RN180_MOUSE
ID RN180_MOUSE Reviewed; 592 AA.
AC Q3U827; Q3UW39; Q80ZX1; Q8CCR1; Q9CXV6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=E3 ubiquitin-protein ligase RNF180;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 180;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF180 {ECO:0000305};
GN Name=Rnf180; Synonyms=Rines;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Epididymis, Head, Inner ear, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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).
RN [3]
RP FUNCTION, TOPOLOGY, DOMAIN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH ZIC2, AND SUBCELLULAR LOCATION.
RX PubMed=18363970; DOI=10.1111/j.1365-2443.2008.01169.x;
RA Ogawa M., Mizugishi K., Ishiguro A., Koyabu Y., Imai Y., Takahashi R.,
RA Mikoshiba K., Aruga J.;
RT "Rines/RNF180, a novel RING finger gene-encoded product, is a membrane-
RT bound ubiquitin ligase.";
RL Genes Cells 13:397-409(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which promotes polyubiquitination
CC and degradation by the proteasome pathway of ZIC2.
CC {ECO:0000269|PubMed:18363970}.
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 ZIC2. {ECO:0000269|PubMed:18363970}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18363970}; Single-pass membrane protein
CC {ECO:0000269|PubMed:18363970}. Nucleus envelope
CC {ECO:0000269|PubMed:18363970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3U827-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U827-2; Sequence=VSP_021741;
CC Name=3;
CC IsoId=Q3U827-3; Sequence=VSP_021743;
CC Name=4;
CC IsoId=Q3U827-4; Sequence=VSP_021741, VSP_021742;
CC -!- TISSUE SPECIFICITY: brain, kidney, testis and uterus. membrane protein.
CC Nucleus envelope. {ECO:0000269|PubMed:18363970}.
CC -!- DEVELOPMENTAL STAGE: Detected in the ventricular zone of the lateral
CC ventricle in brain from 13.5 dpc and 17.5 dpc embryos.
CC {ECO:0000269|PubMed:18363970}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates polyubiquitination of
CC the interacting protein. {ECO:0000269|PubMed:18363970}.
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DR EMBL; AK013941; BAB29072.1; -; mRNA.
DR EMBL; AK032259; BAC27782.1; -; mRNA.
DR EMBL; AK136632; BAE23080.1; -; mRNA.
DR EMBL; AK151379; BAE30351.1; -; mRNA.
DR EMBL; AK152404; BAE31192.1; -; mRNA.
DR EMBL; AK157911; BAE34259.1; -; mRNA.
DR EMBL; BC046775; AAH46775.1; -; mRNA.
DR EMBL; BC075700; AAH75700.1; -; mRNA.
DR CCDS; CCDS36775.1; -. [Q3U827-3]
DR CCDS; CCDS88517.1; -. [Q3U827-2]
DR CCDS; CCDS88518.1; -. [Q3U827-1]
DR RefSeq; NP_082210.1; NM_027934.2. [Q3U827-3]
DR RefSeq; XP_006517820.1; XM_006517757.2.
DR RefSeq; XP_006517822.1; XM_006517759.3. [Q3U827-1]
DR RefSeq; XP_006517823.1; XM_006517760.2. [Q3U827-1]
DR RefSeq; XP_006517824.3; XM_006517761.3.
DR RefSeq; XP_006517825.1; XM_006517762.2.
DR RefSeq; XP_011242998.1; XM_011244696.2.
DR RefSeq; XP_017171096.1; XM_017315607.1. [Q3U827-2]
DR AlphaFoldDB; Q3U827; -.
DR BioGRID; 214948; 2.
DR STRING; 10090.ENSMUSP00000064624; -.
DR iPTMnet; Q3U827; -.
DR PhosphoSitePlus; Q3U827; -.
DR PaxDb; Q3U827; -.
DR PRIDE; Q3U827; -.
DR ProteomicsDB; 300417; -. [Q3U827-1]
DR ProteomicsDB; 300418; -. [Q3U827-2]
DR ProteomicsDB; 300419; -. [Q3U827-3]
DR ProteomicsDB; 300420; -. [Q3U827-4]
DR Antibodypedia; 2028; 129 antibodies from 20 providers.
