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Protein

Gliomedin

Gene

Gldn

Organism
Mus musculus (Mouse)
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:20188654). 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 (PubMed:20188654). Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (PubMed:24719088).By similarity2 Publications

GO - Molecular functioni

  • protein binding involved in heterotypic cell-cell adhesion Source: MGI

GO - Biological processi

  • clustering of voltage-gated sodium channels Source: MGI
  • microvillus organization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Gliomedin
Alternative name(s):
Cancer-related gene liver 2 protein
Short name:
CRG-L2
Cleaved into the following chain:
Gene namesi
Name:Gldn
Synonyms:Crgl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2388361. Gldn.

Subcellular locationi

Gliomedin shedded ectodomain :

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

  • collagen trimer Source: UniProtKB-KW
  • extracellular space Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mutant mice present no obvious neurological phenotype and have normal nerve conduction. Nerves from their peripheral nervous system have myelin sheets that are indistinguishable from wild-type. In contrast, they present impaired and disorganized attachment of Schwann cell microvilli to the axolemma at nodes of Ranvier. Mature nodes are formed by the fusion of two heminodes. During development, mutant mice present defective clustering of sodium channels at heminodes, but display normal sodium channel clustering at mature nodes (PubMed:20188654). Mice lacking both Gldn and Nrcam are born at the expected Mendelian rate, but are smaller than control littermates and display important neurological impairments, in spite of seemingly normal nerve myelination. Motor abnormalities vary between individuals, ranging from ataxia, uncoordinated movements and premature death to weakness of the hind limbs, hypomotility, strongly impaired ability to hang from a horizontal bar with their forelimbs and a tendency to stumble. The motor defects correlate with decreased velocity of nerve conduction and slower propagation of action potentials. Most mice die within 60 days after birth, and none are fertile. Mutant mice display delayed formation of mature nodes of Ranvier; 15 days after birth about 20% of the nodes lack detectable sodium channel clusters. Sodium channel clustering and nerve conduction appear normal 60 and 75 days after birth, but subsequently a gradual disintegration of the nodal protein complexes is seen. About 70% of the mutant nodes present high-density sodium channel clustering at 120 days after birth, as opposed to nearly 100% for wild-type. Contrary to wild-type, in adult nodes of Ranvier the sodium channels are often clustered near the paranode border with an empty gap in the middle. At nodes of Ranvier, Schwann cell microvilli are sparse or absent and show defects in their orientation, resulting in various structural abnormalities at the node and the paranode border (PubMed:24719088).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91R → A: Abolishes furin-mediated cleavage and shedding of ectodomain. 1 Publication1
Mutagenesisi278 – 279DD → AA: Abolishes BMP1-mediated cleavage of ectodomain release of olfactomedin-like domain. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002463221 – 549GliomedinAdd BLAST549
ChainiPRO_000043426695 – 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. Further cleavage by BMP1 releases the olfactomedin-like domain.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei94 – 95Cleavage; by furin-like protease1 Publication2
Sitei277 – 278Cleavage; by BMP11 Publication2

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8BMF8.
PRIDEiQ8BMF8.

PTM databases

PhosphoSitePlusiQ8BMF8.

Expressioni

Tissue specificityi

Detected in sciatic nerve (at protein level) (PubMed:17293346, PubMed:20188654, PubMed:24719088). Widely expressed with higher expression in testis and skeletal muscle (PubMed:12642876).4 Publications

Gene expression databases

BgeeiENSMUSG00000046167.
CleanExiMM_GLDN.

Interactioni

Subunit structurei

Homotrimer (via collagen-like domains) (PubMed:17293346). Interacts with NRCAM and NFACS/neurofascin (PubMed:16039564, PubMed:20188654). Interaction with glial NRCAM enhances interaction with axonal NFACS (PubMed:20188654). Interacts with MYOC (PubMed:23897819).4 Publications

GO - Molecular functioni

  • protein binding involved in heterotypic cell-cell adhesion Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056080.

