ID   RN103_RAT               Reviewed;         682 AA.
AC   Q9EPZ8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF103;
DE            EC=2.3.2.27;
DE   AltName: Full=Protein ADRG34;
DE   AltName: Full=RING finger protein 103;
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF103 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 103;
DE            Short=Zfp-103;
GN   Name=Rnf103; Synonyms=Zfp103;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=11071867; DOI=10.1006/bbrc.2000.3773;
RA   Yamada M., Yamada M., Yamazaki S., Takahashi K., Nishioka G., Kudo K.,
RA   Ozawa H., Yamada S., Kiuchi Y., Kamijima K., Higuchi T., Momose K.;
RT   "Identification of a novel gene with RING-H2 finger motif induced after
RT   chronic antidepressant treatment in rat brain.";
RL   Biochem. Biophys. Res. Commun. 278:150-157(2000).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=18675248; DOI=10.1016/j.bbrc.2008.07.126;
RA   Maruyama Y., Yamada M., Takahashi K., Yamada M.;
RT   "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated
RT   degradation pathway.";
RL   Biochem. Biophys. Res. Commun. 374:737-741(2008).
CC   -!- FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably
CC       involved in the ER-associated protein degradation pathway.
CC       {ECO:0000250|UniProtKB:O00237}.
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 DERL1 and VCP. {ECO:0000250|UniProtKB:O00237}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O00237}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:O00237}.
CC   -!- TISSUE SPECIFICITY: Expressed in different tissues including
CC       hippocampus, cerebral cortex, heart, kidney, spleen and lung.
CC       Expression is increased in hippocampus and frontal cortex after chronic
CC       treatment with antidepressants. {ECO:0000269|PubMed:11071867,
CC       ECO:0000269|PubMed:18675248}.
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DR   EMBL; AF306394; AAG37065.1; -; mRNA.
DR   AlphaFoldDB; Q9EPZ8; -.
DR   SMR; Q9EPZ8; -.
DR   STRING; 10116.ENSRNOP00000062726; -.
DR   PaxDb; Q9EPZ8; -.
DR   UCSC; RGD:620586; rat.
DR   RGD; 620586; Rnf103.
DR   eggNOG; KOG0800; Eukaryota.
DR   InParanoid; Q9EPZ8; -.
DR   BRENDA; 2.3.2.27; 5301.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9EPZ8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR042494; RNF103.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15302; PTHR15302; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..682
FT                   /note="E3 ubiquitin-protein ligase RNF103"
FT                   /id="PRO_0000056086"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         618..660
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          525..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  79019 MW;  77C5462F0EA271B5 CRC64;
     MWLKLFFLLL YFLVLFVLAR FFEAIVWYET GIFATQLVDP VALSFKKLKT ILECRGLGYS
     GLPEKKDVRE LVEKSGDLME GELYSALKEE EASESVSSTN FSGEMHFYEL VEDTKDGIWL
     VQVIANDRSP LVGKIHWEKM VKKVSRFGIR TGTFNCSSDP RYCRRRGWVR STLIMSVPQT
     STSKGKVMLK EYSGRKIEVE HIFKWITAHA ASRIKTIYNV EHLKEEWNKS DQYWVKIYLF
     ANLDQPPAFF SALSIKFTGR VEFIFVNVEN WNNKSYMTDI GIYNMPSYIL RTPEGIYRYG
     NHTGEFISLQ AMDSFLRSLQ PEVNDLFVLS LVLVNLMAWM DLFITQGATI KRFVVLISTL
     GTYNSLLIIS WLPVLGFLQL PYLDSFYEYS LRLLRYSNTT TLASWVRADW MFYSSHPALF
     LSTYLGHGLL IDYFEKKRRR SNNDEVNANN LEWLSSLWDW YTSYLFHPIA SFQNFPVDSD
     WDEDPDLFLE RLAFPDLWLH PLIPTDYIKN LPMWRFKCLG AQSEEEMSES SQDTENDSDS
     DNTDTFSSSK DVFEDKQNVH SSPGRTSRCD TEACSCANKC VSSPCERKRR SYGSHNTKED
     MEPDWLTWPA GTLHCTECVV CLENFENGCL LMGLPCGHVF HQNCIVMWLA GGRHCCPVCR
     WPSYKKKQPY AQQQPLSNDA PS