RNF17_MOUSE
ID RNF17_MOUSE Reviewed; 1640 AA.
AC Q99MV7; Q3T4H2; Q3T4H3; Q4FZG6; Q8CDR4; Q9QXQ2;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=RING finger protein 17;
DE AltName: Full=Mad member-interacting protein 2;
DE Short=Mmip-2;
GN Name=Rnf17;
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] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP SELF-ASSOCIATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Testis;
RX PubMed=16093322; DOI=10.1242/dev.02003;
RA Pan J., Goodheart M., Chuma S., Nakatsuji N., Page D.C., Wang P.J.;
RT "RNF17, a component of the mammalian germ cell nuage, is essential for
RT spermiogenesis.";
RL Development 132:4029-4039(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-320, FUNCTION, INTERACTION WITH MXD1; MXD3;
RP MXD4 AND MXI1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10597267; DOI=10.1038/sj.onc.1203097;
RA Yin X.-Y., Gupta K., Prochownik E.V.;
RT "Mmip-2, a novel RING finger protein that interacts with mad members of the
RT Myc oncoprotein network.";
RL Oncogene 18:6621-6634(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1122 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 962-1640 (ISOFORM 2).
RC TISSUE=Oocyte;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11420703; DOI=10.1038/sj.onc.1204417;
RA Yin X.Y., Grove L.E., Prochownik E.V.;
RT "Mmip-2/Rnf-17 enhances c-Myc function and regulates some target genes in
RT common with glucocorticoid hormones.";
RL Oncogene 20:2908-2917(2001).
RN [7]
RP INTERACTION WITH PIWIL1.
RX PubMed=19584108; DOI=10.1101/gad.1814809;
RA Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT "Proteomic analysis of murine Piwi proteins reveals a role for arginine
RT methylation in specifying interaction with Tudor family members.";
RL Genes Dev. 23:1749-1762(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Seems to be involved in regulation of transcriptional
CC activity of MYC. In vitro, inhibits DNA-binding activity of Mad-MAX
CC heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3,
CC MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis.
CC {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:11420703}.
CC -!- SUBUNIT: Interacts with MXD1, MXD3, MXD4, MXI1 and PIWIL1. Self-
CC associates. {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:19584108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly found in
CC the cytoplasm. Component of a nuage in male germ cells (an electron-
CC dense spherical cytoplasmic body present in late pachytene and
CC diplotene spermatocytes and in elonging spermatids).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=RNF17L;
CC IsoId=Q99MV7-1; Sequence=Displayed;
CC Name=2; Synonyms=RNF17S;
CC IsoId=Q99MV7-2; Sequence=VSP_033080, VSP_033081;
CC Name=3;
CC IsoId=Q99MV7-3; Sequence=VSP_033077;
CC Name=4;
CC IsoId=Q99MV7-4; Sequence=VSP_033078, VSP_033079;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in adult testis. Expressed
CC in male germ cells (at protein level). Expressed at lower levels in
CC adult thyroid, submaxillary gland, ovary and epididymis.
CC {ECO:0000269|PubMed:10597267, ECO:0000269|PubMed:16093322}.
CC -!- DISRUPTION PHENOTYPE: Male mice are sterile, exhibit a complete arrest
CC in round spermatids and fail to produce sperm.
CC {ECO:0000269|PubMed:16093322}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01336.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF285585; AAK31964.1; -; mRNA.
DR EMBL; AY854010; AAX51690.1; -; mRNA.
DR EMBL; AY854011; AAX51691.1; -; mRNA.
DR EMBL; AF190166; AAF01336.1; ALT_FRAME; mRNA.
DR EMBL; AK029693; BAC26567.1; -; mRNA.
DR EMBL; BC099501; AAH99501.1; -; mRNA.
DR CCDS; CCDS27149.1; -. [Q99MV7-1]
DR RefSeq; NP_001028215.1; NM_001033043.1. [Q99MV7-1]
DR RefSeq; XP_006519173.1; XM_006519110.3.
DR RefSeq; XP_006519175.1; XM_006519112.1. [Q99MV7-3]
DR RefSeq; XP_017171542.1; XM_017316053.1.
DR AlphaFoldDB; Q99MV7; -.
DR SMR; Q99MV7; -.
DR BioGRID; 205956; 3.
DR IntAct; Q99MV7; 2.
DR MINT; Q99MV7; -.
DR STRING; 10090.ENSMUSP00000093469; -.
DR iPTMnet; Q99MV7; -.
DR PhosphoSitePlus; Q99MV7; -.
DR PaxDb; Q99MV7; -.
