FT /note="LYPX(n)L motif 1"
FT /evidence="ECO:0000250|UniProtKB:O08992"
FT MOTIF 47..51
FT /note="LYPX(n)L motif 2"
FT /evidence="ECO:0000250|UniProtKB:O08992"
FT MOTIF 51..55
FT /note="LYPX(n)L motif 3"
FT /evidence="ECO:0000250|UniProtKB:O08992"
FT BINDING 252..253
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00560"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5A2P"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5A2P"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6AK2"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:6AK2"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5G1E"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5G1E"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5G1E"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:5G1E"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:5G1E"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:5G1E"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5G1E"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:5G1E"
SQ SEQUENCE 300 AA; 32423 MW; F52D8918DE17F710 CRC64;
MSLYPSLEDL KVDKVIQAQT ASSANPASQA FFLNVVDSAA FPPGGNLYPK LYPELSQYMG
LSLSEAEICE NMPVVSGAPT QGQLVARPSS VNYMVAPVTG NDAGIRRAEI KQGIREVILC
KDQDGKIGLR LKSVDNGIFV QLVQANSPAS LVGLRFGDQV LQINGENCAG WSSDKAHKVL
KQAFGEKITM TIRDRPFERT VTMHKDSSGH VGFIFKSGKI TSIVKDSSAA RNGLLTDHHI
CEINGQNVIG LKDAQIADIL STAGTVVTIT IMPAFIFEHI IKRMAPSIMK SLMDHTIPEV
