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UniProtKB/Swiss-Prot entry P49415


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SDC_DROME
Primary accession number P49415
Secondary accession numbers Q0E8Z8 Q8SXJ0 Q9W2G7
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on October 25, 2004 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 64)
Name and origin of the protein
Protein name Syndecan [Precursor]
Synonyms None
Gene name
Name: Sdc
Synonyms: Syd
ORFNames: CG10497
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8159748 [NCBI, ExPASy, EBI, Israel, Japan]
Spring J., Paine-Saunders S.E., Hynes R.O., Bernfield M.;
"Drosophila syndecan: conservation of a cell-surface heparan sulfate proteoglycan.";
Proc. Natl. Acad. Sci. U.S.A. 91:3334-3338(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0960-9822(04)00007-7; PubMed=14761655 [NCBI, ExPASy, EBI, Israel, Japan]
Steigemann P., Molitor A., Fellert S., Jackle H., Vorbruggen G.;
"Heparan sulfate proteoglycan syndecan promotes axonal and myotube guidance by slit/robo signaling.";
Curr. Biol. 14:225-230(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U03282; AAC34307.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF46724.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAM70897.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069377; AAL39522.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY089610; AAL90348.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A54949; A54949.
RefSeq NP_476965.1; -.
NP_726071.1; -.
UniGene Dm.721
3D structure databases
ModBase P49415.
Protein-protein interaction databases
IntAct P49415; 2.
Organism-specific databases
FlyBase FBgn0010415; Sdc.
Gene expression databases
ArrayExpress P49415; -.
GermOnline CG10497; Drosophila melanogaster.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008092; Molecular function: cytoskeletal protein binding (inferred from electronic annotation from InterPro).
GO:0050908; Biological process: detection of light stimulus involved in visual perception (inferred from mutant phenotype from FlyBase).
GO:0008045; Biological process: motor axon guidance (inferred from mutant phenotype from FlyBase).
GO:0007519; Biological process: skeletal muscle development (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003585; Neurexin-like.
IPR001050; Syndecan.
Graphical view of domain structure.
PANTHER PTHR10915; Syndecan; 1.
Pfam PF01034; Syndecan; 1.
Pfam graphical view of domain structure.
SMART SM00294; 4.1m; 1.
SMART graphical view of domain structure.
PROSITE PS00964; SYNDECAN; 1.
Genome annotation databases
Ensembl CG10497; Drosophila melanogaster. [Contig view]
GeneID 37447; -.
KEGG dme:Dmel_CG10497; -.
NMPDR fig|7227.3.peg.6651; -.
Phylogenomic databases
HOGENOM P49415; -.
Other
NextBio 803680; -.
ProtoNet P49415.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Developmental protein; Differentiation; Glycoprotein; Heparan sulfate; Membrane; Myogenesis; Neurogenesis; Proteoglycan; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
CHAIN   29   399  371     Syndecan. PRO_0000033515
TOPO_DOM   29   340  312     Extracellular (Potential). 
TRANSMEM   341   365  25     Potential. 
TOPO_DOM   366   399  34     Cytoplasmic (Potential). 
COMPBIAS   114   174  61     Pro/Ser/Thr-rich. 
CARBOHYD   62    62        O-linked (Xyl...) (glycosaminoglycan) (Potential). 
CARBOHYD   79    79        O-linked (Xyl...) (glycosaminoglycan) (Potential). 
CARBOHYD   81    81        O-linked (Xyl...) (glycosaminoglycan) (Potential). 
CARBOHYD   110   110        O-linked (Xyl...) (glycosaminoglycan) (Potential). 
CARBOHYD   160   160        N-linked (GlcNAc...) (Potential). 
CARBOHYD   194   194        O-linked (Xyl...) (glycosaminoglycan) (Potential). 
VAR_SEQ   115   287        Missing (in isoform B). VSP_011792
CONFLICT   40    42        APS -> RHP (in Ref. 1; AAC34307). 
CONFLICT   137   141        Missing (in Ref. 1; AAC34307). 
CONFLICT   168   168        T -> TT (in Ref. 1; AAC34307). 
Sequence information
Length: 399 AA [This is the length of the unprocessed precursor] Molecular weight: 42088 Da [This is the MW of the unprocessed precursor] CRC64: FCBC6EA17C5DADBD [This is a checksum on the sequence]
        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 

P49415 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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