ID GLDN_RAT Reviewed; 549 AA.
AC Q80WL1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=Gliomedin {ECO:0000303|PubMed:16039564};
DE Contains:
DE RecName: Full=Gliomedin shedded ectodomain {ECO:0000250|UniProtKB:Q8BMF8};
DE Flags: Precursor;
GN Name=Gldn;
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], FUNCTION, INTERACTION WITH NFASC AND NRCAM,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Schwann cell;
RX PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I.,
RA Bermingham J.R. Jr., Peles E.;
RT "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT assembly of the nodes of Ranvier.";
RL Neuron 47:215-229(2005).
RN [2]
RP PROTEIN SEQUENCE OF 278-281, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE
RP SPECIFICITY, SUBUNIT, INTERACTION WITH NFASC, AND MUTAGENESIS OF ARG-91 AND
RP ARG-94.
RX PubMed=17485493; DOI=10.1083/jcb.200612139;
RA Eshed Y., Feinberg K., Carey D.J., Peles E.;
RT "Secreted gliomedin is a perinodal matrix component of peripheral nerves.";
RL J. Cell Biol. 177:551-562(2007).
RN [3]
RP INTERACTION WITH NFASC AND NRCAM, AND SUBCELLULAR LOCATION.
RX PubMed=22009740; DOI=10.1074/jbc.m111.266353;
RA Labasque M., Devaux J.J., Leveque C., Faivre-Sarrailh C.;
RT "Fibronectin type III-like domains of neurofascin-186 protein mediate
RT gliomedin binding and its clustering at the developing nodes of Ranvier.";
RL J. Biol. Chem. 286:42426-42434(2011).
RN [4] {ECO:0007744|PDB:4D77, ECO:0007744|PDB:4D7C}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 260-543.
RX PubMed=25525261; DOI=10.1074/jbc.m114.627547;
RA Han H., Kursula P.;
RT "The olfactomedin domain from gliomedin is a beta-propeller with unique
RT structural properties.";
RL J. Biol. Chem. 290:3612-3621(2015).
CC -!- FUNCTION: Ligand for NRCAM and NFASC/neurofascin that plays a role in
CC the formation and maintenance of the nodes of Ranvier on myelinated
CC axons. Mediates interaction between Schwann cell microvilli and axons
CC via its interactions with NRCAM and NFASC (PubMed:16039564). Nodes of
CC Ranvier contain clustered sodium channels that are crucial for the
CC saltatory propagation of action potentials along myelinated axons.
CC During development, nodes of Ranvier are formed by the fusion of two
CC heminodes. Required for normal clustering of sodium channels at
CC heminodes; not required for the formation of mature nodes with normal
CC sodium channel clusters. Required, together with NRCAM, for maintaining
CC NFASC and sodium channel clusters at mature nodes of Ranvier (By
CC similarity). {ECO:0000250|UniProtKB:Q8BMF8,
CC ECO:0000269|PubMed:16039564}.
CC -!- SUBUNIT: Homotrimer (via collagen-like domains) (PubMed:17485493)
CC (Probable). Interacts with NRCAM (PubMed:16039564, PubMed:22009740).
CC Interacts with NFASC/neurofascin (PubMed:16039564, PubMed:17485493,
CC PubMed:22009740). Interaction with glial NRCAM enhances interaction
CC with axonal NFASC. Interacts with MYOC (By similarity).
CC {ECO:0000250|UniProtKB:Q8BMF8, ECO:0000269|PubMed:16039564,
CC ECO:0000269|PubMed:17485493, ECO:0000269|PubMed:22009740}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16039564};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:16039564}.
CC Cell projection, axon {ECO:0000269|PubMed:16039564,
CC ECO:0000269|PubMed:22009740}. Note=Detected at the nodes of Ranvier
CC (PubMed:16039564, PubMed:22009740). Detected at immature heminodes
CC (PubMed:22009740). {ECO:0000269|PubMed:16039564,
CC ECO:0000269|PubMed:22009740}.
CC -!- SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted
CC {ECO:0000269|PubMed:17485493}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:17485493}. Note=Proteolytic
CC processing gives rise to a soluble extracellular domain that is
CC secreted. The gliomedin shedded ectodomain localizes to the nodes of
CC Ranvier. {ECO:0000269|PubMed:17485493}.
CC -!- TISSUE SPECIFICITY: Detected in Schwann cells (at protein level).
CC {ECO:0000269|PubMed:17485493}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in myelinating Schwann cells
CC during the initial period of active myelination.
CC {ECO:0000269|PubMed:16039564}.
CC -!- DOMAIN: The olfactomedin-like domain mediates NFASC/neurofascin and
CC NRCAM binding. {ECO:0000250|UniProtKB:Q8BMF8}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17485493}.
