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O35988 (SDC4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syndecan-4

Short name=SYND4
Alternative name(s):
Ryudocan core protein
Gene names
Name:Sdc4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface proteoglycan that bears heparan sulfate.

Subunit structure

Homodimer. Interacts with CDCP1 and SDCBP By similarity. Interacts (via its cytoplasmic domain) with GIPC (via its PDZ domain). Interacts (via its cytoplasmic domain) with NUDT16L1. Ref.4 Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein. Secreted. Note: Shedding of the ectodomain produces a soluble form.

Tissue specificity

Ubiquitous. Highest levels in liver, kidney and lung.

Post-translational modification

Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3.

Sequence similarities

Belongs to the syndecan proteoglycan family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 198175Syndecan-4
PRO_0000033512

Regions

Topological domain24 – 145122Extracellular Potential
Transmembrane146 – 17025Helical; Potential
Topological domain171 – 19828Cytoplasmic Potential

Amino acid modifications

Glycosylation441O-linked (Xyl...) (heparan sulfate) By similarity
Glycosylation621O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation641O-linked (Xyl...) (heparan sulfate) Potential

Sequences

Sequence LengthMass (Da)Tools
O35988 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 4246963EC6A25915

FASTA19821,482
        10         20         30         40         50         60 
MAPACLLAPL LLLLLGGFPL VPGESIRETE VIDPQDLLEG RYFSGALPDD EDAGGSDDFE 

        70         80         90        100        110        120 
LSGSGDLDDT EEPRPFPEVI EPLVPLDNHI PENAQPGIRV PSEPKELEEN EVIPKRAPSD 

       130        140        150        160        170        180 
VGDDMSNKVS MSSTAQGSNI FERTEVLAAL IVGGVVGILF AVFLILLLVY RMKKKDEGSY 

       190 
DLGKKPIYKK APTNEFYA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, genomic organization, promoter activity, and tissue-specific expression of the mouse ryudocan gene."
Tsuzuki S., Kojima T., Katsumi A., Yamazaki T., Sugiura I., Saito H.
J. Biochem. 122:17-24(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ and C3H/An.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[3]"Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase."
Fitzgerald M.L., Wang Z., Park P.W., Murphy G., Bernfield M.
J. Cell Biol. 148:811-824(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SHEDDING.
[4]"Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration."
Gao Y., Li M., Chen W., Simons M.
J. Cell. Physiol. 184:373-379(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GIPC.
[5]"Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5."
Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S., French B., Neveu W., Goetinck P.F.
J. Biol. Chem. 277:12270-12274(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUDT16L1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89571 mRNA. Translation: BAA22135.1.
D89572 Genomic DNA. Translation: BAA22136.1.
BC005679 mRNA. Translation: AAH05679.1.
PIRJC5613.
RefSeqNP_035651.1. NM_011521.2.
UniGeneMm.3815.

3D structure databases

ProteinModelPortalO35988.
SMRO35988. Positions 171-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000017153.

Chemistry

ChEMBLCHEMBL2062355.

PTM databases

PhosphoSiteO35988.

Proteomic databases

PaxDbO35988.
PRIDEO35988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017153; ENSMUSP00000017153; ENSMUSG00000017009.
GeneID20971.
KEGGmmu:20971.
UCSCuc008nuq.1. mouse.

Organism-specific databases

CTD6385.
MGIMGI:1349164. Sdc4.

Phylogenomic databases

eggNOGNOG83582.
HOGENOMHOG000263414.
HOVERGENHBG004501.
InParanoidO35988.
KOK16338.
OMAEGRYFSG.
OrthoDBEOG7RV9HS.
PhylomeDBO35988.
TreeFamTF320463.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.
REACT_189085. Disease.

Gene expression databases

ArrayExpressO35988.
BgeeO35988.
CleanExMM_SDC4.
GenevestigatorO35988.

Family and domain databases

InterProIPR003585. Neurexin-like.
IPR001050. Syndecan.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PANTHERPTHR10915. PTHR10915. 1 hit.
PfamPF01034. Syndecan. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
[Graphical view]
PROSITEPS00964. SYNDECAN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDC4. mouse.
NextBio299938.
PMAP-CutDBO35988.
PROO35988.
SOURCESearch...

Entry information

Entry nameSDC4_MOUSE
AccessionPrimary (citable) accession number: O35988
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot