ERMIN_RAT
ID ERMIN_RAT Reviewed; 282 AA.
AC Q5RJL0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ermin;
DE AltName: Full=Juxtanodin;
DE Short=JN;
GN Name=Ermn;
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, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=CNS;
RX PubMed=16051705; DOI=10.1073/pnas.0500952102;
RA Zhang B., Cao Q., Guo A., Chu H., Chan Y.G., Buschdorf J.P., Low B.C.,
RA Ling E.A., Liang F.;
RT "Juxtanodin: an oligodendroglial protein that promotes cellular
RT arborization and 2',3'-cyclic nucleotide-3'-phosphodiesterase
RT trafficking.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11527-11532(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-212; SER-224 AND
RP THR-235, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in cytoskeletal rearrangements during the late
CC wrapping and/or compaction phases of myelinogenesis as well as in
CC maintenance and stability of myelin sheath in the adult. May play an
CC important role in late-stage oligodendroglia maturation, myelin/Ranvier
CC node formation during CNS development, and in the maintenance and
CC plasticity of related structures in the mature CNS (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16051705}.
CC -!- SUBUNIT: Binds actin. {ECO:0000269|PubMed:16051705}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16051705}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RJL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RJL0-2; Sequence=VSP_030355;
CC -!- TISSUE SPECIFICITY: Expressed specifically by the oligodendrocytes.
CC Highest expression seen in the spinal cord followed by brainstem,
CC cerebellum, thalamus, and hypothalamus. In the myelin sheath, found
CC mainly in the abaxon and the lateral few terminal loops. Its apposition
CC to the myelinated axon, through the latter, defines an axonal
CC subregion, termed juxtanode, at the Ranvier node-paranode junction.
CC {ECO:0000269|PubMed:16051705}.
CC -!- DEVELOPMENTAL STAGE: Undetected at postnatal day 1 (P1) through P7.
CC Expressed weakly at P10, rapidly increases during the period P14 to P21
CC and reaches adult levels by P28. {ECO:0000269|PubMed:16051705}.
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DR EMBL; DQ119821; AAZ14038.1; -; mRNA.
DR EMBL; BC086596; AAH86596.1; -; mRNA.
DR RefSeq; NP_001008312.1; NM_001008311.3. [Q5RJL0-1]
DR AlphaFoldDB; Q5RJL0; -.
DR SMR; Q5RJL0; -.
DR STRING; 10116.ENSRNOP00000029247; -.
DR iPTMnet; Q5RJL0; -.
DR PhosphoSitePlus; Q5RJL0; -.
DR PaxDb; Q5RJL0; -.
DR PRIDE; Q5RJL0; -.
DR Ensembl; ENSRNOT00000034449; ENSRNOP00000029247; ENSRNOG00000021472. [Q5RJL0-1]
DR GeneID; 295619; -.
DR KEGG; rno:295619; -.
DR UCSC; RGD:1308367; rat. [Q5RJL0-1]
DR CTD; 57471; -.
DR RGD; 1308367; Ermn.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_090355_0_0_1; -.
DR InParanoid; Q5RJL0; -.
DR OMA; WDEEINN; -.
DR OrthoDB; 1204148at2759; -.
DR PhylomeDB; Q5RJL0; -.
DR TreeFam; TF337225; -.
DR PRO; PR:Q5RJL0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021472; Expressed in cerebellum and 1 other tissue.
DR ExpressionAtlas; Q5RJL0; baseline and differential.
DR Genevisible; Q5RJL0; RN.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0033269; C:internode region of axon; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0001763; P:morphogenesis of a branching structure; ISO:RGD.
DR GO; GO:0031344; P:regulation of cell projection organization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR DisProt; DP01521; -.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR045346; Ermin.
DR InterPro; IPR008954; Moesin_tail_sf.
DR PANTHER; PTHR47137; PTHR47137; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..282
FT /note="Ermin"
FT /id="PRO_0000314751"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Binds actin"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 268..282
FT /note="NTKQRIDEFESMMHL -> Q (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030355"
SQ SEQUENCE 282 AA; 32228 MW; 010BC8530B4C5702 CRC64;
MTDTPVTLSG SECNGDRPPE NGQQPSSQTR KTTDADETQT YYGVEPSLQH LPAKENQEES
GNSKGNVLPR GSEDEKILNE NTEENLFVVH QAIQDLSLQE TSAEDTVFQE GHPWKKIPLN
SHNLDMSRQK ERIVHQHLEQ REDESAAHQA TEIEWLGFQK SSQVDILHSK CDEEEEVWNE
EINEEDVDEC AEDEGEDEVR VIEFKRKYRE GSPLKEESLA REDSPLSSPS SQPGTPDEQL
VLGKKGDIAR NSYSRYNTIS YRKIRKGNTK QRIDEFESMM HL
