ERMIN_MOUSE
ID ERMIN_MOUSE Reviewed; 281 AA.
AC Q5EBJ4; Q3UVY3; Q5DTZ8; Q8C5L8; Q9CTR3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ermin;
DE AltName: Full=Juxtanodin;
DE Short=JN;
GN Name=Ermn; Synonyms=Kiaa1189;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16421295; DOI=10.1523/jneurosci.4317-05.2006;
RA Brockschnieder D., Sabanay H., Riethmacher D., Peles E.;
RT "Ermin, a myelinating oligodendrocyte-specific protein that regulates cell
RT morphology.";
RL J. Neurosci. 26:757-762(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Diencephalon, Medulla oblongata, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-223; SER-227;
RP SER-230 AND THR-234, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:16421295}.
CC -!- SUBUNIT: Binds actin. {ECO:0000269|PubMed:16421295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16421295}.
CC -!- TISSUE SPECIFICITY: Brain and spinal cord. Exclusively expressed by the
CC oligodendrocytes. Appears at a late stage during myelination, and in
CC the mature nerves, it is localized to the outer cytoplasmic lip of the
CC myelin sheath and the paranodal loops. {ECO:0000269|PubMed:16421295}.
CC -!- DEVELOPMENTAL STAGE: Weakly detectable in the first 3 postnatal days,
CC but increases during the initial 2 weeks after birth.
CC {ECO:0000269|PubMed:16421295}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37121.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ334270; ABC67250.1; -; mRNA.
DR EMBL; AK220372; BAD90431.1; ALT_INIT; mRNA.
DR EMBL; AK020733; BAB32193.1; -; mRNA.
DR EMBL; AK078089; BAC37121.1; ALT_FRAME; mRNA.
DR EMBL; AK136820; BAE23136.1; -; mRNA.
DR EMBL; AK137305; BAE23300.1; -; mRNA.
DR EMBL; AL928564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089515; AAH89515.1; -; mRNA.
DR EMBL; BC090670; AAH90670.1; -; mRNA.
DR CCDS; CCDS16047.1; -.
DR RefSeq; NP_084248.2; NM_029972.3.
DR AlphaFoldDB; Q5EBJ4; -.
DR SMR; Q5EBJ4; -.
DR BioGRID; 218905; 3.
DR IntAct; Q5EBJ4; 1.
DR STRING; 10090.ENSMUSP00000088458; -.
DR iPTMnet; Q5EBJ4; -.
DR PhosphoSitePlus; Q5EBJ4; -.
DR EPD; Q5EBJ4; -.
DR jPOST; Q5EBJ4; -.
DR MaxQB; Q5EBJ4; -.
DR PaxDb; Q5EBJ4; -.
DR PeptideAtlas; Q5EBJ4; -.
DR PRIDE; Q5EBJ4; -.
DR ProteomicsDB; 275474; -.
DR Antibodypedia; 33703; 115 antibodies from 22 providers.
DR DNASU; 77767; -.
DR Ensembl; ENSMUST00000090940; ENSMUSP00000088458; ENSMUSG00000026830.
DR GeneID; 77767; -.
DR KEGG; mmu:77767; -.
DR UCSC; uc008jsh.1; mouse.
DR CTD; 57471; -.
DR MGI; MGI:1925017; Ermn.
DR VEuPathDB; HostDB:ENSMUSG00000026830; -.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00960000186596; -.
DR HOGENOM; CLU_090355_0_0_1; -.
DR InParanoid; Q5EBJ4; -.
DR OMA; WDEEINN; -.
DR OrthoDB; 1204148at2759; -.
DR PhylomeDB; Q5EBJ4; -.
DR TreeFam; TF337225; -.
DR BioGRID-ORCS; 77767; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ermn; mouse.
DR PRO; PR:Q5EBJ4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5EBJ4; protein.
DR Bgee; ENSMUSG00000026830; Expressed in cerebellar nuclear complex and 66 other tissues.
DR Genevisible; Q5EBJ4; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0033270; C:paranode region of axon; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IDA:MGI.
DR GO; GO:0031344; P:regulation of cell projection organization; IDA:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
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; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..281
FT /note="Ermin"
FT /id="PRO_0000314749"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..281
FT /note="Binds actin"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 97
FT /note="L -> P (in Ref. 3; BAE23136)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="D -> DE (in Ref. 2; BAD90431)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> G (in Ref. 3; BAC37121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 32148 MW; 0D457492AAEB18CB CRC64;
MTDTPETLSG TECNGDRPPE NGQQPSSQTR QETTDADETQ AYYKVEPSLE DLPAKENQEE
TGNTKGNILP KGPEDEKILN ENPEENLFVV HQAIKDLSLQ EISAEDMAFR EGHPWKKIPP
NSSNLEVSRQ KERTAQQQLE QRGDASTTEI EWLGFQKSRP VDILHSKCDE EEEEEEEVWN
EEINEEDVDE CAEEEDEVRV IEFKRKHREG SPLKEESLAR EDSPLGSPGS QPGTPDEQPV
FGKKGDIARN SYSRYNTISY RKIRKGNTKQ RIDEFESMMH L
