RNF10_RAT
ID RNF10_RAT Reviewed; 802 AA.
AC Q5XI59;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=RING finger protein 10;
GN Name=Rnf10;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18941509; DOI=10.1371/journal.pone.0003464;
RA Hoshikawa S., Ogata T., Fujiwara S., Nakamura K., Tanaka S.;
RT "A novel function of RING finger protein 10 in transcriptional regulation
RT of the myelin-associated glycoprotein gene and myelin formation in Schwann
RT cells.";
RL PLoS ONE 3:E3464-E3464(2008).
CC -!- FUNCTION: Transcriptional factor involved in the regulation of MAG
CC (Myelin-associated glycoprotein) expression. Acts as a regulator of
CC Schwann cell differentiation and myelination.
CC {ECO:0000269|PubMed:18941509}.
CC -!- SUBUNIT: Interacts with MEOX2. {ECO:0000250|UniProtKB:Q8N5U6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N5U6}. Nucleus
CC {ECO:0000269|PubMed:18941509}.
CC -!- SIMILARITY: Belongs to the RNF10 family. {ECO:0000305}.
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DR EMBL; BC083831; AAH83831.1; -; mRNA.
DR RefSeq; NP_001011904.1; NM_001011904.1.
DR AlphaFoldDB; Q5XI59; -.
DR STRING; 10116.ENSRNOP00000063855; -.
DR PaxDb; Q5XI59; -.
DR PRIDE; Q5XI59; -.
DR Ensembl; ENSRNOT00000064910; ENSRNOP00000063855; ENSRNOG00000001172.
DR GeneID; 288710; -.
DR KEGG; rno:288710; -.
DR UCSC; RGD:1309282; rat.
DR CTD; 9921; -.
DR RGD; 1309282; Rnf10.
DR eggNOG; KOG2164; Eukaryota.
DR GeneTree; ENSGT00390000001731; -.
DR HOGENOM; CLU_018206_0_0_1; -.
DR InParanoid; Q5XI59; -.
DR PRO; PR:Q5XI59; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Genevisible; Q5XI59; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IDA:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039739; Mag2/Rnf10.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; PTHR12983; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..802
FT /note="RING finger protein 10"
FT /id="PRO_0000259587"
FT ZN_FING 225..267
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5U6"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5U6"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5U6"
SQ SEQUENCE 802 AA; 88410 MW; B71581B1A18A759C CRC64;
MPQSSPSTAA TASDMDKNSG SNSSSASSGS SKGQQPPRSA SAGPAGESKP KSDGKNSNGS
KRYNRKREPS YPKNENFSNQ SRRSNSQKSK TFNKTPPQRG GGSSKPFSSS SNGGRRDEVA
EAQRAEFSPA QFSGPKKINL NHLLNFTFEP RGQAGHFEGS GHGSWGKRNK WGHKPFNKEL
FLQANCQFVV SEDQDYTANF ADPDTLVNWD FVEQVRICSH EVPSCPICLY PPTAAKITRC
GHIFCWACIL HYLSLSERTW SKCPICYSSV HKKDLKSVVA TESRQYVVGD TITMQLMKRE
KGVLVALPKS KWMNVDHPIS LGDEQHSQYS KLLLASKEQV LHRVVLEEKV ALEQQLAEEK
HTPESCFIEA ALQEVKIREE ALSGVAGGRA EVTGVVTALE QLVLMAPLAK ESAFQPRKGV
LEYLSAFDEE AAQVCSLDPP GPLALPLVEE EEAVSEPEAC EDLIADDSLG EGTVCAELSQ
EEPIAKPGFT QLSSSPCYYF YQAEDGQHMF LHPVNVRCLV REYGSLEQSP EKISATVVEI
AGYSMSEDVR QRHRYLSHLP LTCEFSICEL ALQPPVVSKE TLEMFSDDIE KRKRQRQKKA
REERRRERRI ELEENKRQGR YPEVHIPLEN LQQFPAFNSY TCSSDSALGP TSTEGHGALS
LSPLSRSPGS HADFLLTPLS PTASQGSPSF CVGSLEEDSP FLSFAQMLRV GKAKADGWPK
AAPKKDDNSL APPAPVDSDG ESDNSDRVPV PSFQNSFSQA IEAAFMKLDT PATSDPLSDR
GGRKRKRQKQ KLLFSTSVVH TK
