ID   RN180_PONAB             Reviewed;         592 AA.
AC   Q5RAK3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF180;
DE            EC=2.3.2.27;
DE   AltName: Full=RING finger protein 180;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF180 {ECO:0000305};
GN   Name=RNF180;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which promotes polyubiquitination
CC       and degradation by the proteasome pathway of ZIC2.
CC       {ECO:0000250|UniProtKB:Q3U827}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with ZIC2. {ECO:0000250|UniProtKB:Q3U827}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein. Nucleus envelope {ECO:0000250|UniProtKB:Q3U827}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates polyubiquitination of
CC       the interacting protein.
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DR   EMBL; CR859012; CAH91207.1; -; mRNA.
DR   RefSeq; NP_001125710.1; NM_001132238.1.
DR   AlphaFoldDB; Q5RAK3; -.
DR   Ensembl; ENSPPYT00000018024; ENSPPYP00000017319; ENSPPYG00000015501.
DR   GeneID; 100172634; -.
DR   KEGG; pon:100172634; -.
DR   CTD; 285671; -.
DR   GeneTree; ENSGT00950000182909; -.
DR   InParanoid; Q5RAK3; -.
DR   OrthoDB; 673463at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
DR   Gene3D; 3.30.40.10; -; 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; PTHR46717; 1.
DR   Pfam; PF19332; RNF180_C; 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   Endoplasmic reticulum; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..592
FT                   /note="E3 ubiquitin-protein ligase RNF180"
FT                   /id="PRO_0000261619"
FT   TOPO_DOM        1..564
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        586..592
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         432..474
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U827"
SQ   SEQUENCE   592 AA;  68308 MW;  596D35B7B4A25615 CRC64;
     MKRSKELITK NHSQEETSIL RCWKCRKCIA SSGCFMEYFE NQVIKDKDDS VDAQNICHVW
     HMNIESLPEW ISCLIQKAQW TVGKLNCPFC GARLGGFNFV STPKCSCGQL AAVHLSKSRT
     DYQPTQAGRL MRPSVKYLSH PRVQSGCDKE VLLTGGGSKN RNHRLLNMAR NNNDPGRLTE
     ALCLEVRPTY FEMKNEKLLS KASEPKYQLF VPQLVTGRCT TRAFHRKSHS LDLNISEKLT
     LLPTLYEIRG KTTAYSRLNE TQPIDLSGLP LQSSKNSCSF QNPSSFDPGM LLQRFSVAPH
     ETQTQRGGEF QCGLEAASVY SDHTNTNNLT FLMDLPSAGR SMPEASDQEE HLSPLDFLHS
     ANFSLGSINQ RLNKRERSKL KNLRRKQRRR ERWLQKQGKY SGVGFLDHMT LNNEMSTDED
     NEYAEEKDSY ICAVCLDVYF NPYMCYPCRH IFCEPCLRTL AKDNPSSTPC PLCRTIISRV
     FFQTELNNAT KTFFTKEYLK IKQSFQKSNS AKWPLPSCRK AFHLFGGFHR HAAPVTRRQF
     PHGAHRMDYL HFEDDSRGWW FDMDMVIIYI YSVNWVIGFI VFCFLCYFFF PF