SDC_DROME
ID SDC_DROME Reviewed; 399 AA.
AC P49415; Q0E8Z8; Q8SXJ0; Q9W2G7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Syndecan;
DE Flags: Precursor;
GN Name=Sdc; Synonyms=Syd; ORFNames=CG10497;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8159748; DOI=10.1073/pnas.91.8.3334;
RA Spring J., Paine-Saunders S.E., Hynes R.O., Bernfield M.;
RT "Drosophila syndecan: conservation of a cell-surface heparan sulfate
RT proteoglycan.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3334-3338(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14761655; DOI=10.1016/j.cub.2004.01.006;
RA Steigemann P., Molitor A., Fellert S., Jackle H., Vorbruggen G.;
RT "Heparan sulfate proteoglycan syndecan promotes axonal and myotube guidance
RT by slit/robo signaling.";
RL Curr. Biol. 14:225-230(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Required for axonal and myotube guidance, is a necessary component of
CC slit/robo signaling and is required in the slit target cells.
CC {ECO:0000269|PubMed:14761655, ECO:0000269|PubMed:8159748}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P49415-1; Sequence=Displayed;
CC Name=B; Synonyms=C;
CC IsoId=P49415-2; Sequence=VSP_011792;
CC -!- TISSUE SPECIFICITY: In 13-16 hours embryos, expressed in lymph glands,
CC peripheral and central nervous system and basal surfaces of gut
CC epithelia. Sdc and robo are coexpressed in domains adjacent to slit; in
CC tracheal pits and midline glia cells. {ECO:0000269|PubMed:14761655,
CC ECO:0000269|PubMed:8159748}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit aberrant midline guidance of axons
CC and establishment of muscle pattern. {ECO:0000269|PubMed:14761655}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U03282; AAC34307.1; -; mRNA.
DR EMBL; AE013599; AAF46724.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM70897.1; -; Genomic_DNA.
DR EMBL; AY069377; AAL39522.1; -; mRNA.
DR EMBL; AY089610; AAL90348.1; -; mRNA.
DR PIR; A54949; A54949.
DR RefSeq; NP_476965.1; NM_057617.5. [P49415-1]
DR RefSeq; NP_726071.1; NM_166449.5. [P49415-2]
DR AlphaFoldDB; P49415; -.
DR BioGRID; 63077; 17.
DR IntAct; P49415; 58.
DR GlyGen; P49415; 6 sites.
DR PaxDb; P49415; -.
DR DNASU; 37447; -.
DR EnsemblMetazoa; FBtr0071706; FBpp0071623; FBgn0010415. [P49415-1]
DR EnsemblMetazoa; FBtr0071707; FBpp0071624; FBgn0010415. [P49415-2]
DR GeneID; 37447; -.
DR KEGG; dme:Dmel_CG10497; -.
DR UCSC; CG10497-RA; d. melanogaster. [P49415-1]
DR CTD; 37447; -.
DR FlyBase; FBgn0010415; Sdc.
DR VEuPathDB; VectorBase:FBgn0010415; -.
DR eggNOG; ENOG502S3JC; Eukaryota.
DR GeneTree; ENSGT00940000168670; -.
DR InParanoid; P49415; -.
DR PhylomeDB; P49415; -.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-DME-2022928; HS-GAG biosynthesis.
DR Reactome; R-DME-2024096; HS-GAG degradation.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 37447; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Sdc; fly.
DR GenomeRNAi; 37447; -.
DR PRO; PR:P49415; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010415; Expressed in brain and 92 other tissues.
DR ExpressionAtlas; P49415; baseline and differential.
DR Genevisible; P49415; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0098595; C:perivitelline space; HDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0021782; P:glial cell development; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR InterPro; IPR031198; Syndecan_inverte.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF1; PTHR10915:SF1; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Differentiation; Glycoprotein;
KW Heparan sulfate; Membrane; Myogenesis; Neurogenesis; Proteoglycan;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..399
FT /note="Syndecan"
FT /id="PRO_0000033515"
FT TOPO_DOM 29..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 115..287
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:14761655"
FT /id="VSP_011792"
FT CONFLICT 40..42
FT /note="APS -> RHP (in Ref. 1; AAC34307)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..141
FT /note="Missing (in Ref. 1; AAC34307)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="T -> TT (in Ref. 1; AAC34307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42088 MW; FCBC6EA17C5DADBD CRC64;
MKPKQKISVE PLLLVAILIG VLVAATHAQD QKSVKPSAAA PSAAASRPHD EIYIDDDSIE
GSGGRGGIHE DLEKDPDYSG SGFGPDDEDA EPDQHSHSSH NTRISQSSNS GINTAHTPTQ
TSSTIPTTST STPMPTTTPT ATTPASTTTA AATQISSFAN SSSTTTTTLA PTIPAEPQQP
LFPPFDKDLD TESSGDGIDA DAEDDDEDDG DDKDYDYNKE LDKEIDIDGP EPGHLPPVVH
HNTVETGHIP TTDEIDVDGG DEDDNGDSDI DGPRIGGNDG DITERGPGAG GSNVHELDPN
TNVNSQPSDT KGIDHRPNGN EVVIMSEDDR TSSFFSQPGI LAAVIGGAVV GLLCAILVVM
FIVYRMRKKD EGSYALDEPK RSPANNSYAK NANNREFYA
