SDC2_MOUSE
ID SDC2_MOUSE Reviewed; 202 AA.
AC P43407;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Syndecan-2;
DE Short=SYND2;
DE AltName: Full=Fibroglycan;
DE AltName: Full=Heparan sulfate proteoglycan core protein;
DE Short=HSPG;
DE AltName: CD_antigen=CD362;
DE Flags: Precursor;
GN Name=Sdc2; Synonyms=Hspg1, Synd2;
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 TISSUE=Embryo;
RX PubMed=8187643; DOI=10.1242/dev.119.3.841;
RA David G.J., Bai X.M., van der Schueren B., Marynen P., Cassiman J.-J.,
RA van den Berghe H.;
RT "Spatial and temporal changes in the expression of fibroglycan (syndecan-2)
RT during mouse embryonic development.";
RL Development 119:841-854(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP FUNCTION, AND INTERACTION WITH SARM1.
RX PubMed=21555464; DOI=10.1083/jcb.201008050;
RA Chen C.Y., Lin C.W., Chang C.Y., Jiang S.T., Hsueh Y.P.;
RT "Sarm1, a negative regulator of innate immunity, interacts with syndecan-2
RT and regulates neuronal morphology.";
RL J. Cell Biol. 193:769-784(2011).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Regulates dendritic arbor morphogenesis. {ECO:0000269|PubMed:21555464}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with SARM1
CC (PubMed:21555464). Forms a complex with SDCBP and PDCD6IP (By
CC similarity). {ECO:0000250|UniProtKB:P34741,
CC ECO:0000269|PubMed:21555464}.
CC -!- INTERACTION:
CC P43407; Q15113: PCOLCE; Xeno; NbExp=4; IntAct=EBI-11578890, EBI-8869614;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Preferential expression in cells of mesenchymal
CC origin.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00674; AAA17781.1; -; mRNA.
DR EMBL; AK011042; BAB27354.1; -; mRNA.
DR EMBL; BC047144; AAH47144.1; -; mRNA.
DR CCDS; CCDS27413.1; -.
DR PIR; I53137; I53137.
DR RefSeq; NP_032330.1; NM_008304.2.
DR AlphaFoldDB; P43407; -.
DR SMR; P43407; -.
DR CORUM; P43407; -.
DR IntAct; P43407; 1.
DR STRING; 10090.ENSMUSP00000022871; -.
DR GlyGen; P43407; 3 sites.
DR iPTMnet; P43407; -.
DR PhosphoSitePlus; P43407; -.
DR MaxQB; P43407; -.
DR PaxDb; P43407; -.
DR PeptideAtlas; P43407; -.
DR PRIDE; P43407; -.
DR ProteomicsDB; 256718; -.
DR Antibodypedia; 25987; 288 antibodies from 31 providers.
DR DNASU; 15529; -.
DR Ensembl; ENSMUST00000022871; ENSMUSP00000022871; ENSMUSG00000022261.
DR GeneID; 15529; -.
DR KEGG; mmu:15529; -.
DR UCSC; uc007vkx.1; mouse.
DR CTD; 6383; -.
DR MGI; MGI:1349165; Sdc2.
DR VEuPathDB; HostDB:ENSMUSG00000022261; -.
DR eggNOG; ENOG502RZ6V; Eukaryota.
DR GeneTree; ENSGT00940000157222; -.
DR HOGENOM; CLU_046599_2_1_1; -.
DR InParanoid; P43407; -.
DR OMA; ASASGSX; -.
DR OrthoDB; 1362808at2759; -.
DR PhylomeDB; P43407; -.
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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 15529; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Sdc2; mouse.
DR PRO; PR:P43407; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P43407; protein.
DR Bgee; ENSMUSG00000022261; Expressed in epithelium of lens and 252 other tissues.
DR Genevisible; P43407; MM.
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:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Differentiation; Glycoprotein; Heparan sulfate; Membrane; Neurogenesis;
KW Phosphoprotein; Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..202
FT /note="Syndecan-2"
FT /id="PRO_0000033504"
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..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 143..144
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34741"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34741"
FT CARBOHYD 41
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 202 AA; 22131 MW; C213D1B64D88376F CRC64;
MQRAWILLTL GLMACVSAET RTELTSDKDM YLDNSSIEEA SGVYPIDDDD YSSASGSGAD
EDIESPVLTT SQLIPRIPLT SAASPKVETM TLKTQSITPA QTESPEETDK EEVDISEAEE
KLGPAIKSTD VYTEKHSDNL FKRTEVLAAV IAGGVIGFLF AIFLILLLVY RMRKKDEGSY
DLGERKPSSA AYQKAPTKEF YA
