ID   ERMIN_PONAB             Reviewed;         284 AA.
AC   Q5R6D6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Ermin;
DE   AltName: Full=Juxtanodin;
DE            Short=JN;
GN   Name=ERMN;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860555; CAH92680.1; -; mRNA.
DR   RefSeq; NP_001126570.1; NM_001133098.1.
DR   AlphaFoldDB; Q5R6D6; -.
DR   SMR; Q5R6D6; -.
DR   STRING; 9601.ENSPPYP00000014355; -.
DR   GeneID; 100173561; -.
DR   KEGG; pon:100173561; -.
DR   CTD; 57471; -.
DR   eggNOG; KOG2030; Eukaryota.
DR   InParanoid; Q5R6D6; -.
DR   OrthoDB; 1204148at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
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..284
FT                   /note="Ermin"
FT                   /id="PRO_0000314750"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..284
FT                   /note="Binds actin"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..199
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJL0"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
FT   MOD_RES         237
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5EBJ4"
SQ   SEQUENCE   284 AA;  32765 MW;  C9F32A7BC3926325 CRC64;
     MTDVPATFTQ AECNGDKPPE NGQQPITKIS EELTDVDSPL PHYRVEPSLE GAPTKGSQEE
     RRKLQGNMLL NSSMEEKILK ENPEEKLFVV HKAITDLSLQ ETSADEMTFR EGRQWEKIPL
     SGSNQEIRRQ KERITEQPLK EEEDEDRKNK GHQAAEIEWL GFRKPSQADM LHSKHDEEQK
     VWDEEIDDDD DDNCNDDEDE VRVIEFKKKH EEVSQFKEEG DASEDSPLSS ASSQAVTPDE
     QPTLGKKSDI SRNAYSRYNT ISYRKIRKGN TKQRIDEFES MMHL