ID A0A2K6EIT0_PROCO Unreviewed; 356 AA.
AC A0A2K6EIT0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RNF167 {ECO:0000313|Ensembl:ENSPCOP00000001634.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000001634.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000001634.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_012515343.1; XM_012659889.1.
DR AlphaFoldDB; A0A2K6EIT0; -.
DR STRING; 379532.ENSPCOP00000001634; -.
DR Ensembl; ENSPCOT00000005795.1; ENSPCOP00000001634.1; ENSPCOG00000005095.1.
DR GeneID; 105822856; -.
DR KEGG; pcoq:105822856; -.
DR CTD; 26001; -.
DR GeneTree; ENSGT00940000159547; -.
DR OMA; RIPTHKF; -.
DR OrthoDB; 5474929at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0036020; C:endolysosome membrane; 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:1990253; P:cellular response to leucine starvation; IEA:Ensembl.
DR GO; GO:0032418; P:lysosome localization; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0035519; P:protein K29-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR CDD; cd16797; RING-H2_RNF167; 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; PTHR47168:SF6; PROTEASE-ASSOCIATED (PA) RING_U-BOX ZINC FINGER FAMILY PROTEIN; 1.
DR PANTHER; PTHR47168; RING ZINC FINGER DOMAIN SUPERFAMILY PROTEIN-RELATED; 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:UP000233160};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..356
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014394293"
FT TRANSMEM 170..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..272
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 271..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38932 MW; 54471ABDE2206BDD CRC64;
MHLAAFPIPV VVATVLWGAA PIRGLIRATS DHNASMDFAD LPALFGATLS QEGLQGFLVE
AHPDNACSPI APPPPAPVNG SVFIALLRRF DCNFDLKVLN AQKAGYGAAI VHNVNSNELL
NMVWNSEEIQ QQIWIPSVFI GERSSEYLRA LFVYDKGARV LLVPDNSFPL GYYLIPFTGI
VGLLVLAMGA VMIVRCIQHR KRLQRNRLTK EQLKQIPTHD YQKGDQYDVC AICLDEYQDG
DKLRVLPCAH AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEEQEEEIQG QEEGDEEGEP
RDHPASERTP LLGSSPTLPT SFGSLAPAPL VFPGPSTDPP PSPSSSSSSL SPAILV
//
