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Database: UniProt
Entry: A0A3B3SJ97_9TELE
LinkDB: A0A3B3SJ97_9TELE
Original site: A0A3B3SJ97_9TELE 
ID   A0A3B3SJ97_9TELE        Unreviewed;       490 AA.
AC   A0A3B3SJ97;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Ring finger protein 180 {ECO:0000313|Ensembl:ENSPKIP00000030423.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000030423.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000030423.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B3SJ97; -.
DR   STRING; 1676925.ENSPKIP00000030423; -.
DR   Ensembl; ENSPKIT00000011240.1; ENSPKIP00000030423.1; ENSPKIG00000011285.1.
DR   GeneTree; ENSGT00950000182909; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0016020; C: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:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   CDD; cd16554; RING-HC_RNF180; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR033263; RNF180.
DR   InterPro; IPR045790; RNF180_C.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46717; E3 UBIQUITIN-PROTEIN LIGASE RNF180; 1.
DR   PANTHER; PTHR46717:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF180; 1.
DR   Pfam; PF19332; RNF180_C; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        463..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          329..371
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          204..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..294
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  55149 MW;  B182349D3AE53E24 CRC64;
     MLLSPYSRLL NKSDHHVNTE CMSVYLSVYP CWSVSLSVCV SAAVCLSLSL SSSVILCVSS
     FVSPSPGQLS LHTRQSAICL VSSLLQTLPG LLFWNHKRLC HCSLVLSRPP LLHKAHIVPP
     VVLQAQWTRG KLLCPHCGAR LGGFDFMRQA SCPCGHQLTV HLSESRVDRD HRLTVFLSDT
     WAYRSRRQPR ELRPSQEVCH LEGLGLPEKT QSTAPQLMGG AEPSGLAEPS PTYRITGEET
     SPDALATTTI RQQLPSRSSM EGGGREGEEP GERRPGRRER KYMRSLRRKR RGRERGLQSQ
     WLEQQEGSTG NASSSDEDEA GRDREGLTCA VCLDIYFNPY MCRPCGHVFC EPCLRTLARS
     CPSNTPCPLC RTPISHVCFQ IELSHTSQSC FPEEYISRRQ NFQKDNCAQW PLPNCGKIFR
     ILGGFRRRAG PVSRRQFPHG PSRLDSLAFE GDSRGRRLDM DVLVVYIYSV NWLIGFIIFC
     FLCYYFFSSL
//
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