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Reviewed, UniProtKB/Swiss-Prot P49415 (SDC_DROME)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Syndecan
Gene names
Name: Sdc
Synonyms: Syd
ORF Names: CG10497
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length399 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. Required for axonal and myotube guidance, is a necessary component of slit/robo signaling and is required in the slit target cells. Ref.1 Ref.2

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

In 13-16 hours embryos, expressed in lymph glands, peripheral and central nervous system and basal surfaces of gut epithelia. Sdc and robo are coexpressed in domains adjacent to slit; in tracheal pits and midline glia cells. Ref.1 Ref.2

Disruption phenotype

Flies exhibit aberrant midline guidance of axons and establishment of muscle pattern. Ref.2

Sequence similarities

Belongs to the syndecan proteoglycan family.

Ontologies

Keywords
   Biological processDifferentiation
Myogenesis
Neurogenesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
   Molecular functionDevelopmental protein
   PTMGlycoprotein
Heparan sulfate
Proteoglycan
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdetection of light stimulus involved in visual perception

Inferred from mutant phenotype. Source: FlyBase

motor axon guidance

Inferred from mutant phenotype. Source: FlyBase

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncytoskeletal protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P49415-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P49415-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     115-287: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 399371Syndecan
PRO_0000033515

Regions

Topological domain29 – 340312Extracellular Potential
Transmembrane341 – 36525 Potential
Topological domain366 – 39934Cytoplasmic Potential
Compositional bias114 – 17461Pro/Ser/Thr-rich

Amino acid modifications

Glycosylation621O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation791O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation811O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1101O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation1941O-linked (Xyl...) (glycosaminoglycan) Potential

Natural variations

Alternative sequence115 – 287173Missing in isoform B.
VSP_011792

Experimental info

Sequence conflict40 – 423APS → RHP in AAC34307. Ref.1
Sequence conflict137 – 1415Missing in AAC34307. Ref.1
Sequence conflict1681T → TT in AAC34307. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: FCBC6EA17C5DADBD

FASTA39942,088
        10         20         30         40         50         60 
MKPKQKISVE PLLLVAILIG VLVAATHAQD QKSVKPSAAA PSAAASRPHD EIYIDDDSIE 

        70         80         90        100        110        120 
GSGGRGGIHE DLEKDPDYSG SGFGPDDEDA EPDQHSHSSH NTRISQSSNS GINTAHTPTQ 

       130        140        150        160        170        180 
TSSTIPTTST STPMPTTTPT ATTPASTTTA AATQISSFAN SSSTTTTTLA PTIPAEPQQP 

       190        200        210        220        230        240 
LFPPFDKDLD TESSGDGIDA DAEDDDEDDG DDKDYDYNKE LDKEIDIDGP EPGHLPPVVH 

       250        260        270        280        290        300 
HNTVETGHIP TTDEIDVDGG DEDDNGDSDI DGPRIGGNDG DITERGPGAG GSNVHELDPN 

       310        320        330        340        350        360 
TNVNSQPSDT KGIDHRPNGN EVVIMSEDDR TSSFFSQPGI LAAVIGGAVV GLLCAILVVM 

       370        380        390 
FIVYRMRKKD EGSYALDEPK RSPANNSYAK NANNREFYA 

« Hide

Isoform B (C).

Checksum: FF4083118628498F
Show »

FASTA22624,039

References

« Hide 'large scale' references
[1]"Drosophila syndecan: conservation of a cell-surface heparan sulfate proteoglycan."
Spring J., Paine-Saunders S.E., Hynes R.O., Bernfield M.
Proc. Natl. Acad. Sci. U.S.A. 91:3334-3338(1994) [PubMed: 8159748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY.
[2]"Heparan sulfate proteoglycan syndecan promotes axonal and myotube guidance by slit/robo signaling."
Steigemann P., Molitor A., Fellert S., Jackle H., Vorbruggen G.
Curr. Biol. 14:225-230(2004) [PubMed: 14761655] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

U03282 mRNA. Translation: AAC34307.1.
AE013599 Genomic DNA. Translation: AAF46724.2.
AE013599 Genomic DNA. Translation: AAM70897.1.
AY069377 mRNA. Translation: AAL39522.1.
AY089610 mRNA. Translation: AAL90348.1.
PIRA54949.
RefSeqNP_476965.1.
NP_726071.1.
UniGeneDm.721

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP49415. 2 interactions.

Genome annotation databases

EnsemblFBgn0010415. Drosophila melanogaster. [Contig view]
GeneID37447.
KEGGdme:Dmel_CG10497.
NMPDRfig|7227.3.peg.6651.

Organism-specific databases

FlyBaseFBgn0010415. Sdc.

Phylogenomic databases

HOGENOMP49415.

Gene expression databases

ArrayExpressP49415.
GermOnlineCG10497. Drosophila melanogaster.

Family and domain databases

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

Other Resources

NextBio803680.

Entry information

Entry nameSDC_DROME
AccessionPrimary (citable) accession number: P49415
Secondary accession number(s): Q0E8Z8, Q8SXJ0, Q9W2G7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 25, 2004
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents