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DescriptionRecName: Full=E3 ubiquitin-protein ligase RNF103; EC=2.3.2.27; AltName: Full=Protein ADRG34; AltName: Full=RING finger protein 103; AltName: Full=RING-type E3 ubiquitin transferase RNF103 {ECO:0000305}; AltName: Full=Zinc finger protein 103; Short=Zfp-103;
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MyHits synonymsRN103_RAT , Q9EPZ8 , 77C5462F0EA271B5
match map segment
ipfam:zf-RING_2 ismart:RING iprf:ZF_RING_2  
Legends: 1, TRANSMEM Helical. {ECO:0000255}; 2, ZN_FING RING-type. {ECO:0000255|PROSITE- ProRule:PRU00175}; 3, ipfam:zf-RING_2 [T]; 4, ismart:RING [T]; 5, iprf:ZF_RING_2 [T].
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   10-MAY-2017, entry version 94.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   after 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-
RT   associated degradation pathway.";
RL   Biochem. Biophys. Res. Commun. 374:737-741(2008).
CC   -!- FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase,
CC       probably involved in the ER-associated protein degradation
CC       pathway. {ECO:0000250|UniProtKB:O00237}.
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DERL1 and VCP.
CC       {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
CC       chronic treatment with antidepressants.
CC       {ECO:0000269|PubMed:11071867, ECO:0000269|PubMed:18675248}.
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DR   EMBL; AF306394; AAG37065.1; -; mRNA.
DR   UniGene; Rn.45685; -.
DR   ProteinModelPortal; 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   eggNOG; ENOG41121N2; LUCA.
DR   HOGENOM; HOG000006578; -.
DR   HOVERGEN; HBG054144; -.
DR   InParanoid; Q9EPZ8; -.
DR   BRENDA; 2.3.2.B10; 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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   CDD; cd00162; RING; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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   Complete proteome; Endoplasmic reticulum; Membrane; Metal-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    682       E3 ubiquitin-protein ligase RNF103.
FT                                /FTId=PRO_0000056086.
FT   TRANSMEM      6     26       Helical. {ECO:0000255}.
FT   TRANSMEM    326    346       Helical. {ECO:0000255}.
FT   TRANSMEM    366    386       Helical. {ECO:0000255}.
FT   TRANSMEM    411    431       Helical. {ECO:0000255}.
FT   ZN_FING     618    660       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       617    660       ipfam:zf-RING_2 [T]
FT   MYHIT       618    659       ismart:RING [T]
FT   MYHIT       618    660       iprf:ZF_RING_2 [T]
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
//