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Protein

Syndecan-2

Gene

Sdc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-MMU-2022928. HS-GAG biosynthesis.
R-MMU-2024096. HS-GAG degradation.
R-MMU-3000170. Syndecan interactions.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Syndecan-2
Short name:
SYND2
Alternative name(s):
Fibroglycan
Heparan sulfate proteoglycan core protein
Short name:
HSPG
CD_antigen: CD362
Gene namesi
Name:Sdc2
Synonyms:Hspg1, Synd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1349165. Sdc2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 145127ExtracellularSequence analysisAdd
BLAST
Transmembranei146 – 17025HelicalSequence analysisAdd
BLAST
Topological domaini171 – 20232CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 202184Syndecan-2PRO_0000033504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi55 – 551O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi57 – 571O-linked (Xyl...) (heparan sulfate)Sequence analysis
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei143 – 1442Cleavage of ectodomainSequence analysis

Keywords - PTMi

Glycoprotein, Heparan sulfate, Phosphoprotein, Proteoglycan

Proteomic databases

MaxQBiP43407.
PaxDbiP43407.
PeptideAtlasiP43407.
PRIDEiP43407.

PTM databases

iPTMnetiP43407.
PhosphoSiteiP43407.

Expressioni

Tissue specificityi

Preferential expression in cells of mesenchymal origin.

Gene expression databases

BgeeiP43407.
CleanExiMM_SDC2.
GenevisibleiP43407. MM.

Interactioni

Subunit structurei

Interacts (via cytoplasmic domain) with SARM1 (PubMed:21555464). Forms a complex with SDCBP and PDCD6IP (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022871.

Structurei

3D structure databases

ProteinModelPortaliP43407.
SMRiP43407. Positions 171-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the syndecan proteoglycan family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IW5I. Eukaryota.
ENOG4111QSA. LUCA.
GeneTreeiENSGT00530000063116.
HOGENOMiHOG000263414.
HOVERGENiHBG004501.
InParanoidiP43407.
KOiK16336.
OMAiASASGSX.
OrthoDBiEOG7GJ6G5.
PhylomeDBiP43407.
TreeFamiTF320463.

Family and domain databases

InterProiIPR003585. Neurexin-like.
IPR001050. Syndecan.
IPR031201. Syndecan-2.
IPR027789. Syndecan/Neurexin_dom.
IPR030479. Syndecan_CS.
[Graphical view]
PANTHERiPTHR10915. PTHR10915. 1 hit.
PTHR10915:SF6. PTHR10915:SF6. 1 hit.
PfamiPF01034. Syndecan. 1 hit.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
[Graphical view]
PROSITEiPS00964. SYNDECAN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43407-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRAWILLTL GLMACVSAET RTELTSDKDM YLDNSSIEEA SGVYPIDDDD
60 70 80 90 100
YSSASGSGAD EDIESPVLTT SQLIPRIPLT SAASPKVETM TLKTQSITPA
110 120 130 140 150
QTESPEETDK EEVDISEAEE KLGPAIKSTD VYTEKHSDNL FKRTEVLAAV
160 170 180 190 200
IAGGVIGFLF AIFLILLLVY RMRKKDEGSY DLGERKPSSA AYQKAPTKEF

YA
Length:202
Mass (Da):22,131
Last modified:November 1, 1995 - v1
Checksum:iC213D1B64D88376F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00674 mRNA. Translation: AAA17781.1.
AK011042 mRNA. Translation: BAB27354.1.
BC047144 mRNA. Translation: AAH47144.1.
CCDSiCCDS27413.1.
PIRiI53137.
RefSeqiNP_032330.1. NM_008304.2.
UniGeneiMm.234266.

Genome annotation databases

EnsembliENSMUST00000022871; ENSMUSP00000022871; ENSMUSG00000022261.
GeneIDi15529.
KEGGimmu:15529.
UCSCiuc007vkx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00674 mRNA. Translation: AAA17781.1.
AK011042 mRNA. Translation: BAB27354.1.
BC047144 mRNA. Translation: AAH47144.1.
CCDSiCCDS27413.1.
PIRiI53137.
RefSeqiNP_032330.1. NM_008304.2.
UniGeneiMm.234266.

3D structure databases

ProteinModelPortaliP43407.
SMRiP43407. Positions 171-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022871.

PTM databases

iPTMnetiP43407.
PhosphoSiteiP43407.

Proteomic databases

MaxQBiP43407.
PaxDbiP43407.
PeptideAtlasiP43407.
PRIDEiP43407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022871; ENSMUSP00000022871; ENSMUSG00000022261.
GeneIDi15529.
KEGGimmu:15529.
UCSCiuc007vkx.1. mouse.

Organism-specific databases

CTDi6383.
MGIiMGI:1349165. Sdc2.

Phylogenomic databases

eggNOGiENOG410IW5I. Eukaryota.
ENOG4111QSA. LUCA.
GeneTreeiENSGT00530000063116.
HOGENOMiHOG000263414.
HOVERGENiHBG004501.
InParanoidiP43407.
KOiK16336.
OMAiASASGSX.
OrthoDBiEOG7GJ6G5.
PhylomeDBiP43407.
TreeFamiTF320463.

Enzyme and pathway databases

ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-MMU-2022928. HS-GAG biosynthesis.
R-MMU-2024096. HS-GAG degradation.
R-MMU-3000170. Syndecan interactions.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiSdc2. mouse.
PROiP43407.
SOURCEiSearch...

Gene expression databases

BgeeiP43407.
CleanExiMM_SDC2.
GenevisibleiP43407. MM.

Family and domain databases

InterProiIPR003585. Neurexin-like.
IPR001050. Syndecan.
IPR031201. Syndecan-2.
IPR027789. Syndecan/Neurexin_dom.
IPR030479. Syndecan_CS.
[Graphical view]
PANTHERiPTHR10915. PTHR10915. 1 hit.
PTHR10915:SF6. PTHR10915:SF6. 1 hit.
PfamiPF01034. Syndecan. 1 hit.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
[Graphical view]
PROSITEiPS00964. SYNDECAN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Spatial and temporal changes in the expression of fibroglycan (syndecan-2) during mouse embryonic development."
    David G.J., Bai X.M., van der Schueren B., Marynen P., Cassiman J.-J., van den Berghe H.
    Development 119:841-854(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  4. "Sarm1, a negative regulator of innate immunity, interacts with syndecan-2 and regulates neuronal morphology."
    Chen C.Y., Lin C.W., Chang C.Y., Jiang S.T., Hsueh Y.P.
    J. Cell Biol. 193:769-784(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SARM1.

Entry informationi

Entry nameiSDC2_MOUSE
AccessioniPrimary (citable) accession number: P43407
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.