DR Ensembl; ENSMUST00000069686; ENSMUSP00000064624; ENSMUSG00000021720. [Q3U827-3]
DR Ensembl; ENSMUST00000224011; ENSMUSP00000153678; ENSMUSG00000021720. [Q3U827-3]
DR Ensembl; ENSMUST00000224662; ENSMUSP00000153506; ENSMUSG00000021720. [Q3U827-1]
DR Ensembl; ENSMUST00000226044; ENSMUSP00000153478; ENSMUSG00000021720. [Q3U827-2]
DR GeneID; 71816; -.
DR KEGG; mmu:71816; -.
DR UCSC; uc007rtr.1; mouse. [Q3U827-1]
DR UCSC; uc007rts.1; mouse. [Q3U827-2]
DR UCSC; uc007rtt.1; mouse. [Q3U827-3]
DR CTD; 285671; -.
DR MGI; MGI:1919066; Rnf180.
DR VEuPathDB; HostDB:ENSMUSG00000021720; -.
DR eggNOG; ENOG502QQJ8; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_039803_0_0_1; -.
DR InParanoid; Q3U827; -.
DR OMA; KNHNQEE; -.
DR OrthoDB; 673463at2759; -.
DR PhylomeDB; Q3U827; -.
DR TreeFam; TF328580; -.
DR BRENDA; 2.3.2.27; 3474.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 71816; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf180; mouse.
DR PRO; PR:Q3U827; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3U827; protein.
DR Bgee; ENSMUSG00000021720; Expressed in lens of camera-type eye and 190 other tissues.
DR ExpressionAtlas; Q3U827; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; IMP:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
DR GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033263; RNF180.
DR InterPro; IPR045790; RNF180_C.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46717; PTHR46717; 1.
DR Pfam; PF19332; RNF180_C; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..592
FT /note="E3 ubiquitin-protein ligase RNF180"
FT /id="PRO_0000261618"
FT TOPO_DOM 1..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ZN_FING 432..474
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 282..489
FT /note="Interaction with ZIC2"
FT /evidence="ECO:0000269|PubMed:18363970"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 46
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021741"
FT VAR_SEQ 485..592
FT /note="ELNNATKTFFTKEYLKIKQSFQKSSSAKWPLPSCRKGFHLFGGFHRRAAPVT
FT RRQFPHGAHRMDYLHFEDDSRGWWFDMDMVIIYIYSVNWVIGFVVFCFLCYFFFPF ->
FT AQAGSCGRLIPIFQRKPPR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021742"
FT VAR_SEQ 528..592
FT /note="FHRRAAPVTRRQFPHGAHRMDYLHFEDDSRGWWFDMDMVIIYIYSVNWVIGF
FT VVFCFLCYFFFPF -> KPAQRLKPCRILDTGMRYEAMEGCCLLTCSHGWRAQPAFLSH
FT SGHCLG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021743"
FT CONFLICT 266
FT /note="D -> H (in Ref. 1; BAE31192/BAE30351)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="N -> D (in Ref. 1; BAC27782)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="F -> L (in Ref. 1; BAE31192/BAE30351)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="Y -> F (in Ref. 1; BAE31192/BAE30351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 67371 MW; 4121E22EC8C9D861 CRC64;
MKRSEESTST QSPEEQTGTL HCWRCRKCIA SSGCFMTPLE TQVVEQDRHE SVDAQNTCHL
WHMNVDALPE WISCLLQKAQ WTVGKLNCPF CGARLGGFNF VSTPKCSCGQ LAAVHLCKSR
TDHQAAQGGR LMRPALKHLP HPGVPSGCDK ETLLTGGGSK TRNHWLLSMA RNSNGLGRLT
EALCLEVRAT YFEMKNEKLL FKASDPKCQP FVPQPDTGRC PSRASHRKSH SLDLNISEKL
ILLPTLYEIH RKPTAYPRLN ETGPIDLSGL ALPCSNSSCS FQSPPSFDPN MLLHRLSVAP
HETQAQRGRE CQCGLEASSV YSDHANANSL PFLMDLPSAG RSVLEASDQE EHLSQLDFLR
SASFPLGTIN HRLNNRERSK LRTLRRQQRR ERWLQKQGKY SGVGLLDHMT VSNEMSTDEE
TEFPEEKDSY MCAVCLDVYF NPYMCYPCHH IFCEPCLRTL AKDNPASTPC PLCRTIISRV
FLQTELNNAT KTFFTKEYLK IKQSFQKSSS AKWPLPSCRK GFHLFGGFHR RAAPVTRRQF
PHGAHRMDYL HFEDDSRGWW FDMDMVIIYI YSVNWVIGFV VFCFLCYFFF PF
