ID   SDC4_PONAB              Reviewed;         198 AA.
AC   Q5RAT9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Syndecan-4;
DE            Short=SYND4;
DE   Flags: Precursor;
GN   Name=SDC4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC       Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
CC       {ECO:0000250|UniProtKB:P31431}.
CC   -!- SUBUNIT: Homodimer. Interacts with CDCP1 and SDCBP. Interacts (via its
CC       cytoplasmic domain) with GIPC (via its PDZ domain). Interacts (via its
CC       cytoplasmic domain) with NUDT16L1 (By similarity).
CC       {ECO:0000250|UniProtKB:O35988, ECO:0000250|UniProtKB:P31431}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}. Secreted
CC       {ECO:0000250|UniProtKB:P31431}. Note=Shedding of the ectodomain
CC       produces a soluble form. {ECO:0000250|UniProtKB:P31431}.
CC   -!- PTM: Shedding is enhanced by a number of factors such as heparanase,
CC       thrombin or EGF. Also by stress and wound healing. PMA-mediated
CC       shedding is inhibited by TIMP3 (By similarity).
CC       {ECO:0000250|UniProtKB:P31431}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR   EMBL; CR858923; CAH91121.1; -; mRNA.
DR   RefSeq; NP_001127378.1; NM_001133906.1.
DR   RefSeq; XP_009231914.1; XM_009233639.1.
DR   AlphaFoldDB; Q5RAT9; -.
DR   BMRB; Q5RAT9; -.
DR   SMR; Q5RAT9; -.
DR   STRING; 9601.ENSPPYP00000012352; -.
DR   Ensembl; ENSPPYT00000040026; ENSPPYP00000034832; ENSPPYG00000038657.
DR   GeneID; 100174444; -.
DR   KEGG; pon:100174444; -.
DR   CTD; 6385; -.
DR   eggNOG; ENOG502S1SZ; Eukaryota.
DR   GeneTree; ENSGT00940000160663; -.
DR   HOGENOM; CLU_046599_3_0_1; -.
DR   InParanoid; Q5RAT9; -.
DR   OMA; GSWVPTE; -.
DR   OrthoDB; 1507361at2759; -.
DR   TreeFam; TF320463; -.
DR   Proteomes; UP000001595; Chromosome 20.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   InterPro; IPR030479; Syndecan_CS.
DR   PANTHER; PTHR10915; PTHR10915; 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   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..198
FT                   /note="Syndecan-4"
FT                   /id="PRO_0000329297"
FT   TOPO_DOM        19..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   198 AA;  21618 MW;  688488B14BD45EEE CRC64;
     MAPARLFALL LLFVGGVAES IRETEVIDPQ DLLEGRYFSG ALPDDEDVVG PGQESDDFEL
     SGSGDLDDLE DSIIGPEVIH PLVPLDNHIP ERAGSGSQVP TEPKKLEENE VIPKRISPIE
     ESEDVSNKVS MSSTVQGSNI FERTEVLAAL IVGGIVGILF AVFLILLLMY RMKKKDEGSY
     DLGKKPIYKK APTNEFYA