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   25-MAY-2022, entry version 83.
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 that bears heparan sulfate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   InterPro; IPR031201; Syndecan-2.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   InterPro; IPR030479; Syndecan_CS.
DR   PANTHER; PTHR10915; PTHR10915; 1.
DR   PANTHER; PTHR10915:SF6; PTHR10915:SF6; 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...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        48
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="O-linked (Xyl...) (heparan sulfate) 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