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Protein

Gliomedin

Gene

Gldn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC (PubMed:16039564). Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (By similarity).By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Gliomedin1 Publication
Cleaved into the following chain:
Gliomedin shedded ectodomainBy similarity
Gene namesi
Name:Gldn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi727879. Gldn.

Subcellular locationi

Gliomedin shedded ectodomain :
  • Secreted 1 Publication
  • Secretedextracellular spaceextracellular matrix 1 Publication

  • Note: Proteolytic processing gives rise to a soluble extracellular domain that is secreted. The gliomedin shedded ectodomain localizes to the nodes of Ranvier.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence analysisAdd
BLAST
Transmembranei18 – 3821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini39 – 549511ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911R → G: Abolishes cleavage and shedding of ectodomain; when associated with A-94. 1 Publication
Mutagenesisi94 – 941R → A: Abolishes cleavage and shedding of ectodomain; when associated with G-91. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549GliomedinPRO_0000246323Add
BLAST
Chaini95 – 451357Gliomedin shedded ectodomain1 PublicationPRO_0000434267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication
Proteolytic proccessing by a furin-like protease causes shedding of the ectodomain (PubMed:17485493). Further cleavage by BMP1 releases the olfactomedin-like domain.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei94 – 952Cleavage; by furin-like protease1 Publication
Sitei277 – 2782Cleavage; by BMP1By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ80WL1.
PRIDEiQ80WL1.

Expressioni

Tissue specificityi

Detected in Schwann cells (at protein level).1 Publication

Developmental stagei

Expression increases in myelinating Schwann cells during the initial period of active myelination.1 Publication

Interactioni

Subunit structurei

Homotrimer (via collagen-like domains) (PubMed:17485493) (Probable). Interacts with NRCAM (PubMed:16039564, PubMed:22009740). Interacts with NFACS/neurofascin (PubMed:16039564, PubMed:17485493, PubMed:22009740). Interaction with glial NRCAM enhances interaction with axonal NFACS. Interacts with MYOC (By similarity).By similarity3 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029833.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi301 – 3044Combined sources
Beta strandi308 – 3125Combined sources
Beta strandi316 – 3227Combined sources
Beta strandi332 – 34817Combined sources
Helixi349 – 3535Combined sources
Beta strandi358 – 36912Combined sources
Beta strandi375 – 3828Combined sources
Beta strandi385 – 3928Combined sources
Turni393 – 3953Combined sources
Beta strandi399 – 4024Combined sources
Helixi416 – 4183Combined sources
Beta strandi423 – 4275Combined sources
Beta strandi430 – 4378Combined sources
Turni438 – 4403Combined sources
Beta strandi443 – 4508Combined sources
Turni451 – 4544Combined sources
Beta strandi455 – 46511Combined sources
Helixi466 – 4683Combined sources
Beta strandi472 – 4754Combined sources
Beta strandi478 – 4825Combined sources
Beta strandi486 – 4949Combined sources
Turni495 – 4984Combined sources
Beta strandi499 – 5013Combined sources
Beta strandi514 – 5207Combined sources
Turni521 – 5244Combined sources
Beta strandi525 – 5306Combined sources
Beta strandi533 – 5419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D77X-ray1.48A260-543[»]
4D7CX-ray1.45A/B260-543[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 19559Collagen-like 1Add
BLAST
Domaini196 – 22227Collagen-like 2Add
BLAST
Domaini296 – 543248Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi237 – 26125Pro-richAdd
BLAST

Domaini

The olfactomedin-like domain mediates NFASC/neurofascin and NRCAM binding.By similarity

Sequence similaritiesi

Contains 2 collagen-like domains.Curated
Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KCV6. Eukaryota.
ENOG4110Z7Z. LUCA.
HOGENOMiHOG000112733.
HOVERGENiHBG081557.
InParanoidiQ80WL1.
KOiK16364.
PhylomeDBiQ80WL1.

