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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
 
 
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