SDC4_HUMAN
ID SDC4_HUMAN Reviewed; 198 AA.
AC P31431; O00773; Q16833; Q53FN9; Q6FGN3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Syndecan-4;
DE Short=SYND4;
DE AltName: Full=Amphiglycan;
DE AltName: Full=Ryudocan core protein;
DE Flags: Precursor;
GN Name=SDC4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP LEU-12.
RC TISSUE=Lung fibroblast;
RX PubMed=1500433; DOI=10.1083/jcb.118.4.961;
RA David G., van der Schueren B., Marynen P., Cassiman J.-J.,
RA van den Berghe H.;
RT "Molecular cloning of amphiglycan, a novel integral membrane heparan
RT sulfate proteoglycan expressed by epithelial and fibroblastic cells.";
RL J. Cell Biol. 118:961-969(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7916598; DOI=10.1006/bbrc.1993.1122;
RA Kojima T., Inazawa J., Takamatsu J., Rosenberg R.D., Saito H.;
RT "Human ryudocan core protein: molecular cloning and characterization of the
RT cDNA, and chromosomal localization of the gene.";
RL Biochem. Biophys. Res. Commun. 190:814-822(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8797100; DOI=10.1093/oxfordjournals.jbchem.a021338;
RA Takagi A., Kojima T., Tsuzuki S., Katsumi A., Yamazaki T., Sugiura I.,
RA Hamaguchi M., Saito H.;
RT "Structural organization and promoter activity of the human ryudocan
RT gene.";
RL J. Biochem. 119:979-984(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-12.
RC TISSUE=Stomach;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-153 (ISOFORM 2).
RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L.,
RA Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A.,
RA Wohldmann P., Wilson R.;
RT "The WashU-Merck EST project.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-153 (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=8889549; DOI=10.1101/gr.6.9.807;
RA Hillier L.D., Lennon G., Becker M., Bonaldo M.F., Chiapelli B., Chissoe S.,
RA Dietrich N., DuBuque T., Favello A., Gish W., Hawkins M., Hultman M.,
RA Kucaba T., Lacy M., Le M., Le N., Mardis E., Moore B., Morris M.,
RA Parsons J., Prange C., Rifkin L., Rohlfing T., Schellenberg K.,
RA Bento Soares M., Tan F., Thierry-Meg J., Trevaskis E., Underwood K.,
RA Wohldman P., Waterston R., Wilson R., Marra M.;
RT "Generation and analysis of 280,000 human expressed sequence tags.";
RL Genome Res. 6:807-828(1996).
RN [12]
RP SHEDDING, AND SUBCELLULAR LOCATION.
RX PubMed=9169435; DOI=10.1074/jbc.272.23.14713;
RA Subramanian S.V., Fitzgerald M.L., Bernfield M.;
RT "Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth
RT factor receptor activation.";
RL J. Biol. Chem. 272:14713-14720(1997).
RN [13]
RP ALTERNATIVE SPLICING (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=14675776; DOI=10.1016/s0014-5793(03)01354-1;
RA Xing Y., Xu Q., Lee C.;
RT "Widespread production of novel soluble protein isoforms by alternative
RT splicing removal of transmembrane anchoring domains.";
RL FEBS Lett. 555:572-578(2003).
RN [14]
RP INTERACTION WITH CDCP1.
RX PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL Oncogene 24:5333-5343(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP STRUCTURE BY NMR OF 171-198.
RX PubMed=11456484; DOI=10.1021/bi002750r;
RA Shin J., Lee W., Lee D., Koo B.-K., Han I., Lim Y., Woods A.,
RA Couchman J.R., Oh E.-S.;
RT "Solution structure of the dimeric cytoplasmic domain of syndecan-4.";
RL Biochemistry 40:8471-8478(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 193-198 IN COMPLEX WITH SDCBP.
RX PubMed=12842047; DOI=10.1016/s0969-2126(03)00125-4;
RA Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.;
RT "Molecular roots of degenerate specificity in syntenin's PDZ2 domain:
RT reassessment of the PDZ recognition paradigm.";
RL Structure 11:845-853(2003).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 182-198 IN COMPLEX WITH SDCBP.