Family and domain databases

InterProiIPR008160. Collagen.
IPR031224. Gliomedin.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF5. PTHR23192:SF5. 1 hit.
PfamiPF01391. Collagen. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q80WL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRAAERGQG ATGWGLRGAL MAVALLSVLN AVGTVFVLYQ WRELSAALRA
60 70 80 90 100
LEAQHGQEQR EDSALRAFLA ELSRAPARVP EPPQDPMSAA RNKRSHGGEP
110 120 130 140 150
ASHIRAESQD MMMMMTYSMV PIRVMIDLCN STQGICLTGP PGPPGPPGAG
160 170 180 190 200
GLPGHNGSDG QPGLQGPKGE KGAVGKRGKM GLPGATGNPG EKGEKGDAGE
210 220 230 240 250
LGLPGNEGPP GQKGDKGDKG DVSNDVLLTG AKGDQGPPGP PGPPGPPGPP
260 270 280 290 300
GSRRAKGPRQ PNSFTNQCPG ETCVIPNDDT LVGRADEKVN ERHSPQTEPM
310 320 330 340 350
ITSIGNPAQV LKVKETFGTW LRESANRSDD RIWVTEHFSG IMVKEFEDLP
360 370 380 390 400
ALLNSSFTLL HLPHYFHGCG HAVYNNSLYY HKGGSNTIVR FEFGKETPQT
410 420 430 440 450
LKLEDALYFD RKYLFANSKT YFNIAVDEKG LWIIYASSVD GSSILVAQLD
460 470 480 490 500
ERTFSVLRHI NTTYPKSKAG NAFIAQGILY VTDTKDTRVT FAFDLLRGKQ
510 520 530 540
INANFGLRMS QSVLAMLSYN MRDQHLYSWE DGHLMLYPVH FSSTAPSQR
Length:549
Mass (Da):59,330
Last modified:June 1, 2003 - v1
Checksum:iB772F28EEC85FA21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY266116 mRNA. Translation: AAP22419.1.
RefSeqiNP_852047.1. NM_181382.2.
UniGeneiRn.38054.

Genome annotation databases

GeneIDi315675.
KEGGirno:315675.
UCSCiRGD:727879. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY266116 mRNA. Translation: AAP22419.1.
RefSeqiNP_852047.1. NM_181382.2.
UniGeneiRn.38054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D77X-ray1.48A260-543[»]
4D7CX-ray1.45A/B260-543[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029833.

Proteomic databases

PaxDbiQ80WL1.
PRIDEiQ80WL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi315675.
KEGGirno:315675.
UCSCiRGD:727879. rat.

Organism-specific databases

CTDi342035.
RGDi727879. Gldn.

Phylogenomic databases

eggNOGiENOG410KCV6. Eukaryota.
ENOG4110Z7Z. LUCA.
HOGENOMiHOG000112733.
HOVERGENiHBG081557.
InParanoidiQ80WL1.
KOiK16364.
PhylomeDBiQ80WL1.

Miscellaneous databases

NextBioi669645.
PROiQ80WL1.

Family and domain databases

InterProiIPR008160. Collagen.
IPR031224. Gliomedin.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF5. PTHR23192:SF5. 1 hit.
PfamiPF01391. Collagen. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier."
    Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I., Bermingham J.R. Jr., Peles E.
    Neuron 47:215-229(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NFASC AND NRCAM, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    Strain: Wistar.
    Tissue: Schwann cell.
  2. "Secreted gliomedin is a perinodal matrix component of peripheral nerves."
    Eshed Y., Feinberg K., Carey D.J., Peles E.
    J. Cell Biol. 177:551-562(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 278-281, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, SUBUNIT, INTERACTION WITH NFACS, MUTAGENESIS OF ARG-91 AND ARG-94.
  3. "Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier."
    Labasque M., Devaux J.J., Leveque C., Faivre-Sarrailh C.
    J. Biol. Chem. 286:42426-42434(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFASC AND NRCAM, SUBCELLULAR LOCATION.
  4. "The olfactomedin domain from gliomedin is a beta-propeller with unique structural properties."
    Han H., Kursula P.
    J. Biol. Chem. 290:3612-3621(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 260-543.

Entry informationi

Entry nameiGLDN_RAT
AccessioniPrimary (citable) accession number: Q80WL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 2003
Last modified: December 9, 2015
This is version 77 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.