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O75056 (SDC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-3

Short name=SYND3
Gene names
Name:SDC3
Synonyms:KIAA0468
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface proteoglycan that may bear heparan sulfate By similarity. May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism. Ref.1

Subunit structure

Interacts with TIAM1. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in the nervous system, the adrenal gland, and the spleen. Ref.1

Post-translational modification

O-glycosylated within the Thr/Ser-rich region which could interact with lectin domains on other molecules Probable.

Sequence similarities

Belongs to the syndecan proteoglycan family.

Sequence caution

The sequence BAA32313.2 differs from that shown. Reason: Intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Syndecan-3
PRO_0000183989

Regions

Topological domain1 – 387387Extracellular Potential
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 44234Cytoplasmic Potential
Compositional bias115 – 302188Ser/Thr-rich (mucin-like)

Sites

Site383 – 3842Cleavage of ectodomain Potential

Amino acid modifications

Modified residue4091Phosphotyrosine Ref.5
Modified residue4191Phosphotyrosine Ref.5
Modified residue4311Phosphotyrosine Ref.5
Modified residue4411Phosphotyrosine Ref.5
Glycosylation801O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation821O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation841O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation911O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation3141O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation3671O-linked (Xyl...) (glycosaminoglycan) Potential

Natural variations

Natural variant2081V → I.
Corresponds to variant rs2491132 [ dbSNP | Ensembl ].
VAR_027251
Natural variant3031D → N. Ref.1
Corresponds to variant rs4949184 [ dbSNP | Ensembl ].
VAR_027252
Natural variant3291T → I.
Corresponds to variant rs2282440 [ dbSNP | Ensembl ].
VAR_027253

Sequences

Sequence LengthMass (Da)Tools
O75056 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: D4C284CBC36A92E2

FASTA44245,497
        10         20         30         40         50         60 
MKPGPPHRAG AAHGAGAGAG AAAGPGARGL LLPPLLLLLL AGRAAGAQRW RSENFERPVD 

        70         80         90        100        110        120 
LEGSGDDDSF PDDELDDLYS GSGSGYFEQE SGIETAMRFS PDVALAVSTT PAVLPTTNIQ 

       130        140        150        160        170        180 
PVGTPFEELP SERPTLEPAT SPLVVTEVPE EPSQRATTVS TTMATTAATS TGDPTVATVP 

       190        200        210        220        230        240 
ATVATATPST PAAPPFTATT AVIRTTGVRR LLPLPLTTVA TARATTPEAP SPPTTAAVLD 

       250        260        270        280        290        300 
TEAPTPRLVS TATSRPRALP RPATTQEPDI PERSTLPLGT TAPGPTEVAQ TPTPETFLTT 

       310        320        330        340        350        360 
IRDEPEVPVS GGPSGDFELP EEETTQPDTA NEVVAVGGAA AKASSPPGTL PKGARPGPGL 

       370        380        390        400        410        420 
LDNAIDSGSS AAQLPQKSIL ERKEVLVAVI VGGVVGALFA AFLVTLLIYR MKKKDEGSYT 

       430        440 
LEEPKQASVT YQKPDKQEEF YA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of human syndecan-3."
Berndt C., Casaroli-Marano R.P., Vilaro S., Reina M.
J. Cell. Biochem. 82:246-259(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT ASN-303.
[2]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Muscle.
[5]"Phosphorylation of recombinant N-syndecan (syndecan 3) core protein."
Asundi V.K., Carey D.J.
Biochem. Biophys. Res. Commun. 240:502-506(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-409; TYR-419; TYR-431 AND TYR-441.
[6]"The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics."
Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.
Structure 21:342-354(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIAM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF248634 mRNA. Translation: AAK39969.1.
AB007937 mRNA. Translation: BAA32313.2. Sequence problems.
AL445235 Genomic DNA. Translation: CAI22245.1.
AL445235 Genomic DNA. Translation: CAI22250.1.
BC013974 mRNA. No translation available.
CCDSCCDS30661.1.
RefSeqNP_055469.3. NM_014654.3.
UniGeneHs.158287.

3D structure databases

ProteinModelPortalO75056.
SMRO75056. Positions 410-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115027. 9 interactions.
DIPDIP-29944N.
IntActO75056. 2 interactions.
MINTMINT-3057059.
STRING9606.ENSP00000344468.

PTM databases

PhosphoSiteO75056.

Proteomic databases

MaxQBO75056.
PaxDbO75056.
PRIDEO75056.

Protocols and materials databases

DNASU9672.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339394; ENSP00000344468; ENSG00000162512.
GeneID9672.
KEGGhsa:9672.
UCSCuc001bse.2. human.

Organism-specific databases

CTD9672.
GeneCardsGC01M031342.
H-InvDBHIX0000348.
HGNCHGNC:10660. SDC3.
HPACAB025786.
HPA017087.
MIM186357. gene.
neXtProtNX_O75056.
PharmGKBPA35590.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85596.
HOGENOMHOG000049151.
HOVERGENHBG004144.
InParanoidO75056.
KOK16337.
OMAETAMRFS.
PhylomeDBO75056.
TreeFamTF320463.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressO75056.
BgeeO75056.
CleanExHS_SDC3.
GenevestigatorO75056.

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

ChiTaRSSDC3. human.
GeneWikiSDC3.
GenomeRNAi9672.
NextBio36319.
PROO75056.
SOURCESearch...

Entry information

Entry nameSDC3_HUMAN
AccessionPrimary (citable) accession number: O75056
Secondary accession number(s): Q5T1Z6 expand/collapse secondary AC list , Q5T1Z7, Q96CT3, Q96PR8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM