RN123_RAT
ID RN123_RAT Reviewed; 1318 AA.
AC D3ZXK7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=E3 ubiquitin-protein ligase RNF123;
DE EC=2.3.2.27;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 1;
DE AltName: Full=RING finger protein 123;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF123 {ECO:0000305};
GN Name=Rnf123; Synonyms=Kpc1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP19.
RX PubMed=19015242; DOI=10.1128/mcb.00329-08;
RA Lu Y., Adegoke O.A.J., Nepveu A., Nakayama K.I., Bedard N., Cheng D.,
RA Peng J., Wing S.S.;
RT "USP19 deubiquitinating enzyme supports cell proliferation by stabilizing
RT KPC1, a ubiquitin ligase for p27Kip1.";
RL Mol. Cell. Biol. 29:547-558(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-
CC mediated degradation of CDKN1B which is the cyclin-dependent kinase
CC inhibitor at the G0-G1 transition of the cell cycle. Functions also as
CC an inhibitor of innate antiviral signaling mediated by DDX58 and IFIH1
CC independently of its E3 ligase activity. Interacts with the N-terminal
CC CARD domains of DDX58 and IFIH1 and competes with the downstream
CC adapter MAVS. {ECO:0000250|UniProtKB:Q5XPI4}.
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: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with UBAC1 and CDKN1B via its N-terminal domain.
CC Interacts with DDX58 (via N-terminus) and IFIH1 (via N-terminus).
CC {ECO:0000250|UniProtKB:Q5XPI4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5XPI4}.
CC -!- PTM: Ubiquitinated, leading to its degradation. Deubiquitinated by
CC USP19, thereby stimulating CDKN1B ubiquitin-dependent degradation.
CC {ECO:0000269|PubMed:19015242}.
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DR AlphaFoldDB; D3ZXK7; -.
DR SMR; D3ZXK7; -.
DR STRING; 10116.ENSRNOP00000049507; -.
DR iPTMnet; D3ZXK7; -.
DR PhosphoSitePlus; D3ZXK7; -.
DR jPOST; D3ZXK7; -.
DR PaxDb; D3ZXK7; -.
DR PeptideAtlas; D3ZXK7; -.
DR UCSC; RGD:2301394; rat.
DR RGD; 2301394; Rnf123.
DR eggNOG; KOG2242; Eukaryota.
DR eggNOG; KOG4692; Eukaryota.
DR InParanoid; D3ZXK7; -.
DR OMA; NHQHVMG; -.
DR PhylomeDB; D3ZXK7; -.
DR TreeFam; TF313546; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:D3ZXK7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000033378; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; D3ZXK7; baseline and differential.
DR Genevisible; D3ZXK7; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd12882; SPRY_RNF123; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035773; SPRY_RNF123.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363; PTHR13363; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Methylation; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1318
FT /note="E3 ubiquitin-protein ligase RNF123"
FT /id="PRO_0000396860"
FT DOMAIN 72..252
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 1258..1296
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 459..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5XPI3"
SQ SEQUENCE 1318 AA; 149077 MW; 6FDD7EA06AD67E1D CRC64;
MTSKGAAMSF SRKSYRLTSD AEKSRVTGIV QEKLLSDYLY RIFSSPDHGT PAATSRKPLN
FHNLPEHVDQ LLQVDDEESQ GQVEGRLGPS TVVLDHTGGF EGLLLVDDDL LGVIGHSNFG
TIRSSTCVYK GKWVYEVLIS SQGLMQIGWC TINCRFNQEE GVGDTHNSYA YDGNRVRKWN
VTTTNYGKAW AAGDIVSCLI DLDDGTLSFC LNGVSLGTAF ENLSRGLGMA YFPAISLSFK
ESVAFNFGSR PLRYPVAGFR PLQDPPFADL VRAQRLLGCF QTVLSVELDP VEGRLVEKES
SEWQLHGQPT VLLTLAHIFH HFAPLLRKVY LVEAVLMSFL LGIVEKGTPE QAQSVVHQIL
DLLWLFMEDY EVQDCLKQLM MSLLRLYRFS PIVPDLGLQI HYLRLTMAVL RHEKSRKFLL
SNVLFDMLRS VVFFYIKSPL RVEEAGLKEL IPTTWWPHRS SREGRDGQEA KEETTEERQR
RRAYERGCQR LKKRIEVVEE LQVQILKLLL DNKDDNGGEA SRYIFLTKFR KFLQENASGR
GNTPVLCPPE YMVCFLHRLV SALRFYWDEY KASNPRASFS DEAYIPPQIF YNGKVDYFDL
QRLGGLLSHL RKTLKDDLAS KANIVIDPLE LQAATMDDLD EDEEPAPTAA QSWRARQRPV
QALAIGGALP LPRPGWLSSP TLGRANRFLS TAAVSLMTPR RLLSTMEKVK VRSLNVEQRT
REDIEGSHWN EGLLLGRPPE EPERPLTENS LLEVLDGTVM MYSLSVHQQL GKMVGVSDDV
NEYAMALRDT EDKLRRCPKR RKDILAELTK SQKVFSEKLD HLSRRLAWVH ATVYSQEKML
DIYWLLRVCL QTIEHGDRTG SLFAFMPEFY LSVAINSYSA LKNYFGPVHS MEELPGYEET
LTRLAAILAK HFADPRIVGT DIRDSLMQAL ASYVCYPHSL RAVERIPEEQ RIAMVRNLLA
PYEQRPWAQT NWILVRLWRG CGFGYRYTRL PHLLKTKPED ANLPSLQKPC PSTLLQQHMA
DLLRQGSDVA PSFLNSVLNQ LNWAFSEFIG MIQEIQQAAE RLERNFVDSR QLKVCATCFD
LSVSLLRVLE MTITLVPEIF LDWSRPTSEM LLRRLAQLLN QVLNRVTAER NLFDRVVTLR
LPGLESVDHY PILVAVTGIL VRLLAHGPSS ETEQATSVLL ADPCFQLRSI RYLLGQPEPL
APGSALPAPD RKRFSLQSYA DYISAEELAQ VERMLAHLTA ASAQAAAASL PTNEEDLCPI
CYAHPISAVF QPCGHKSCKA CINQHLMNNK DCFFCKATIV SVEDWDKAAS TSATSSAA
