SDC2_RAT
ID SDC2_RAT Reviewed; 201 AA.
AC P34900;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 145.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1740437; DOI=10.1016/s0021-9258(19)50610-x;
RA Pierce A., Lyon M., Hampson I., Cowling G.J., Gallagher J.;
RT "Molecular cloning of the major cell surface heparan sulfate proteoglycan
RT from rat liver.";
RL J. Biol. Chem. 267:3894-3900(1992).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Regulates dendritic arbor morphogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with SARM1. Forms a complex
CC with SDCBP and PDCD6IP. {ECO:0000250|UniProtKB:P34741,
CC ECO:0000250|UniProtKB:P43407}.
CC -!- INTERACTION:
CC P34900; P26260: Sdc1; NbExp=2; IntAct=EBI-1173032, EBI-1173127;
CC P34900; P34900: Sdc2; NbExp=2; IntAct=EBI-1173032, EBI-1173032;
CC P34900; P33671: Sdc3; NbExp=2; IntAct=EBI-1173032, EBI-1173159;
CC P34900; P34901: Sdc4; NbExp=4; IntAct=EBI-1173032, EBI-1173182;
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; M81687; AAA41355.1; -; mRNA.
DR PIR; A42261; A42261.
DR RefSeq; NP_037214.1; NM_013082.3.
DR AlphaFoldDB; P34900; -.
DR SMR; P34900; -.
DR BioGRID; 247644; 5.
DR CORUM; P34900; -.
DR IntAct; P34900; 5.
DR STRING; 10116.ENSRNOP00000007255; -.
DR GlyGen; P34900; 3 sites.
DR iPTMnet; P34900; -.
DR PhosphoSitePlus; P34900; -.
DR PaxDb; P34900; -.
DR PRIDE; P34900; -.
DR GeneID; 25615; -.
DR KEGG; rno:25615; -.
DR UCSC; RGD:3649; rat.
DR CTD; 6383; -.
DR RGD; 3649; Sdc2.
DR eggNOG; ENOG502S3JC; Eukaryota.
DR InParanoid; P34900; -.
DR OrthoDB; 1362808at2759; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR Reactome; R-RNO-2024096; HS-GAG degradation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P34900; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IEP:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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..201
FT /note="Syndecan-2"
FT /id="PRO_0000033505"
FT TOPO_DOM 19..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 42..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 142..143
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34741"
FT MOD_RES 187
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 201 AA; 22149 MW; 02E08455754C5E5A CRC64;
MQRAWILLTL GLMACVSAET RAELTSDKDM YLDSSSIEEA SGLYPIDDDD YSSASGSGAY
EDKGSPDLTT SQLIPRISLT SAAPEVETMT LKTQSITPTQ TESPEETDKK EFEISEAEEK
QDPAVKSTDV YTEKHSDNLF KRTEVLAAVI AGGVIGFLFA IFLILLLVYR MRKKDEGSYD
LGERKPSSAA YQKAPTKEFY A