GenomeNet

Database: UniProt
Entry: F1RJI6_PIG
LinkDB: F1RJI6_PIG
Original site: F1RJI6_PIG 
ID   F1RJI6_PIG              Unreviewed;       700 AA.
AC   F1RJI6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 4.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF10 {ECO:0000256|ARBA:ARBA00035131};
DE   AltName: Full=RING finger protein 10 {ECO:0000256|ARBA:ARBA00035390};
GN   Name=RNF10 {ECO:0000313|Ensembl:ENSSSCP00000010576.5,
GN   ECO:0000313|VGNC:VGNC:92345};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000010576.5, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000010576.5, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000010576.5,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000010576.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the RNF10 family.
CC       {ECO:0000256|ARBA:ARBA00008117}.
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DR   AlphaFoldDB; F1RJI6; -.
DR   STRING; 9823.ENSSSCP00000010576; -.
DR   PaxDb; 9823-ENSSSCP00000010576; -.
DR   Ensembl; ENSSSCT00000010860.5; ENSSSCP00000010576.5; ENSSSCG00000009910.5.
DR   VGNC; VGNC:92345; RNF10.
DR   eggNOG; KOG2164; Eukaryota.
DR   GeneTree; ENSGT00390000001731; -.
DR   HOGENOM; CLU_018206_0_0_1; -.
DR   InParanoid; F1RJI6; -.
DR   TreeFam; TF323455; -.
DR   ChiTaRS; RNF10; pig.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Bgee; ENSSSCG00000009910; Expressed in blood and 44 other cell types or tissues.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
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   GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   CDD; cd16536; RING-HC_RNF10; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039739; MAG2/RNF10.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          225..266
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..686
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   COMPBIAS        612..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  77982 MW;  197A8E5434FB0074 CRC64;
     MPQSSPNAAA TASDMDKNSG SSSSSTSSGS SKGQQPPRSA SAGPAGESKP KSDGKNSSGS
     KRYNRKREPS YPKNENFITQ SRRSNSQKSK TFNKLPPQRG GGSSKPFSSS FNGGRRDEVA
     EAQRAEFSPA QFSGPKKINL NHLLNFTFEP RGQAGHFEGN GHGSWGKRNK WGHKPFNKEL
     FLQANCQFVV SEDQDYTVHF ADPDTLVNWD FVEQVRICSH EVPSCPICLY PPTAAKITRC
     GHIFCWACIL HYLSLSEKTW SKCPICYSSV HKKDLKSVVA TESRQYVVGD TITMQLMKRE
     KGVLVALPKS KWMNVDHPIH LGDEQHSQYS KLLLASKEQV LHRVIQEEKA ALEQQLAEEK
     HTPESCFIEA AIQELKTREE ALSGLAESRE AVTGVVAALE QLVLMAPLEK ESLFQPRKGV
     LEYLSAFDEE TTEVCSLGAP SRPLALPLVE EEEAVSEPEP EGSSEACNDL ELAEDSLGEG
     TICAESSQQE PVTKPSITHL SSSPCYYFYQ AEDGQHMFLH PVNVRCLVRE YGSLEQSPEK
     ISATVVEIVG YSMSEDVRQR HRYLSHLPLT CEFSICELAL QPPLVSKETL EIFSDDIEKR
     KRQRQKKARE ERRRERRIEM EENKKQGKYP EVHIPLENLQ QFPAFNSYTC SSDSALGPTS
     TESHGALSLS PLSRSPGSQA DAESWKSKSR CVAQNCSKER
//
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