ERMIN_BOVIN
ID ERMIN_BOVIN Reviewed; 282 AA.
AC Q3ZBR9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ermin;
DE AltName: Full=Juxtanodin;
DE Short=JN;
GN Name=ERMN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBUNIT: Binds actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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DR EMBL; BT026259; ABG67098.1; -; mRNA.
DR EMBL; BC103144; AAI03145.1; -; mRNA.
DR RefSeq; NP_001029971.1; NM_001034799.1.
DR AlphaFoldDB; Q3ZBR9; -.
DR SMR; Q3ZBR9; -.
DR STRING; 9913.ENSBTAP00000017162; -.
DR PaxDb; Q3ZBR9; -.
DR Ensembl; ENSBTAT00000017162; ENSBTAP00000017162; ENSBTAG00000012912.
DR GeneID; 617274; -.
DR KEGG; bta:617274; -.
DR CTD; 57471; -.
DR VEuPathDB; HostDB:ENSBTAG00000012912; -.
DR VGNC; VGNC:28591; ERMN.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_090355_0_0_1; -.
DR InParanoid; Q3ZBR9; -.
DR OMA; WDEEINN; -.
DR OrthoDB; 1204148at2759; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000012912; Expressed in pons and 32 other tissues.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IBA:GO_Central.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0033270; C:paranode region of axon; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IBA:GO_Central.
DR GO; GO:0031344; P:regulation of cell projection organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..282
FT /note="Ermin"
FT /id="PRO_0000314747"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..282
FT /note="Binds actin"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJL0"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
SQ SEQUENCE 282 AA; 32392 MW; 967B8176658E7BA5 CRC64;
MTDVPVTFSQ VECNGDTPPE NGQQKITKIT EGASDVDGTP PHCRVEPRLD VPTERNQEKS
EKLQEDILLS SSMDEKILKE KPEEKLYVVH KALTDLSLQE AAVDKMALRE GHQWEKIPLS
SSNQEISRQK ERISEQPLEE REDEELENTA LQATEIEWLG FQKSSQVDLS HSKQDEEQEV
WDEEINNDDD DDCKDDEDEV RVIEFKKKNE EDTQLKEEGD ASEDSPLSSP SSQPVTPDEQ
PTFGKKGDFS RNAYSRYNTI SYRKIRKGNT KQRIDEFESM IN