CC -!- PTM: Proteolytic proccessing by a furin-like protease causes shedding
CC of the ectodomain (PubMed:17485493). Further cleavage by BMP1 releases
CC the olfactomedin-like domain. {ECO:0000250|UniProtKB:Q8BMF8,
CC ECO:0000269|PubMed:17485493}.
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DR EMBL; AY266116; AAP22419.1; -; mRNA.
DR RefSeq; NP_852047.1; NM_181382.2.
DR PDB; 4D77; X-ray; 1.48 A; A=260-543.
DR PDB; 4D7C; X-ray; 1.45 A; A/B=260-543.
DR PDBsum; 4D77; -.
DR PDBsum; 4D7C; -.
DR AlphaFoldDB; Q80WL1; -.
DR SMR; Q80WL1; -.
DR STRING; 10116.ENSRNOP00000029833; -.
DR GlyCosmos; Q80WL1; 6 sites, No reported glycans.
DR GlyGen; Q80WL1; 6 sites.
DR PhosphoSitePlus; Q80WL1; -.
DR PaxDb; 10116-ENSRNOP00000029833; -.
DR Ensembl; ENSRNOT00055052997; ENSRNOP00055043797; ENSRNOG00055030546.
DR Ensembl; ENSRNOT00060030101; ENSRNOP00060024297; ENSRNOG00060017611.
DR Ensembl; ENSRNOT00065028213; ENSRNOP00065022306; ENSRNOG00065016907.
DR GeneID; 315675; -.
DR KEGG; rno:315675; -.
DR UCSC; RGD:727879; rat.
DR AGR; RGD:727879; -.
DR CTD; 342035; -.
DR RGD; 727879; Gldn.
DR eggNOG; KOG3545; Eukaryota.
DR InParanoid; Q80WL1; -.
DR OrthoDB; 2876896at2759; -.
DR PhylomeDB; Q80WL1; -.
DR PRO; PR:Q80WL1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISO:RGD.
DR GO; GO:0032528; P:microvillus organization; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR23192:SF5; GLIOMEDIN; 1.
DR PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Collagen;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..549
FT /note="Gliomedin"
FT /id="PRO_0000246323"
FT CHAIN 95..451
FT /note="Gliomedin shedded ectodomain"
FT /evidence="ECO:0000305|PubMed:17485493"
FT /id="PRO_0000434267"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..549
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 137..195
FT /note="Collagen-like 1"
FT DOMAIN 196..222
FT /note="Collagen-like 2"
FT DOMAIN 296..543
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT REGION 74..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 94..95
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000269|PubMed:17485493"
FT SITE 277..278
FT /note="Cleavage; by BMP1"
FT /evidence="ECO:0000250|UniProtKB:Q8BMF8"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 91
FT /note="R->G: Abolishes cleavage and shedding of ectodomain;
FT when associated with A-94."
FT /evidence="ECO:0000269|PubMed:17485493"
FT MUTAGEN 94
FT /note="R->A: Abolishes cleavage and shedding of ectodomain;
FT when associated with G-91."
FT /evidence="ECO:0000269|PubMed:17485493"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 332..348
FT /evidence="ECO:0007829|PDB:4D7C"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 358..369
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:4D7C"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:4D7C"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:4D7C"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:4D7C"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:4D7C"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:4D7C"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:4D7C"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:4D7C"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:4D7C"
SQ SEQUENCE 549 AA; 59330 MW; B772F28EEC85FA21 CRC64;
MTRAAERGQG ATGWGLRGAL MAVALLSVLN AVGTVFVLYQ WRELSAALRA LEAQHGQEQR
EDSALRAFLA ELSRAPARVP EPPQDPMSAA RNKRSHGGEP ASHIRAESQD MMMMMTYSMV
PIRVMIDLCN STQGICLTGP PGPPGPPGAG GLPGHNGSDG QPGLQGPKGE KGAVGKRGKM
GLPGATGNPG EKGEKGDAGE LGLPGNEGPP GQKGDKGDKG DVSNDVLLTG AKGDQGPPGP
PGPPGPPGPP GSRRAKGPRQ PNSFTNQCPG ETCVIPNDDT LVGRADEKVN ERHSPQTEPM
ITSIGNPAQV LKVKETFGTW LRESANRSDD RIWVTEHFSG IMVKEFEDLP ALLNSSFTLL
HLPHYFHGCG HAVYNNSLYY HKGGSNTIVR FEFGKETPQT LKLEDALYFD RKYLFANSKT
YFNIAVDEKG LWIIYASSVD GSSILVAQLD ERTFSVLRHI NTTYPKSKAG NAFIAQGILY
VTDTKDTRVT FAFDLLRGKQ INANFGLRMS QSVLAMLSYN MRDQHLYSWE DGHLMLYPVH
FSSTAPSQR
//
