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GLDN_RAT
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   25-MAY-2022, entry version 101.
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   GlyGen; Q80WL1; 6 sites.
DR   PaxDb; Q80WL1; -.
DR   GeneID; 315675; -.
DR   KEGG; rno:315675; -.
DR   UCSC; RGD:727879; rat.
DR   CTD; 342035; -.
DR   RGD; 727879; Gldn.
DR   eggNOG; KOG3545; Eukaryota.
DR   InParanoid; Q80WL1; -.
DR   OrthoDB; 421994at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR008160; Collagen.
DR   InterPro; IPR031224; Gliomedin.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR23192:SF5; PTHR23192:SF5; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF02191; OLF; 1.
DR   SMART; SM00284; OLF; 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
 
 
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