RNFT1_MOUSE
ID RNFT1_MOUSE Reviewed; 395 AA.
AC Q9DCN7; Q3U649; Q80X62;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase RNFT1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5M7Z0};
DE AltName: Full=RING finger and transmembrane domain-containing protein 1;
GN Name=Rnft1;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Bone marrow, and Kidney;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17074343; DOI=10.1016/j.fertnstert.2006.04.039;
RA Lin Y.H., Lin Y.M., Teng Y.N., Hsieh T.Y., Lin Y.S., Kuo P.L.;
RT "Identification of ten novel genes involved in human spermatogenesis by
RT microarray analysis of testicular tissue.";
RL Fertil. Steril. 86:1650-1658(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=27485036; DOI=10.1038/srep30955;
RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S.,
RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.;
RT "Genome-wide identification and gene expression profiling of ubiquitin
RT ligases for endoplasmic reticulum protein degradation.";
RL Sci. Rep. 6:30955-30955(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts in the endoplasmic
CC reticulum (ER)-associated degradation (ERAD) pathway, which targets
CC misfolded proteins that accumulate in the endoplasmic reticulum (ER)
CC for ubiquitination and subsequent proteasome-mediated degradation.
CC Protects cells from ER stress-induced apoptosis.
CC {ECO:0000250|UniProtKB:Q5M7Z0}.
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; Evidence={ECO:0000250|UniProtKB:Q5M7Z0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q5M7Z0}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q5M7Z0}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:17074343, ECO:0000269|PubMed:27485036}.
CC -!- DEVELOPMENTAL STAGE: Expression in testis already detected at postnatal
CC day 1 (P1), progressively increases with adult levels reached at P20.
CC {ECO:0000269|PubMed:17074343}.
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DR EMBL; AK002624; BAB22239.1; -; mRNA.
DR EMBL; AK036401; BAC29412.1; -; mRNA.
DR EMBL; AK153293; BAE31876.1; -; mRNA.
DR EMBL; AK171077; BAE42231.1; -; mRNA.
DR EMBL; AL604063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050796; AAH50796.1; -; mRNA.
DR CCDS; CCDS25200.1; -.
DR RefSeq; NP_084064.1; NM_029788.5.
DR AlphaFoldDB; Q9DCN7; -.
DR STRING; 10090.ENSMUSP00000020827; -.
DR iPTMnet; Q9DCN7; -.
DR PhosphoSitePlus; Q9DCN7; -.
DR EPD; Q9DCN7; -.
DR MaxQB; Q9DCN7; -.
DR PaxDb; Q9DCN7; -.
DR PeptideAtlas; Q9DCN7; -.
DR PRIDE; Q9DCN7; -.
DR ProteomicsDB; 300561; -.
DR Antibodypedia; 2746; 87 antibodies from 15 providers.
DR DNASU; 76892; -.
DR Ensembl; ENSMUST00000020827; ENSMUSP00000020827; ENSMUSG00000020521.
DR GeneID; 76892; -.
DR KEGG; mmu:76892; -.
DR UCSC; uc007ksl.1; mouse.
DR CTD; 51136; -.
DR MGI; MGI:1924142; Rnft1.
DR VEuPathDB; HostDB:ENSMUSG00000020521; -.
DR eggNOG; KOG0802; Eukaryota.
DR eggNOG; KOG4638; Eukaryota.
DR GeneTree; ENSGT00940000156740; -.
DR HOGENOM; CLU_039460_2_1_1; -.
DR InParanoid; Q9DCN7; -.
DR OMA; GCIHSRL; -.
DR OrthoDB; 1321151at2759; -.
DR PhylomeDB; Q9DCN7; -.
DR TreeFam; TF331930; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76892; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Rnft1; mouse.
DR PRO; PR:Q9DCN7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DCN7; protein.
DR Bgee; ENSMUSG00000020521; Expressed in spermatocyte and 252 other tissues.
DR Genevisible; Q9DCN7; MM.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044235; RNFT1/2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR15860; PTHR15860; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Endosome; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..395
FT /note="E3 ubiquitin-protein ligase RNFT1"
FT /id="PRO_0000320636"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 335..373
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..379
FT /note="Required for ubiquitin ligase activity and for
FT protection against ER stress-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q5M7Z0"
FT CONFLICT 92
FT /note="E -> K (in Ref. 3; AAH50796)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> V (in Ref. 1; BAE31876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45277 MW; ECCE50BD2E951108 CRC64;
MQASCNQLHD PPGTAHEDAA ASPCGHSRST EGSLHPGDVH IQINSGPKEY SENPSSRNPR
SGVCTCAHGC VHGRFRSYSH SEARPPDDFA TESGEHGSGS FSEFRYLFKW LQKSLPYILI
LGIKLVMQHI TGISLGIGLL TTFMYANKSI VNQVFLRERS SKLRCAWLLV FLAGSSVLLY
YTFHSQSLHY SLIFLNPTLE QLSFWEVLWI VGITDFILKF FFMGLKCLIL LVPSFIMPFK
SKGYWYMLLE ELCQYYRIFV PIPVWFRYLI SYGEFGNVTT WSLGILLALL YLILKLLDFF
GHLRTFRQVL RVFFTRPSYG VPASKRQCSD MDGICTICQA EFQKPVLLFC QHIFCEECIT
LWFNREKTCP LCRTVISECI NKWKDGATSS HLQMY
