SDC3_MOUSE
ID SDC3_MOUSE Reviewed; 442 AA.
AC Q64519; Q3UDD9; Q6ZQA4; Q7TQD4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Syndecan-3;
DE Short=SYND3;
DE Flags: Precursor;
GN Name=Sdc3; Synonyms=Kiaa0468;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA;
RA Kung C.E., Deuel T.F.;
RT "Cloning of rat and mouse syndecan-3 cDNAs.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP INTERACTION WITH MDK.
RX PubMed=12084985; DOI=10.1023/a:1016042303253;
RA Kurosawa N., Chen G.Y., Kadomatsu K., Ikematsu S., Sakuma S., Muramatsu T.;
RT "Glypican-2 binds to midkine: the role of glypican-2 in neuronal cell
RT adhesion and neurite outgrowth.";
RL Glycoconj. J. 18:499-507(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cell surface proteoglycan that may bear heparan sulfate. May
CC have a role in the organization of cell shape by affecting the actin
CC cytoskeleton, possibly by transferring signals from the cell surface in
CC a sugar-dependent mechanism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TIAM1 (By similarity). Interacts with PTN (via
CC heparan sulfate chains); this interaction mediates the neurite
CC outgrowth-promoting signal from PTN to the cytoskeleton of growing
CC neurites; this interaction mediates osteoblast recruitment (By
CC similarity). Interacts with MDK; this interaction induces SDC3
CC clustering; this interaction induces neuronal cell adhesion and neurite
CC outgrowth (PubMed:12084985). {ECO:0000250,
CC ECO:0000250|UniProtKB:O75056, ECO:0000250|UniProtKB:P33671,
CC ECO:0000269|PubMed:12084985}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
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; U52826; AAB03283.1; -; mRNA.
DR EMBL; AK129153; BAC97963.1; -; mRNA.
DR EMBL; AK150120; BAE29322.1; -; mRNA.
DR EMBL; AK155127; BAE33064.1; -; mRNA.
DR EMBL; BC054795; AAH54795.1; -; mRNA.
DR EMBL; BC062093; AAH62093.1; -; mRNA.
DR CCDS; CCDS38894.1; -.
DR RefSeq; NP_035650.2; NM_011520.3.
DR AlphaFoldDB; Q64519; -.
DR IntAct; Q64519; 1.
DR STRING; 10090.ENSMUSP00000065877; -.
DR GlyGen; Q64519; 6 sites.
DR iPTMnet; Q64519; -.
DR PhosphoSitePlus; Q64519; -.
DR MaxQB; Q64519; -.
DR PaxDb; Q64519; -.
DR PeptideAtlas; Q64519; -.
DR PRIDE; Q64519; -.
DR ProteomicsDB; 256757; -.
DR Antibodypedia; 1502; 229 antibodies from 31 providers.
DR DNASU; 20970; -.
DR Ensembl; ENSMUST00000070478; ENSMUSP00000065877; ENSMUSG00000025743.
DR GeneID; 20970; -.
DR KEGG; mmu:20970; -.
DR UCSC; uc008uzr.1; mouse.
DR CTD; 9672; -.
DR MGI; MGI:1349163; Sdc3.
DR VEuPathDB; HostDB:ENSMUSG00000025743; -.
DR eggNOG; ENOG502QTD2; Eukaryota.
DR GeneTree; ENSGT00940000160209; -.
DR HOGENOM; CLU_047258_0_0_1; -.
DR InParanoid; Q64519; -.
DR OMA; MKPGPPH; -.
DR OrthoDB; 1340825at2759; -.
DR PhylomeDB; Q64519; -.
DR TreeFam; TF320463; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 20970; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Sdc3; mouse.
DR PRO; PR:Q64519; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64519; protein.
DR Bgee; ENSMUSG00000025743; Expressed in humerus cartilage element and 241 other tissues.
DR ExpressionAtlas; Q64519; baseline and differential.
DR Genevisible; Q64519; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0044393; C:microspike; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein;
KW Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..442
FT /note="Syndecan-3"
FT /id="PRO_0000033508"
FT TOPO_DOM 45..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 383..384
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 419
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 78
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 161
FT /note="O-linked (GalNAc) serine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 162
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 163
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 170
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 172
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000250|UniProtKB:O75056"
FT CARBOHYD 315
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CONFLICT 133
FT /note="S -> R (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="T -> K (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="RA -> QS (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="V -> I (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> E (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="M -> V (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="I -> T (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="P -> L (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="P -> L (in Ref. 1; AAB03283)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="V -> D (in Ref. 4; BAE29322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 46002 MW; E8FF8B90C5F0706B CRC64;
MKPGPPRRGT AQGQRVDTAT HAPGARGLLL PPLLLLLLAG RAAGAQRWRN ENFERPVDLE
GSGDDDSFPD DELDDLYSGS GSGYFEQESG LETAMRFIPD MALAAPTAPA MLPTTVIQPV
DTPFEELLSE HPSPEPVTSP PLVTEVTEVV EESSQKATTI STTTSTTAAT TTGAPTMATA
PATAATTAPS TPEAPPATAT VADVRTTGIQ GMLPLPLTTA ATAKITTPAA PSPPTTVATL
DTEAPTPRLV NTATSRPRAL PRPVTTQEPD VAERSTLPLG TTAPGPTEMA QTPTPESLLT
TIQDEPEVPV SGGPSGDFEL QEETTQPDTA NEVVAVEGAA AKPSPPLGTL PKGARPGPGL
HDNAIDSGSS AAQLPQKSIL ERKEVLVAVI VGGVVGALFA AFLVTLLIYR MKKKDEGSYT
LEEPKQASVT YQKPDKQEEF YA