RX PubMed=16533050; DOI=10.1021/bi052225y;
RA Grembecka J., Cierpicki T., Devedjiev Y., Derewenda U., Kang B.S.,
RA Bushweller J.H., Derewenda Z.S.;
RT "The binding of the PDZ tandem of syntenin to target proteins.";
RL Biochemistry 45:3674-3683(2006).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Regulates exosome biogenesis in concert with SDCBP and PDCD6IP
CC (PubMed:22660413). {ECO:0000269|PubMed:22660413}.
CC -!- SUBUNIT: Homodimer. Interacts (via its cytoplasmic domain) with GIPC
CC (via its PDZ domain). Interacts (via its cytoplasmic domain) with
CC NUDT16L1 (By similarity). Interacts with CDCP1 and SDCBP.
CC {ECO:0000250|UniProtKB:O35988, ECO:0000269|PubMed:12842047,
CC ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16533050}.
CC -!- INTERACTION:
CC P31431; Q6PRD1: GPR179; NbExp=2; IntAct=EBI-3913237, EBI-20895185;
CC P31431; P16871: IL7R; NbExp=3; IntAct=EBI-3913237, EBI-80490;
CC P31431; P21145: MAL; NbExp=3; IntAct=EBI-3913237, EBI-3932027;
CC P31431; Q01453: PMP22; NbExp=3; IntAct=EBI-3913237, EBI-2845982;
CC P31431; P17252: PRKCA; NbExp=2; IntAct=EBI-3913237, EBI-1383528;
CC P31431; P34741: SDC2; NbExp=2; IntAct=EBI-3913237, EBI-1172957;
CC P31431; O75056: SDC3; NbExp=2; IntAct=EBI-3913237, EBI-1642090;
CC P31431; P31431: SDC4; NbExp=3; IntAct=EBI-3913237, EBI-3913237;
CC P31431; O43765: SGTA; NbExp=6; IntAct=EBI-3913237, EBI-347996;
CC P31431; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-3913237, EBI-744081;
CC P31431; Q8C419: Gpr158; Xeno; NbExp=3; IntAct=EBI-3913237, EBI-776313;
CC P31431; P0DTC2: S; Xeno; NbExp=17; IntAct=EBI-3913237, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass
CC type I membrane protein {ECO:0000255}. Secreted
CC {ECO:0000269|PubMed:9169435}. Note=Shedding of the ectodomain produces
CC a soluble form. {ECO:0000269|PubMed:9169435}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31431-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31431-2; Sequence=VSP_044449;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial and fibroblastic cells.
CC {ECO:0000269|PubMed:1500433}.
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. {ECO:0000269|PubMed:9169435}.
CC -!- MISCELLANEOUS: [Isoform 2]: Soluble form, lacks the transmembrane
CC domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; X67016; CAA47406.1; -; mRNA.
DR EMBL; D13292; BAA02550.1; -; mRNA.
DR EMBL; D79206; BAA19613.1; -; Genomic_DNA.
DR EMBL; AK312507; BAG35408.1; -; mRNA.
DR EMBL; CR542045; CAG46842.1; -; mRNA.
DR EMBL; CR542074; CAG46871.1; -; mRNA.
DR EMBL; AK222695; BAD96415.1; -; mRNA.
DR EMBL; AK223243; BAD96963.1; -; mRNA.
DR EMBL; AL021578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75861.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75862.1; -; Genomic_DNA.
DR EMBL; BC030805; AAH30805.1; -; mRNA.
DR EMBL; AA151028; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AA258502; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13350.1; -. [P31431-1]
DR PIR; JC1457; JC1457.
DR RefSeq; NP_002990.2; NM_002999.3. [P31431-1]
DR PDB; 1EJP; NMR; -; A/B=171-198.
DR PDB; 1EJQ; NMR; -; A/B=171-198.
DR PDB; 1OBY; X-ray; 1.85 A; P/Q=193-198.
DR PDB; 1YBO; X-ray; 2.30 A; C/D=182-198.
DR PDBsum; 1EJP; -.
DR PDBsum; 1EJQ; -.
DR PDBsum; 1OBY; -.
DR PDBsum; 1YBO; -.
DR AlphaFoldDB; P31431; -.
DR BMRB; P31431; -.
