SDC_CAEEL
ID SDC_CAEEL Reviewed; 288 AA.
AC P50605;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable syndecan;
DE Flags: Precursor;
GN Name=sdn-1 {ECO:0000312|WormBase:F57C7.3a};
GN ORFNames=F57C7.3 {ECO:0000312|WormBase:F57C7.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=24066155; DOI=10.1371/journal.pone.0074908;
RA Gysi S., Rhiner C., Flibotte S., Moerman D.G., Hengartner M.O.;
RT "A network of HSPG core proteins and HS modifying enzymes regulates netrin-
RT dependent guidance of D-type motor neurons in Caenorhabditis elegans.";
RL PLoS ONE 8:E74908-E74908(2013).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION
RP PHENOTYPE, GLYCOSYLATION AT SER-71; SER-86 AND SER-214, AND MUTAGENESIS OF
RP SER-71; SER-86 AND SER-214.
RX PubMed=25344071; DOI=10.1242/dev.113266;
RA Dejima K., Kang S., Mitani S., Cosman P.C., Chisholm A.D.;
RT "Syndecan defines precise spindle orientation by modulating Wnt signaling
RT in C. elegans.";
RL Development 141:4354-4365(2014).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26022293; DOI=10.1534/g3.115.018770;
RA Sundararajan L., Norris M.L., Lundquist E.A.;
RT "SDN-1/Syndecan acts in parallel to the transmembrane molecule MIG-13 to
RT promote anterior neuroblast migration.";
RL G3 (Bethesda) 5:1567-1574(2015).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate (By
CC similarity). Required for correct mitotic spindle orientation of the
CC ABar blastomere division plane and this may be through modulation of
CC astral microtubule array, and in association with the wnt-signaling
CC proteins mig-5 and dsh-2 (PubMed:25344071). Involved in the migration
CC of AQR and PQR neurons, which descend from the Q neuroblasts
CC (PubMed:26022293). Promotes the axon guidance of D-type motor neurons
CC (PubMed:24066155). {ECO:0000250|UniProtKB:P49415,
CC ECO:0000269|PubMed:24066155, ECO:0000269|PubMed:25344071,
CC ECO:0000269|PubMed:26022293}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25344071}; Single-
CC pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000269|PubMed:25344071}. Cell junction
CC {ECO:0000269|PubMed:25344071}. Cytoplasm {ECO:0000269|PubMed:25344071}.
CC Note=Initially localizes to the ABar blastomere cell surface during
CC interphase and prophase, and is internalized during metaphase and
CC anaphase. {ECO:0000269|PubMed:25344071}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the one-cell stage of embryogenesis
CC onwards. {ECO:0000269|PubMed:25344071}.
CC -!- DOMAIN: The cytoplasmic domain is required for correct mitotic spindle
CC orientation and internalization of sdn-1.
CC {ECO:0000269|PubMed:25344071}.
CC -!- DISRUPTION PHENOTYPE: Disrupted mitotic spindle orientation of the ABar
CC blastomere division axis, orientating parallel rather than orthogonally
CC to the division axis of AB derived cells ABpr and ABal
CC (PubMed:25344071). Reduced mig-5 accumulation at the cell contact sites
CC between the ABar and C blastomere cells (PubMed:25344071). Irregular
CC positioning of the AQR and PQR neurons in larva at the L4 stage
CC (PubMed:26022293). {ECO:0000269|PubMed:25344071,
CC ECO:0000269|PubMed:26022293}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; BX284606; CAA93474.1; -; Genomic_DNA.
DR PIR; T22846; T22846.
DR RefSeq; NP_741894.1; NM_171972.4.
DR AlphaFoldDB; P50605; -.
DR BioGRID; 46171; 1.
DR ELM; P50605; -.
DR STRING; 6239.F57C7.3a; -.
DR iPTMnet; P50605; -.
DR PaxDb; P50605; -.
DR PeptideAtlas; P50605; -.
DR EnsemblMetazoa; F57C7.3a.1; F57C7.3a.1; WBGene00004749.
DR GeneID; 181259; -.
DR UCSC; F57C7.3a; c. elegans.
DR CTD; 181259; -.
DR WormBase; F57C7.3a; CE05996; WBGene00004749; sdn-1.
DR eggNOG; ENOG502RZ6V; Eukaryota.
DR InParanoid; P50605; -.
DR OMA; FHETMTN; -.
DR OrthoDB; 1476863at2759; -.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR Reactome; R-CEL-2024096; HS-GAG degradation.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P50605; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004749; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P50605; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
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 PROSITE; PS00964; SYNDECAN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Glycoprotein; Heparan sulfate; Membrane;
KW Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..288
FT /note="Probable syndecan"
FT /id="PRO_0000033514"
FT TOPO_DOM 27..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 67..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:25344071"
FT CARBOHYD 86
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:25344071"
FT CARBOHYD 214
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:25344071"
FT MUTAGEN 71
FT /note="S->A: Reduced heperan sulfate binding; when
FT associated with A-86 and A-214."
FT /evidence="ECO:0000269|PubMed:25344071"
FT MUTAGEN 86
FT /note="S->A: Reduced heperan sulfate binding; when
FT associated with A-71 and A-214."
FT /evidence="ECO:0000269|PubMed:25344071"
FT MUTAGEN 214
FT /note="S->A: Reduced heperan sulfate binding; when
FT associated with A-71 and A-86."
FT /evidence="ECO:0000269|PubMed:25344071"
SQ SEQUENCE 288 AA; 30979 MW; 10F14F118541341F CRC64;
MILKLNFCLS TYSVLILLSL STQAFAANQA KTKVVPSSTI STKSLKNGIS EQVEGSANIP
GRLADIEVNG SGYPTDDEDG DDVHGSGKPP SSATTKSDKV TSPSHAVVTA KPTTVPTTTA
SFKPPVQPKP KPAANDKEIK VEEDEDDDED EDEDDEDDEE DFADENIHND EDFFTTTTTT
TYRPIVVATT STPRSAATNP PRQQPPMVTS TISSGPFSPF HETLANGFYA AIAGGVLVAV
ITAILLVLFV VFRIRKKDEG SYALDEPKQA RPYASYGYTK ASTKEFYA
