P49415 (SDC_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Syndecan

Gene names

Name:	Sdc
Synonyms:	Syd
ORF Names:	CG10497

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 process	Differentiation Myogenesis Neurogenesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Glycoprotein Heparan sulfate Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	detection of light stimulus involved in visual perception Inferred from mutant phenotype. Source: FlyBase energy homeostasis 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 regulation of multicellular organismal metabolic process Inferred from mutant phenotype. Source: FlyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytoskeletal protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 399	371	Syndecan		PRO_0000033515
Regions
	Topological domain	29 – 340	312	Extracellular Potential
	Transmembrane	341 – 365	25	Helical; Potential
	Topological domain	366 – 399	34	Cytoplasmic Potential
	Compositional bias	114 – 174	61	Pro/Ser/Thr-rich
Amino acid modifications
	Glycosylation	62	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	79	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	81	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	110	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	O-linked (Xyl...) (glycosaminoglycan) Potential
Natural variations
	Alternative sequence	115 – 287	173	Missing in isoform B.		VSP_011792
Experimental info
	Sequence conflict	40 – 42	3	APS → RHP in AAC34307. Ref.1
	Sequence conflict	137 – 141	5	Missing in AAC34307. Ref.1
	Sequence conflict	168	1	T → TT in AAC34307. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 25, 2004. Version 2. Checksum: FCBC6EA17C5DADBD	FASTA	399	42,088
	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
	Isoform B (C) [UniParc]. Checksum: FF4083118628498F	FASTA	226	24,039
	10 20 30 40 50 60 MKPKQKISVE PLLLVAILIG VLVAATHAQD QKSVKPSAAA PSAAASRPHD EIYIDDDSIE 70 80 90 100 110 120 GSGGRGGIHE DLEKDPDYSG SGFGPDDEDA EPDQHSHSSH NTRISQSSNS GINTGAGGSN 130 140 150 160 170 180 VHELDPNTNV NSQPSDTKGI DHRPNGNEVV IMSEDDRTSS FFSQPGILAA VIGGAVVGLL 190 200 210 220 CAILVVMFIV YRMRKKDEGS YALDEPKRSP ANNSYAKNAN NREFYA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. Strain: Berkeley.
[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
EMBL GenBank DDBJ	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.
PIR	A54949.
RefSeq	NP_001163238.1. NM_001169767.1. NP_476965.1. NM_057617.4. NP_726071.1. NM_166449.4. NP_726072.1. NM_166450.2.
UniGene	Dm.721.
3D structure databases
ProteinModelPortal	P49415.
SMR	P49415. Positions 365-399.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49415. 2 interactions.
MINT	MINT-807380.
STRING	P49415.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071706; FBpp0071623; FBgn0010415. FBtr0301557; FBpp0290772; FBgn0010415.
GeneID	37447.
KEGG	dme:Dmel_CG10497.
NMPDR	fig|7227.3.peg.6651.
UCSC	CG10497-RA. d. melanogaster.
Organism-specific databases
CTD	37447.
FlyBase	FBgn0010415. Sdc.
Phylogenomic databases
eggNOG	inNOG10924.
GeneTree	EMGT00050000002086.
InParanoid	P49415.
OMA	GGIHDDL.
OrthoDB	EOG4TMPJJ.
Gene expression databases
ArrayExpress	P49415.
Bgee	P49415.
GermOnline	CG10497. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003585. Neurexin-like. IPR001050. Syndecan. [Graphical view]
KO	K06257.
PANTHER	PTHR10915. Syndecan. 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
NextBio	803680.

Entry information

Entry name

SDC_DROME

Accession

Primary (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:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project