RNF10_BOVIN
ID RNF10_BOVIN Reviewed; 810 AA.
AC Q08E13; A6H708;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=RING finger protein 10;
GN Name=RNF10;
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].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q5XI59}.
CC -!- SUBUNIT: Interacts with MEOX2. {ECO:0000250|UniProtKB:Q8N5U6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N5U6}. Nucleus
CC {ECO:0000250|UniProtKB:Q5XI59}.
CC -!- SIMILARITY: Belongs to the RNF10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123470; AAI23471.1; -; mRNA.
DR EMBL; BC146068; AAI46069.1; -; mRNA.
DR RefSeq; NP_001070337.1; NM_001076869.1.
DR AlphaFoldDB; Q08E13; -.
DR STRING; 9913.ENSBTAP00000020937; -.
DR PaxDb; Q08E13; -.
DR PRIDE; Q08E13; -.
DR Ensembl; ENSBTAT00000020937; ENSBTAP00000020937; ENSBTAG00000015767.
DR GeneID; 520757; -.
DR KEGG; bta:520757; -.
DR CTD; 9921; -.
DR VEuPathDB; HostDB:ENSBTAG00000015767; -.
DR VGNC; VGNC:34007; RNF10.
DR eggNOG; KOG2164; Eukaryota.
DR GeneTree; ENSGT00390000001731; -.
DR HOGENOM; CLU_018206_0_0_1; -.
DR InParanoid; Q08E13; -.
DR OMA; PCLLHYL; -.
DR OrthoDB; 1373540at2759; -.
DR TreeFam; TF323455; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000015767; Expressed in cardiac ventricle and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
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; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..810
FT /note="RING finger protein 10"
FT /id="PRO_0000283048"
FT ZN_FING 225..267
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..185
FT /note="Interaction with MEOX2"
FT /evidence="ECO:0000250"
FT REGION 598..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..810
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..111
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 810 AA; 89716 MW; A2A1052DF8DB6976 CRC64;
MPQSSPSAAA TASDMDKNSG SSSSSASSGS SKGQQPPRSA SAGPAGESKP KSDGKNSSGS
KRYNRKREPS YPKNENFINQ SRRSNSQKSK TFNKMPPQRG GGSSKLFSSS FNGGRRDEVA
EAQRAEFSPA QFSGPKKINL NHLLNFTFEP RGQAGHFEGS GHGSWGKRNK WGHKPFNKEL
FLQANCQFVV SEDQDYTVHF ADPDTLVNWD FVEQVRICSH EVPSCPICLY PPTAAKITRC
GHIFCWACIL HYLSLSEKTW SKCPICYSSV HKKDLKSVVA TESRQYVVGD TITMQLMKRE
KGVLVALPKS KWMNVDHPIH LGDEQHSQYS KLLLASKEQV LRRVVQEEKA ALERQLAEEK
HTPESCFIEA AIQELKAREE ALSGLAESRG EVPGVVAALE QRVLMAPLAK ESVFQPRKGV
LEYLSAFDED ATEVCSLGPP HPVALPLVEE EETVSEPEPE GLSEACEDLE LVEDNLGEGT
ICTESSQQEP VSKPSVTHLS SSPCYYFYQA EDGQHMFLHP VNVRCLVREY GSLEQSPEKI
SATVVEISGY SMSEDMRQRH RYLSHLPLTC EFSICELALQ PPLVSKETLE IFSDDIEKRK
RQRQKKAREE RRRERRIEME ENKKQGKYPE VHIPLENLQQ FPAFNSYTCS SDSALGSTST
EGRGALSLSP LSRSPGSQAD FLLTPLSPTA SQGSPSFCVG SLEEDSPFPS FAQMLRVGKA
KADVWPKTAP KKDENTLGPP APVDSDGESD NSDRVPVPSF QNSFSQAIEA AFMKLDTPVT
SDPLSEEKGG KKRKKQKQKL LFSTSVVHTK