RN103_MOUSE
ID RN103_MOUSE Reviewed; 683 AA.
AC Q9R1W3; B9EHC2; O08670; O08883;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=E3 ubiquitin-protein ligase RNF103;
DE EC=2.3.2.27;
DE AltName: Full=KF-1;
DE Short=mKF-1;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9070305; DOI=10.1006/bbrc.1996.6033;
RA Yasojima K., Tsujimura A., Mizuno T., Shigeyoshi Y., Inazawa J., Kikuno R.,
RA Kuma K., Ohkubo K., Hosokawa Y., Ibata Y., Abe T., Miyata T., Matsubara K.,
RA Nakajima K., Hashimoto-Gotoh T.;
RT "Cloning of human and mouse cDNAs encoding novel zinc finger proteins
RT expressed in cerebellum and hippocampus.";
RL Biochem. Biophys. Res. Commun. 231:481-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Brain;
RA Tsujimura A., Hashimoto-Gotoh T.;
RT "Structure of mouse KF-1 genomic DNA.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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: Highly expressed in the normal cerebellum but not
CC in the cerebral cortex. {ECO:0000269|PubMed:9070305}.
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DR EMBL; D76445; BAA19795.1; -; mRNA.
DR EMBL; AB012161; BAA34912.2; -; Genomic_DNA.
DR EMBL; BC137624; AAI37625.1; -; mRNA.
DR CCDS; CCDS39508.1; -.
DR PIR; JC5393; JC5393.
DR RefSeq; NP_033569.2; NM_009543.3.
DR AlphaFoldDB; Q9R1W3; -.
DR SMR; Q9R1W3; -.
DR BioGRID; 204633; 1.
DR STRING; 10090.ENSMUSP00000066324; -.
DR iPTMnet; Q9R1W3; -.
DR PhosphoSitePlus; Q9R1W3; -.
DR PaxDb; Q9R1W3; -.
DR PRIDE; Q9R1W3; -.
DR ProteomicsDB; 299839; -.
DR Antibodypedia; 34817; 128 antibodies from 21 providers.
DR DNASU; 22644; -.
DR Ensembl; ENSMUST00000064637; ENSMUSP00000066324; ENSMUSG00000052656.
DR Ensembl; ENSMUST00000114179; ENSMUSP00000109817; ENSMUSG00000052656.
DR GeneID; 22644; -.
DR KEGG; mmu:22644; -.
DR UCSC; uc009cgv.1; mouse.
DR CTD; 7844; -.
DR MGI; MGI:109483; Rnf103.
DR VEuPathDB; HostDB:ENSMUSG00000052656; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00390000006413; -.
DR HOGENOM; CLU_031351_0_0_1; -.
DR InParanoid; Q9R1W3; -.
DR OMA; IYKTPSY; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9R1W3; -.
DR TreeFam; TF329229; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22644; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Rnf103; mouse.
DR PRO; PR:Q9R1W3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9R1W3; protein.
DR Bgee; ENSMUSG00000052656; Expressed in metanephric proximal tubule and 248 other tissues.
DR ExpressionAtlas; Q9R1W3; baseline and differential.
DR Genevisible; Q9R1W3; MM.
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:MGI.
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..683
FT /note="E3 ubiquitin-protein ligase RNF103"
FT /id="PRO_0000056085"
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 619..661
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 525..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 70
FT /note="E -> V (in Ref. 1; BAA19795)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="D -> E (in Ref. 1; BAA19795 and 2; BAA34912)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="T -> S (in Ref. 1; BAA19795 and 2; BAA34912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 79189 MW; CF307FC74CE63A54 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 PYLDSFYDYS LRLLRYSNTT TLASWVRADW MFYTSHPALF
LSTYLGHGLL IDYFEKKRRR SNNDEVNANN LEWLSSLWDW YTSYLFHPIA SFQNFPVDSD
WDEDPDLFLE RLAFPDLWLH PLIPTDYIKN LPMWRFKCLG VQSEEEMSES SQDTENDSDS
DNMDTFSSSK DIFEDKQSVV HSSPGRTSHC DTEACSCANK CESSPCERKR RSYGSHNTDE
DMEPDWLTWP AGTLHCTECV VCLENFENGC LLMGLPCGHV FHQNCIVMWL AGGRHCCPVC
RWPSYKKKQP YAQQQPLSND VPS
