SDC3_CHICK
ID SDC3_CHICK Reviewed; 405 AA.
AC P26261;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Syndecan-3;
DE Flags: Precursor;
GN Name=SDC3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Limb bud;
RX PubMed=7729580; DOI=10.1006/dbio.1995.1093;
RA Gould S.E., Upholt W.B., Kosher R.A.;
RT "Characterization of chicken syndecan-3 as a heparan sulfate proteoglycan
RT and its expression during embryogenesis.";
RL Dev. Biol. 168:438-451(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-405.
RC TISSUE=Limb bud;
RX PubMed=1565618; DOI=10.1073/pnas.89.8.3271;
RA Gould S.E., Upholt W.B., Kosher R.A.;
RT "Syndecan 3: a member of the syndecan family of membrane-intercalated
RT proteoglycans that is expressed in high amounts at the onset of chicken
RT limb cartilage differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3271-3275(1992).
CC -!- FUNCTION: Cell surface proteoglycan that may bear both heparan sulfate
CC and chondroitin sulfate. The multiple functional domains provide
CC potential sites for mediating the adhesive cell-matrix interactions and
CC cytoskeletal reorganization involved in limb chondrogenesis.
CC Interaction with other matrix ligands as well as phosphorylation and
CC shedding of the ectodomain might be involved in cell shape changes that
CC occur during chondrogenesis. Furthermore, shedding of the ectodomain
CC might break the adhesive interactions that promoted condensation, thus
CC facilitating the deposition of cartilage matrix molecules.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Proximal chondrogenic central core of embryonic
CC limb buds where cartilage differentiation is being initiated.
CC -!- DEVELOPMENTAL STAGE: Expressed in high amounts at the onset of limb
CC cartilage differentiation.
CC -!- PTM: O-glycosylated within the Thr/Ser-rich region which could interact
CC with lectin domains on other molecules. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; M84910; AAA82104.1; -; mRNA.
DR PIR; A44146; A44146.
DR RefSeq; NP_990714.1; NM_205383.1.
DR AlphaFoldDB; P26261; -.
DR SMR; P26261; -.
DR STRING; 9031.ENSGALP00000000792; -.
DR PaxDb; P26261; -.
DR GeneID; 396343; -.
DR KEGG; gga:396343; -.
DR CTD; 9672; -.
DR VEuPathDB; HostDB:geneid_396343; -.
DR eggNOG; ENOG502QTD2; Eukaryota.
DR InParanoid; P26261; -.
DR OrthoDB; 1340825at2759; -.
DR PhylomeDB; P26261; -.
DR PRO; PR:P26261; -.
DR Proteomes; UP000000539; Unplaced.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; TAS:AgBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0035988; P:chondrocyte proliferation; IMP:AgBase.
DR GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; TAS:AgBase.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:AgBase.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR031194; Syndecan-3.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF7; PTHR10915:SF7; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Glycoprotein; Heparan sulfate;
KW Membrane; Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..405
FT /note="Syndecan-3"
FT /id="PRO_0000033507"
FT TOPO_DOM 23..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 346..347
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 43069 MW; 21AF5DD393B8F7AC CRC64;
MPAELRRLAV LLLLLSARAA LAQPWRNENY ERPVDLEGSG DDDPFGDDEL DDIYSGSGSG
YFEQESGLET AVSLTTDTSV PLPTTVAVLP VTLVQPMATP FELFPTEDTS PEQTTSVLYI
PKITEAPVIP SWKTTTASTT ASDSPSTTST TTTTAATTTT TTTTISTTVA TSKPTTTQRF
LPPFVTKAAT TRATTLETPT TSIPETSVLT EVTTSRLVPS STAKPRSLPK PSTSRTAEPT
EKSTALPSSP TTLPPTEAPQ VEPGELTTVL DSDLEVPTSS GPSGDFEIQE EEETTRPELG
NEVVAVVTPP AAPGLGKNAE PGLIDNTIES GSSAAQLPQK NILERKEVLI AVIVGGVVGA
LFAAFLVMLL IYRMKKKDEG SYTLEEPKQA NVTYQKPDKQ EEFYA
