ID SDC2A_XENLA Reviewed; 191 AA.
AC P49414; O42473;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Syndecan-2-A;
DE Short=SYND2-A;
DE Flags: Precursor;
GN Name=sdc2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7619084; DOI=10.1042/bj3090069;
RA Rosenblum N.D., Botelho B.B., Bernfield M.;
RT "Expression of a Xenopus counterpart of mammalian syndecan 2 during
RT embryogenesis.";
RL Biochem. J. 309:69-76(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell surface proteoglycan.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: O-glycosylated; contains both heparan sulfate and chondroitin
CC sulfate. {ECO:0000250|UniProtKB:P43407}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; U24433; AAA87197.1; -; mRNA.
DR EMBL; BC041490; AAH41490.1; -; mRNA.
DR AlphaFoldDB; P49414; -.
DR SMR; P49414; -.
DR GlyCosmos; P49414; 4 sites, No reported glycans.
DR AGR; Xenbase:XB-GENE-6254482; -.
DR Xenbase; XB-GENE-6254482; sdc2.L.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; SYNDECAN; 1.
DR PANTHER; PTHR10915:SF6; SYNDECAN-2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heparan sulfate; Membrane; Proteoglycan; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..191
FT /note="Syndecan-2-A"
FT /id="PRO_0000033506"
FT TOPO_DOM 23..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CONFLICT 92
FT /note="Q -> L (in Ref. 1; AAA87197)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="R -> G (in Ref. 1; AAA87197)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> R (in Ref. 1; AAA87197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 20927 MW; 877A2E8BF396EFCF CRC64;
MRNVWLIVPF ALLAALSGET WAQADRDLYI DSTESSGNYP VDDDDYSSGS GSGIPARGDD
EDENVVLTTV QTLISSPSSE MPYVETTTLK TQTKMAPETK EPGEVESTNT VLVYGKKDIV
QTATHTENLF HRTEVLAAVI AGGGIGFLFA VFLILLLVYR MRKKDEGSYD LGERKPSSAV
YQKAPTKEFY A
//