DR SASBDB; P31431; -.
DR SMR; P31431; -.
DR BioGRID; 112286; 81.
DR CORUM; P31431; -.
DR DIP; DIP-29945N; -.
DR ELM; P31431; -.
DR IntAct; P31431; 30.
DR MINT; P31431; -.
DR STRING; 9606.ENSP00000361818; -.
DR TCDB; 9.A.35.1.1; the peptide translocating syndecan (syndecan) family.
DR GlyGen; P31431; 5 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P31431; -.
DR PhosphoSitePlus; P31431; -.
DR BioMuta; SDC4; -.
DR DMDM; 2851418; -.
DR EPD; P31431; -.
DR jPOST; P31431; -.
DR MassIVE; P31431; -.
DR MaxQB; P31431; -.
DR PaxDb; P31431; -.
DR PeptideAtlas; P31431; -.
DR PRIDE; P31431; -.
DR ProteomicsDB; 54789; -. [P31431-1]
DR TopDownProteomics; P31431-1; -. [P31431-1]
DR Antibodypedia; 969; 505 antibodies from 40 providers.
DR DNASU; 6385; -.
DR Ensembl; ENST00000372733.3; ENSP00000361818.3; ENSG00000124145.6. [P31431-1]
DR GeneID; 6385; -.
DR KEGG; hsa:6385; -.
DR MANE-Select; ENST00000372733.3; ENSP00000361818.3; NM_002999.4; NP_002990.2.
DR UCSC; uc002xnu.4; human. [P31431-1]
DR CTD; 6385; -.
DR DisGeNET; 6385; -.
DR GeneCards; SDC4; -.
DR HGNC; HGNC:10661; SDC4.
DR HPA; ENSG00000124145; Tissue enhanced (liver).
DR MIM; 600017; gene.
DR neXtProt; NX_P31431; -.
DR OpenTargets; ENSG00000124145; -.
DR PharmGKB; PA35591; -.
DR VEuPathDB; HostDB:ENSG00000124145; -.
DR eggNOG; ENOG502S1SZ; Eukaryota.
DR GeneTree; ENSGT00940000160663; -.
DR HOGENOM; CLU_046599_3_0_1; -.
DR InParanoid; P31431; -.
DR OMA; GSWVPTE; -.
DR OrthoDB; 1507361at2759; -.
DR PhylomeDB; P31431; -.
DR TreeFam; TF320463; -.
DR PathwayCommons; P31431; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P31431; -.
DR SIGNOR; P31431; -.
DR BioGRID-ORCS; 6385; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; SDC4; human.
DR EvolutionaryTrace; P31431; -.
DR GeneWiki; SDC4; -.
DR GenomeRNAi; 6385; -.
DR Pharos; P31431; Tbio.
DR PRO; PR:P31431; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P31431; protein.
DR Bgee; ENSG00000124145; Expressed in olfactory segment of nasal mucosa and 204 other tissues.
DR Genevisible; P31431; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0070053; F:thrombospondin receptor activity; IMP:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR DisProt; DP01434; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein; Heparan sulfate;
KW Membrane; Proteoglycan; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..198
FT /note="Syndecan-4"
FT /id="PRO_0000033511"
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"
FT VAR_SEQ 149..198
FT /note="ALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA
FT -> GCPEH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8889549, ECO:0000303|Ref.10"
FT /id="VSP_044449"
FT VARIANT 12
FT /note="F -> L (in dbSNP:rs2228384)"
FT /evidence="ECO:0000269|PubMed:1500433, ECO:0000269|Ref.6"
FT /id="VAR_021851"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1EJQ"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1OBY"
SQ SEQUENCE 198 AA; 21642 MW; 8229AA2733F77A10 CRC64;
MAPARLFALL LFFVGGVAES IRETEVIDPQ DLLEGRYFSG ALPDDEDVVG PGQESDDFEL
SGSGDLDDLE DSMIGPEVVH PLVPLDNHIP ERAGSGSQVP TEPKKLEENE VIPKRISPVE
ESEDVSNKVS MSSTVQGSNI FERTEVLAAL IVGGIVGILF AVFLILLLMY RMKKKDEGSY
DLGKKPIYKK APTNEFYA
