Syndecan-4 precursor - Mus musculus (Mouse)

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O35988 (SDC4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Syndecan-4
Short name=SYND4

Alternative name(s):
Ryudocan core protein

Gene names

Name:

Sdc4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane Secreted
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Heparan sulfate Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of focal adhesion assembly Inferred from electronic annotation. Source: Compara positive regulation of protein kinase activity Inferred from electronic annotation. Source: Compara positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara ureteric bud development Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome cell surface Inferred from direct assay PubMed 15381701. Source: MGI costamere Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from electronic annotation. Source: Compara
Molecular_function	thrombospondin receptor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Chain

24 – 198

175

Syndecan-4

PRO_0000033512

Regions

Topological domain

24 – 145

122

Extracellular Potential

Transmembrane

146 – 170

Helical; Potential

Topological domain

171 – 198

Cytoplasmic Potential

Amino acid modifications

Glycosylation

O-linked (Xyl...) (heparan sulfate) By similarity

Glycosylation

O-linked (Xyl...) (heparan sulfate) Potential

Glycosylation

O-linked (Xyl...) (heparan sulfate) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O35988 [UniParc].

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

198

21,482

        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' referencesShow '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.
IPI	IPI00136382.
PIR	JC5613.
RefSeq	NP_035651.1. NM_011521.2.
UniGene	Mm.490266.
3D structure databases
ProteinModelPortal	O35988.
SMR	O35988. Positions 171-198.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000017153.
PTM databases
PhosphoSite	O35988.
Proteomic databases
PaxDb	O35988.
PRIDE	O35988.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017153; ENSMUSP00000017153; ENSMUSG00000017009.
GeneID	20971.
KEGG	mmu:20971.
Organism-specific databases
CTD	6385.
MGI	MGI:1349164. Sdc4.
Phylogenomic databases
eggNOG	NOG83582.
HOGENOM	HOG000263414.
HOVERGEN	HBG004501.
InParanoid	O35988.
KO	K16338.
OMA	EGRYFSG.
OrthoDB	EOG4MSD0Z.
Enzyme and pathway databases
Reactome	REACT_112621. Metabolism. REACT_118324. Disease.
Gene expression databases
ArrayExpress	O35988.
Bgee	O35988.
CleanEx	MM_SDC4.
Genevestigator	O35988.
GermOnline	ENSMUSG00000017009. Mus musculus.
Family and domain databases
InterPro	IPR003585. Neurexin-like. IPR001050. Syndecan. [Graphical view]
PANTHER	PTHR10915. PTHR10915. 1 hit.
Pfam	PF01034. Syndecan. 1 hit. [Graphical view]
SMART	SM00294. 4.1m. 1 hit. [Graphical view]
PROSITE	PS00964. SYNDECAN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SDC4. mouse.
NextBio	299938.
PMAP-CutDB	O35988.
SOURCE	Search...

Entry information

Entry name

SDC4_MOUSE

Accession

Primary (citable) accession number: O35988

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents