Legends: 1, CONFLICT E -> V (in Ref. 1; BAA19795). {ECO:0000305}; 2, CONFLICT D -> E (in Ref. 1; BAA19795 and 2; BAA34912). {ECO:0000305}; 3, CONFLICT T -> S (in Ref. 1; BAA19795 and 2; BAA34912). {ECO:0000305}; 4, TRANSMEM Helical. {ECO:0000255}; 5, ZN_FING RING-type. {ECO:0000255|PROSITE- ProRule:PRU00175}; 6, ipfam:zf-RING_2 [T]; 7, ismart:RING [T]; 8, iprf:ZF_RING_2 [T].
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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 10-MAY-2017, entry version 116.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; 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.,
RA Kikuno R., Kuma K., Ohkubo K., Hosokawa Y., Ibata Y., Abe T.,
RA Miyata T., Matsubara K., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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: Highly expressed in the normal cerebellum but
CC not 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 UniGene; Mm.422969; -.
DR ProteinModelPortal; Q9R1W3; -.
DR SMR; Q9R1W3; -.
DR STRING; 10090.ENSMUSP00000066324; -.
DR iPTMnet; Q9R1W3; -.
DR PhosphoSitePlus; Q9R1W3; -.
DR PaxDb; Q9R1W3; -.
DR PRIDE; Q9R1W3; -.
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 eggNOG; KOG0800; Eukaryota.
DR eggNOG; ENOG41121N2; LUCA.
DR GeneTree; ENSGT00390000006413; -.
DR HOGENOM; HOG000006578; -.
DR HOVERGEN; HBG054144; -.
DR InParanoid; Q9R1W3; -.
DR KO; K15695; -.
DR OMA; GKVHWEK; -.
DR OrthoDB; EOG091G0EZD; -.
DR TreeFam; TF329229; -.
DR Reactome; R-MMU-901032; ER Quality Control Compartment (ERQC).
DR UniPathway; UPA00143; -.
DR ChiTaRS; Rnf103; mouse.
DR PRO; PR:Q9R1W3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000052656; -.
DR CleanEx; MM_RNF103; -.
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: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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
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 1 683 E3 ubiquitin-protein ligase RNF103.
FT /FTId=PRO_0000056085.
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 619 661 RING-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00175}.
FT CONFLICT 70 70 E -> V (in Ref. 1; BAA19795).
FT {ECO:0000305}.
FT CONFLICT 388 388 D -> E (in Ref. 1; BAA19795 and 2;
FT BAA34912). {ECO:0000305}.
FT CONFLICT 414 414 T -> S (in Ref. 1; BAA19795 and 2;
FT BAA34912). {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 618 661 ipfam:zf-RING_2 [T]
FT MYHIT 619 660 ismart:RING [T]
FT MYHIT 619 661 iprf:ZF_RING_2 [T]
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
//
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