SDC3_RAT
ID SDC3_RAT Reviewed; 442 AA.
AC P33671; P97614;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Syndecan-3;
DE Short=SYND3;
DE AltName: Full=N-syndecan;
DE AltName: Full=Neuroglycan;
DE Flags: Precursor;
GN Name=Sdc3; Synonyms=Synd3;
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].
RC STRAIN=Sprague-Dawley;
RA Kung C.E., Deuel T.F.;
RT "Cloning of rat and mouse syndecan-3 cDNAs.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9006931; DOI=10.1074/jbc.272.5.2873;
RA Carey D.J., Conner K., Asundi V.K., O'Mahony D.J., Stahl R.C.,
RA Showalter L., Cizmeci-Smith G., Hartman J., Rothblum L.I.;
RT "cDNA cloning, genomic organization, and in vivo expression of rat N-
RT syndecan.";
RL J. Biol. Chem. 272:2873-2879(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-442.
RC STRAIN=Sprague-Dawley; TISSUE=Schwann cell;
RX PubMed=1556152; DOI=10.1083/jcb.117.1.191;
RA Carey D.J., Evans D.M., Stahl R.C., Asundi V.K., Conner K.J., Garbes P.,
RA Cizmeci-Smith G.;
RT "Molecular cloning and characterization of N-syndecan, a novel
RT transmembrane heparan sulfate proteoglycan.";
RL J. Cell Biol. 117:191-201(1992).
RN [4]
RP INTERACTION WITH PTN.
RX PubMed=8175719; DOI=10.1016/s0021-9258(18)99975-8;
RA Raulo E., Chernousov M.A., Carey D.J., Nolo R., Rauvala H.;
RT "Isolation of a neuronal cell surface receptor of heparin binding growth-
RT associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3).";
RL J. Biol. Chem. 269:12999-13004(1994).
RN [5]
RP INTERACTION WITH MDK.
RX PubMed=9089390;
RA Nakanishi T., Kadomatsu K., Okamoto T., Ichihara-Tanaka K., Kojima T.,
RA Saito H., Tomoda Y., Muramatsu T.;
RT "Expression of syndecan-1 and -3 during embryogenesis of the central
RT nervous system in relation to binding with midkine.";
RL J. Biochem. 121:197-205(1997).
RN [6]
RP INTERACTION WITH PTN.
RX PubMed=9817766; DOI=10.1083/jcb.143.4.1113;
RA Imai S., Kaksonen M., Raulo E., Kinnunen T., Fages C., Meng X., Lakso M.,
RA Rauvala H.;
RT "Osteoblast recruitment and bone formation enhanced by cell matrix-
RT associated heparin-binding growth-associated molecule (HB-GAM).";
RL J. Cell Biol. 143:1113-1128(1998).
CC -!- FUNCTION: Cell surface proteoglycan that may bear heparan sulfate. May
CC have a role in the organization of cell shape by affecting the actin
CC cytoskeleton, possibly by transferring signals from the cell surface in
CC a sugar-dependent mechanism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TIAM1 (By similarity). Interacts (via heparan
CC sulfate chains) with PTN; this interaction mediates the neurite
CC outgrowth-promoting signal from PTN to the cytoskeleton of growing
CC neurites; this interaction mediates osteoblast recruitment
CC (PubMed:8175719, PubMed:9817766). Interacts with MDK; this interaction
CC induces SDC3 clustering; this interaction induces neuronal cell
CC adhesion and neurite outgrowth (PubMed:9089390). {ECO:0000250,
CC ECO:0000250|UniProtKB:O75056, ECO:0000269|PubMed:8175719,
CC ECO:0000269|PubMed:9089390, ECO:0000269|PubMed:9817766}.
CC -!- INTERACTION:
CC P33671; P34900: Sdc2; NbExp=2; IntAct=EBI-1173159, EBI-1173032;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: High levels in neonatal brain, heart, and Schwann
CC cells, barely detectable in neonatal or adult liver, or adult brain.
CC -!- DEVELOPMENTAL STAGE: Higher levels in developing tissues.
CC -!- PTM: O-glycosylated within the Thr/Ser-rich region which could interact
CC with lectin domains on other molecules. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; U52825; AAB03284.1; -; mRNA.
DR EMBL; U73184; AAB18192.1; -; mRNA.
DR EMBL; X63143; CAA44848.1; -; mRNA.
DR PIR; A41558; A41558.
DR RefSeq; NP_446345.3; NM_053893.3.
DR AlphaFoldDB; P33671; -.
DR SMR; P33671; -.
DR BioGRID; 250556; 4.
DR IntAct; P33671; 4.
DR STRING; 10116.ENSRNOP00000041634; -.
DR GlyGen; P33671; 6 sites.
DR iPTMnet; P33671; -.
DR PhosphoSitePlus; P33671; -.
DR PaxDb; P33671; -.
DR PRIDE; P33671; -.
DR GeneID; 116673; -.
DR KEGG; rno:116673; -.
DR UCSC; RGD:621486; rat.
DR CTD; 9672; -.
DR RGD; 621486; Sdc3.
DR eggNOG; ENOG502QTD2; Eukaryota.
DR InParanoid; P33671; -.
DR OrthoDB; 1340825at2759; -.
DR PhylomeDB; P33671; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR Reactome; R-RNO-2024096; HS-GAG degradation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P33671; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0044393; C:microspike; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IDA:CACAO.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR031194; Syndecan-3.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF7; PTHR10915:SF7; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein;
KW Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..442
FT /note="Syndecan-3"
FT /id="PRO_0000033509"
FT TOPO_DOM 45..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 383..384
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 419
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 78
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 161
FT /note="O-linked (GalNAc) serine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 162
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 163
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 170
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 172
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 315
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="Q -> E (in Ref. 1; AAB03284)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="Q -> E (in Ref. 1; AAB03284)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..91
FT /note="GL -> LR (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> G (in Ref. 1; AAB03284)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> S (in Ref. 1; AAB03284)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> V (in Ref. 1; AAB03284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 45919 MW; 4842C8BEAA0A338C CRC64;
MKPGPPRRGT AQGQRVDTAT HGPGARGLLL PPLLLLLLAG RAAGAQRWRN ENFERPVDLE
GSGDDDSFPD DELDDLYSGS GSGYFEQESG LETAMRFIPD IALAAPTAPA MLPTTVIQPV
DTPFEELLSE HPGPEPVTSP PLVTEVTEVV EEPSQRATTI STTTSTTAAT TTGAPTMATA
PATAATTAPS TPAAPPATAT TADIRTTGIQ GLLPLPLTTA ATAKATTPAV PSPPTTVTTL
DTEAPTPRLV NTATSRPRAL PRPVTTQEPE VAERSTLPLG TTAPGPTEVA QTPTPESLLT
TTQDEPEVPV SGGPSGDFEL QEETTQPDTA NEVVAVEGAA AKPSPPLGTL PKGARPGLGL
HDNAIDSGSS AAQLPQKSIL ERKEVLVAVI VGGVVGALFA AFLVTLLIYR MKKKDEGSYT
LEEPKQASVT YQKPDKQEEF YA
