RNFT2_PONAB
ID RNFT2_PONAB Reviewed; 444 AA.
AC Q5RAG4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=RING finger and transmembrane domain-containing protein 2;
DE AltName: Full=Transmembrane protein 118;
GN Name=RNFT2; Synonyms=TMEM118;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; CR859053; CAH91246.1; -; mRNA.
DR RefSeq; NP_001127393.1; NM_001133921.1.
DR AlphaFoldDB; Q5RAG4; -.
DR STRING; 9601.ENSPPYP00000005700; -.
DR GeneID; 100174460; -.
DR KEGG; pon:100174460; -.
DR CTD; 84900; -.
DR eggNOG; KOG4638; Eukaryota.
DR InParanoid; Q5RAG4; -.
DR OrthoDB; 1321151at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044235; RNFT1/2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR15860; PTHR15860; 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 Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..444
FT /note="RING finger and transmembrane domain-containing
FT protein 2"
FT /id="PRO_0000279510"
FT TOPO_DOM 1..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ZN_FING 384..422
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 13..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48919 MW; 3743EB2C862EABDB CRC64;
MWLFTVNQVL RKMQRRHSSN TDNIPPERNR SQALSSEASV DEGGVFESLK AEAASPPALF
SGLSGSLPTS SFPSSLVLGS SAGGGDVFIQ MPASREEGGG RGEGGAYHHR QPHHHFHHGG
HRGGSLLQHV GGDHRGHSEE GGDEQPGTPA PALSELKAVI CWLQKGLPFI LILLAKLCFQ
HKLGIAVCIG MASTFAYANS TLREQVSLKE KRSVLVILWI LAFLAGNTLY VLYTFSSQQL
YNSLIFLKPN LETLDFFDLL WIVGIADFVL KYITIALKCL IVALPKIILA VKSKGKFYLV
IEELSQLFRS LVPIQLWYKY IMGDDSSNSY FLGGVLIVLY SLCKSFDICG RVGGVRKALK
LLCTSQNYGV RATGQQCTEA GDICAICQAE FREPLILLCQ HVFCEECLCL WLDRERTCPL
SRSVAVDTLR CWKDGATSAH FQVY