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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}.
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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
 
 
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