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 – 321Combined sources6
Beta strandi325 – 327Combined sources3
Beta strandi332 – 348Combined sources17
Helixi349 – 353Combined sources5
Beta strandi358 – 369Combined sources12
Beta strandi375 – 382Combined sources8
Beta strandi385 – 392Combined sources8
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
4XAVX-ray2.05A/B/C/D279-549[»]
ProteinModelPortaliQ8BMF8.
SMRiQ8BMF8.
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.1 Publication

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

eggNOGiENOG410INP7. Eukaryota.
ENOG4110Z7Z. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000112733.
HOVERGENiHBG081557.
InParanoidiQ8BMF8.
KOiK16364.
OMAiERIWLTM.
OrthoDBiEOG091G0841.
PhylomeDBiQ8BMF8.
TreeFamiTF315964.

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.

Q8BMF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRAAERGQG ATGWGLRGAL VAIALLSALN AAGTVFVLCQ WRGLSAALRA
60 70 80 90 100
LEAQRGREQR EDSALRAFLA ELSRAPGRVP EPSQDPMSAA RNKRSHNGEP
110 120 130 140 150
ASHIRAESQD MMMMMTYSMV PIRVMIDLCN STQGICLTGP PGPPGPPGAG
160 170 180 190 200
GLPGHNGSDG QPGLQGPKGE KGAIGKRGKM GLPGATGNPG EKGEKGDAGE
210 220 230 240 250
LGLPGNEGPP GQKGDKGDKG DVSNDVLLTG AKGDQGPPGP PGPPGPPGPP
260 270 280 290 300
GSRRSKGPRP PNVFNSQCPG ETCVIPNDDT LVGRADEKAN ERHSPQTESM
310 320 330 340 350
ITSIGNPAQV LKVRETFGTW MRESANKSDD RIWVTEHFSG IMVKEFKDLP
360 370 380 390 400
ALLNSSFTLL HLPHYFHGCG HAVYNNSLYY HKGGSNTIVR FEFGKETPQT
410 420 430 440 450
LKLENALYFD RKYLFANSKT YFNIAVDEKG IWIIYASSVD GSSILVAQLD
460 470 480 490 500
ERTFSVTQHI NTTYPKSKAG NAFIARGILY VTDTKDTRVT FAFDLLGGKQ
510 520 530 540
INANFDFRMS QSVLAMLSYN MRDQHLYSWE DGHLMLYPVQ FLSAASSQR
Length:549
Mass (Da):59,137
Last modified:March 1, 2003 - v1
Checksum:i43F1B89FF9634F1D
GO

Sequence cautioni

The sequence AAO49510 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti451E → G in AAO49510 (PubMed:12642876).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031523 mRNA. Translation: BAC27432.1.
AF548022 mRNA. Translation: AAO49510.1. Different initiation.
CCDSiCCDS23189.1.
RefSeqiNP_796324.1. NM_177350.5.
UniGeneiMm.123549.

Genome annotation databases

EnsembliENSMUST00000056740; ENSMUSP00000056080; ENSMUSG00000046167.
GeneIDi235379.
KEGGimmu:235379.
UCSCiuc009pqx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031523 mRNA. Translation: BAC27432.1.
AF548022 mRNA. Translation: AAO49510.1. Different initiation.
CCDSiCCDS23189.1.
RefSeqiNP_796324.1. NM_177350.5.
UniGeneiMm.123549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XAVX-ray2.05A/B/C/D279-549[»]
ProteinModelPortaliQ8BMF8.
SMRiQ8BMF8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056080.

PTM databases

PhosphoSitePlusiQ8BMF8.

Proteomic databases

PaxDbiQ8BMF8.
PRIDEiQ8BMF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056740; ENSMUSP00000056080; ENSMUSG00000046167.
GeneIDi235379.
KEGGimmu:235379.
UCSCiuc009pqx.1. mouse.

Organism-specific databases

CTDi342035.
MGIiMGI:2388361. Gldn.

Phylogenomic databases

eggNOGiENOG410INP7. Eukaryota.
ENOG4110Z7Z. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000112733.
HOVERGENiHBG081557.
InParanoidiQ8BMF8.
KOiK16364.
OMAiERIWLTM.
OrthoDBiEOG091G0841.
PhylomeDBiQ8BMF8.
TreeFamiTF315964.

Miscellaneous databases

PROiQ8BMF8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046167.
CleanExiMM_GLDN.

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_MOUSE
AccessioniPrimary (citable) accession number: Q8BMF8
Secondary accession number(s): Q80ZC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: November 30, 2016
This is version 103 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.