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Database: UniProt
Entry: U3K547_FICAL
LinkDB: U3K547_FICAL
Original site: U3K547_FICAL 
ID   U3K547_FICAL            Unreviewed;       558 AA.
AC   U3K547;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Ring finger protein 180 {ECO:0000313|Ensembl:ENSFALP00000010151.2};
GN   Name=RNF180 {ECO:0000313|Ensembl:ENSFALP00000010151.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000010151.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000010151.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000010151.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; U3K547; -.
DR   Ensembl; ENSFALT00000010191.2; ENSFALP00000010151.2; ENSFALG00000009728.2.
DR   eggNOG; ENOG502QQJ8; Eukaryota.
DR   GeneTree; ENSGT00950000182909; -.
DR   HOGENOM; CLU_039803_0_0_1; -.
DR   Proteomes; UP000016665; Chromosome Z.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0042415; P:norepinephrine metabolic process; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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   Reference proteome {ECO:0000313|Proteomes:UP000016665};
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        532..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          397..439
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          352..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  63953 MW;  51EEA110347EA43F CRC64;
     MSNQEAGVLR CWSCTKHIAN AVFLAKCNGK ETSKITQSSA AAQNSCNVWH VSLEAIPEWV
     KCVIEKAQWK IGKLHCPFCE ACLGSFNFVC NKECSCGQLV NRHFCKTWTE HQPPFSVKLS
     KSSEKHLLLK IQSGFNKDTC HEVVNATLEI KNHGLSCPAG SNNSAGRLTE ALCLEVRTPR
     YEIESKKLPL KASCYPIKDA FTVNPFHGRS RSLDLNTRGR FVLSPVLYET CSMGTLYRGR
     NENPPAYIQG NLQLESSRKD SSSFQDLYSS SADILQNQFQ VTSITKLLHK ETESECDFEV
     TGQSSGSIIA DGSPFVINLS SPTRAVEDKQ YITHGNLVRP MSISFNQKLS KRERNKSNCL
     RRKQRRREQC LQKQPANDHL HTDDEHELRG DKESYLCAVC LDVYFNPYMC YPCHHIFCEP
     CLRMLAKDNP TSTPCPLCRT TIARVFFQTD LNNSTRSFFP VEYLNLKENF QKSNSAKWPL
     PSCKKAFRVF EAGFRRHSNT VTRRHFPHAA HRMDYMDFED DSRGWRFDMD MVIIYIYSVN
     WIIGFIVFCF LCYFFFPL
//
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