Entry sw:RN139_PONAB

ID   RN139_PONAB             Reviewed;         664 AA.
AC   Q5RBT7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   11-MAY-2016, entry version 79.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF139;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 139;
DE   AltName: Full=Translocation in renal carcinoma on chromosome 8 protein;
GN   Name=RNF139;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3-ubiquitin ligase; acts as a negative regulator of the
CC       cell proliferation through mechanisms involving G2/M arrest and
CC       cell death. Required for MHC class I ubiquitination in cells
CC       expressing the cytomegalovirus protein US2 before dislocation from
CC       the endoplasmic reticulum (ER). Affects SREBP processing by
CC       hindering the SREBP/SCAP complex translocation from the ER to the
CC       Golgi, thereby reducing SREBF2 target gene expression. Required
CC       for INSIG1 ubiquitination. May be required for EIF3 complex
CC       ubiquitination. May function as a signaling receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with VHL. Interacts with MHC class I and HM13.
CC       Component of SCAP/SREBP complex composed of SREBF2, SCAP and
CC       RNF139; the complex hampers the interaction between SCAP and
CC       SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts
CC       with SREBF2 (via C-terminal domain). Interacts with SCAP; the
CC       interaction inhibits the interaction of SCAP with SEC24B and
CC       hampering the ER to Golgi transport of the SCAP/SREBP complex.
CC       Interacts with SEC24B. Interacts with INSIG1 and INSIG2. Interacts
CC       with EIF3F and EIF3H; the interaction leads to protein translation
CC       inhibitions in a ubiquitination-dependent manner. Interacts with
CC       XBP1; the interaction induces ubiquitination and degradation of
CC       XBP1 (By similarity). {ECO:0000250|UniProtKB:Q8WU17}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The RING-type zinc finger domain may be essential for
CC       ubiquitin ligase activity. {ECO:0000250}.
CC   -!- PTM: Autoubiquitinated. Ubiquitination is induced by sterol and
CC       leads to ist degradation via the ubiquitin-proteasome pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00175}.
DR   EMBL; CR858546; CAH90773.1; -; mRNA.
DR   UniGene; Pab.7809; -.
DR   ProteinModelPortal; Q5RBT7; -.
DR   STRING; 9601.ENSPPYP00000021168; -.
DR   eggNOG; KOG0802; Eukaryota.
DR   eggNOG; COG5243; LUCA.
DR   HOVERGEN; HBG053146; -.
DR   InParanoid; Q5RBT7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR025754; TRC8_N_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13705; TRC8_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Endoplasmic reticulum; Ligase;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q8WU17}.
FT   CHAIN         2    664       E3 ubiquitin-protein ligase RNF139.
FT                                /FTId=PRO_0000284916.
FT   TRANSMEM     51     71       Helical. {ECO:0000255}.
FT   TRANSMEM     85    105       Helical. {ECO:0000255}.
FT   TRANSMEM    125    145       Helical. {ECO:0000255}.
FT   TRANSMEM    154    174       Helical. {ECO:0000255}.
FT   TRANSMEM    178    198       Helical. {ECO:0000255}.
FT   TRANSMEM    293    313       Helical. {ECO:0000255}.
FT   TRANSMEM    323    343       Helical. {ECO:0000255}.
FT   TRANSMEM    356    376       Helical. {ECO:0000255}.
FT   TRANSMEM    390    410       Helical. {ECO:0000255}.
FT   TRANSMEM    420    440       Helical. {ECO:0000255}.
FT   TRANSMEM    469    489       Helical. {ECO:0000255}.
FT   TRANSMEM    495    512       Helical. {ECO:0000255}.
FT   ZN_FING     547    586       RING-type; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     634    634       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     635    635       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     663    663       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        20    516       ipfam:TRC8_N [T]
FT   MYHIT       547    586       iprf:ZF_RING_2 [T]
FT   MYHIT       546    585       ipfam:zf-RING_2 [T]
FT   MYHIT       547    585       ismart:RING [T]
FT   MYHIT       546    586       ismart:RINGv [T]
SQ   SEQUENCE   664 AA;  75941 MW;  51F0E0C0068813D6 CRC64;
     MAAVGPPQQQ VRMAHRQVWA ALEVALRVPC LYIIDAIFNS YPDSSQSRFC IVLQIFLRLL
     GIFVSSIVLI LSQRSLFKFY MYSSAFLLAA TSVLVNYYAS LHIDFYGAYN TSAFGIELLP
     RKGPSLWMAL IVLQLTFGIG YVTLLQIHSI YSQLIILDLL VPVIGLITEL PLHIRETLVF
     TSSLILTLNT VLVLAVKLKW FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV
     FWLTRVTAQA TVLMYILRMA NETDSFFISW DDFWDLICNL IISGCDSTLT VLGMSAVISS
     VAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI RLSRNMCLLL
     TAVLHFIHGM TDPVLMSLSA SHVSSFRRHF PVLFVSACLF ILPVLLSYVL WHHYALNTWL
     FAATAFCVEL CLKVIVSLTV YTLFMIDGYY NVLWEKLDNY VYYVRSTGSI IVFIFGVVMF
     GNGAYTMMFE SGSKIRAFMM CLHAYFNIYL QAKNGWKTFM NRRTAVKKIN SLPEIKGSRL
     QEINDVCAIC YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDDIKDNSN
     VSNNNGFTPP NETPEEAVRE AAAESDRELN EDDSTDCDDD VQRERNGVIQ HTGAAAEEFN
     DDTD
//