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Database: UniProt
Entry: I3MGB6_ICTTR
LinkDB: I3MGB6_ICTTR
Original site: I3MGB6_ICTTR 
ID   I3MGB6_ICTTR            Unreviewed;       381 AA.
AC   I3MGB6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RNF13 {ECO:0000313|Ensembl:ENSSTOP00000009777.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000009777.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000009777.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AGTP01103837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01103838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005339961.1; XM_005339904.1.
DR   AlphaFoldDB; I3MGB6; -.
DR   STRING; 43179.ENSSTOP00000009777; -.
DR   Ensembl; ENSSTOT00000010902.3; ENSSTOP00000009777.2; ENSSTOG00000010899.3.
DR   GeneID; 101965398; -.
DR   CTD; 11342; -.
DR   eggNOG; KOG4628; Eukaryota.
DR   GeneTree; ENSGT00940000154942; -.
DR   HOGENOM; CLU_035275_1_1_1; -.
DR   InParanoid; I3MGB6; -.
DR   OMA; GHIVLIP; -.
DR   OrthoDB; 5474929at2759; -.
DR   TreeFam; TF317486; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0008432; F:JUN kinase binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051640; P:organelle localization; IEA:Ensembl.
DR   GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; IEA:Ensembl.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   CDD; cd02123; PA_C_RZF_like; 1.
DR   CDD; cd16796; RING-H2_RNF13; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR   PANTHER; PTHR22765:SF34; E3 UBIQUITIN-PROTEIN LIGASE RNF13; 1.
DR   PANTHER; PTHR22765; RING FINGER AND PROTEASE ASSOCIATED DOMAIN-CONTAINING; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        182..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          240..282
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          285..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..354
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  42620 MW;  32AA0FD32A4ACEE9 CRC64;
     MLLSIGMLML SATQVYTLLT VQLFAFLNLL PVEADILAYN LENASQTFDD LPARFGYRLP
     AEGLKGFLIN SKPENACEPI APPPLKDNSS GAFIVLIRRL DCNFDIKVLN AQRAGYKAAI
     VHNVDSDDLI SMGSNDIDVL KKIDIPSVFI GESSANSLKD EFTYEKGGHI ILVPEFSLPL
     EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FRKGDEYDVC
     AICLDDYEDG DKLRVLPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
     EENEVSEHTP LLRPLASVSA QSFGALSESH SHQNMTESSD YEDEDNEDTD SSDAENEINE
     HSVVVQLQAN GDRDYNIANT V
//
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