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Database: UniProt
Entry: H2MJG7_ORYLA
LinkDB: H2MJG7_ORYLA
Original site: H2MJG7_ORYLA 
ID   H2MJG7_ORYLA            Unreviewed;       271 AA.
AC   H2MJG7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   18-JUN-2025, entry version 73.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=rnf144aa {ECO:0000313|Ensembl:ENSORLP00000018813.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018813.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000018813.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018813.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000018813.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018813.2};
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC       ubiquitin-conjugating enzymes ube2l3 and ube2l6 in the form of a
CC       thioester and then directly transfers the ubiquitin to targeted
CC       substrates. {ECO:0000256|ARBA:ARBA00058293}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038342}.
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DR   AlphaFoldDB; H2MJG7; -.
DR   Ensembl; ENSORLT00000018814.2; ENSORLP00000018813.2; ENSORLG00000015013.2.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000157701; -.
DR   HOGENOM; CLU_053598_1_0_1; -.
DR   TreeFam; TF324777; -.
DR   Proteomes; UP000001038; Chromosome 22.
DR   Bgee; ENSORLG00000015013; Expressed in heart and 14 other cell types or tissues.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16777; mRING-HC-C4C4_RBR_RNF144A; 1.
DR   CDD; cd20352; Rcat_RBR_RNF144; 1.
DR   FunFam; 1.20.120.1750:FF:000006; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000051; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          16..239
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          20..66
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   271 AA;  30855 MW;  2B6C233EF56BDCF7 CRC64;
     MTTARYRPTW ELAVDPLVSC KLCLGEFPLE QMTTITQCQC VFCTLCLKQY VELLIKEGLE
     TAISCPDSAC PKRGHLQENE IECMVATDMM QRYKKLQFER EVLLDPCRTW CPSSSCQAVC
     QVKEAESPAL PQLVRCSVCT LEFCSACKAN WHPGQACQES NLPITSFLPG ENSSFYKSEE
     DDAPIKRCPK CKVYIERDEG CAQMMCKNCK HAFCWYCLES LDDDFLLIHY DKGPCRNKLG
     HSRASVIWHR TQSSICSPSG FSQLCLFRRL T
//
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