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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)DescriptionActionsGraphical viewLength
Topological domaini1 – 17CytoplasmicSequence analysisAdd BLAST17
Transmembranei18 – 38Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini39 – 549ExtracellularSequence analysisAdd BLAST511

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91R → G: Abolishes cleavage and shedding of ectodomain; when associated with A-94. 1 Publication1
Mutagenesisi94R → A: Abolishes cleavage and shedding of ectodomain; when associated with G-91. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002463231 – 549GliomedinAdd BLAST549
ChainiPRO_000043426795 – 451Gliomedin shedded ectodomain1 PublicationAdd BLAST357

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi375N-linked (GlcNAc...)Sequence analysis1
Glycosylationi461N-linked (GlcNAc...)Sequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei94 – 95Cleavage; by furin-like protease1 Publication2
Sitei277 – 278Cleavage; by BMP1By similarity2

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

1549
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi301 – 304Combined sources4
Beta strandi308 – 312Combined sources5
Beta strandi316 – 322Combined sources7
Beta strandi332 – 348Combined sources17
Helixi349 – 353Combined sources5
Beta strandi358 – 369Combined sources12
Beta strandi375 – 382Combined sources8
Beta strandi385 – 392Combined sources8
Turni393 – 395Combined sources3
Beta strandi399 – 402Combined sources4
Helixi416 – 418Combined sources3
Beta strandi423 – 427Combined sources5
Beta strandi430 – 437Combined sources8
Turni438 – 440Combined sources3
Beta strandi443 – 450Combined sources8
Turni451 – 454Combined sources4
Beta strandi455 – 465Combined sources11
Helixi466 – 468Combined sources3
Beta strandi472 – 475Combined sources4
Beta strandi478 – 482Combined sources5
Beta strandi486 – 494Combined sources9
Turni495 – 498Combined sources4
Beta strandi499 – 501Combined sources3
Beta strandi514 – 520Combined sources7
Turni521 – 524Combined sources4
Beta strandi525 – 530Combined sources6
Beta strandi533 – 541Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D77X-ray1.48A260-543[»]
4D7CX-ray1.45A/B260-543[»]
SMRiQ80WL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini137 – 195Collagen-like 1Add BLAST59
Domaini196 – 222Collagen-like 2Add BLAST27
Domaini296 – 543Olfactomedin-likePROSITE-ProRule annotationAdd BLAST248

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi237 – 261Pro-richAdd BLAST25

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D77X-ray1.48A260-543[»]
4D7CX-ray1.45A/B260-543[»]
SMRiQ80WL1.
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

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...

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: November 2, 2016
This is version 79 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.