DR PeptideAtlas; Q99MV7; -.
DR PRIDE; Q99MV7; -.
DR ProteomicsDB; 300495; -. [Q99MV7-1]
DR ProteomicsDB; 300496; -. [Q99MV7-2]
DR ProteomicsDB; 300497; -. [Q99MV7-3]
DR ProteomicsDB; 300498; -. [Q99MV7-4]
DR Antibodypedia; 22496; 75 antibodies from 19 providers.
DR Ensembl; ENSMUST00000095793; ENSMUSP00000093469; ENSMUSG00000000365. [Q99MV7-1]
DR Ensembl; ENSMUST00000223627; ENSMUSP00000153222; ENSMUSG00000000365. [Q99MV7-4]
DR GeneID; 30054; -.
DR KEGG; mmu:30054; -.
DR UCSC; uc007ubx.1; mouse. [Q99MV7-4]
DR UCSC; uc007ubz.1; mouse. [Q99MV7-2]
DR UCSC; uc007uca.1; mouse. [Q99MV7-1]
DR UCSC; uc011zma.1; mouse. [Q99MV7-3]
DR CTD; 56163; -.
DR MGI; MGI:1353419; Rnf17.
DR VEuPathDB; HostDB:ENSMUSG00000000365; -.
DR eggNOG; KOG2039; Eukaryota.
DR eggNOG; KOG2279; Eukaryota.
DR GeneTree; ENSGT00940000157559; -.
DR HOGENOM; CLU_003202_1_0_1; -.
DR InParanoid; Q99MV7; -.
DR OMA; FYVRYVA; -.
DR OrthoDB; 117171at2759; -.
DR PhylomeDB; Q99MV7; -.
DR BioGRID-ORCS; 30054; 5 hits in 80 CRISPR screens.
DR ChiTaRS; Rnf17; mouse.
DR PRO; PR:Q99MV7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99MV7; protein.
DR Bgee; ENSMUSG00000000365; Expressed in spermatocyte and 66 other tissues.
DR ExpressionAtlas; Q99MV7; baseline and differential.
DR Genevisible; Q99MV7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 3.
DR InterPro; IPR039117; RNF17.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16442; PTHR16442; 1.
DR Pfam; PF00567; TUDOR; 5.
DR SMART; SM00333; TUDOR; 4.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..1640
FT /note="RING finger protein 17"
FT /id="PRO_0000056060"
FT DOMAIN 751..809
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 985..1044
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1246..1303
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 1496..1556
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT ZN_FING 30..73
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 348..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..580
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033077"
FT VAR_SEQ 612..626
FT /note="TEGWEKEAKVEFLKM -> VSERESDSPSKAVEF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11279525"
FT /id="VSP_033078"
FT VAR_SEQ 627..1640
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11279525"
FT /id="VSP_033079"
FT VAR_SEQ 1127..1129
FT /note="VSK -> ASS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16093322"
FT /id="VSP_033080"
FT VAR_SEQ 1130..1640
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16093322"
FT /id="VSP_033081"
FT CONFLICT 20
FT /note="S -> SGAQ (in Ref. 3; AAF01336)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="Q -> S (in Ref. 3; AAF01336)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="R -> E (in Ref. 3; AAF01336)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="K -> P (in Ref. 3; AAF01336)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Q -> L (in Ref. 3; AAF01336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1640 AA; 185600 MW; F6597E5750AE5ECC CRC64;
MAAEASSTGL ASCHLVESKS GAQGASGCQC TRCGRKVSVA SGDHHKFPCG HAFCELCLLA
PQEYTTSKCT DCEVHTTVSM NQGHYPVDGF IEEDSSLEAL PPKMVNNCSS DLEKTVDQLI
NDLEHSSSIH RNVSNPSAVM SETEEIDEAL KIAGCNFEQL SNAIKMLDST QDQTRQETHS
LTEAVEKQFD TLLASLDSRK KSLCEELIRR TDDYLSKLVT VKSYIEEKKS DLDAAMKIAK
ELRSAPSLRT YCDLTQIIRT LKLTFESELS QVSSIIPRNT PRLDINCSEA ICMFSSMGKI
EFEDSTKCYP QENEDGQNVQ KKFNNRKELC CDVYSSLEKK KVDAAVLTDE TPEPPLQAEA
PDRHLEGKKK QPTKEMVVVT SPKTIAVLPQ LGSSPDVIIE EIIEENLESC FTDDPIETSG
YPKKPPQKEQ SAPVGSKAGC PELVFVSHVI HPCHFYVRKY SQIKDATILE KKMKQVCNRS
LHLDPSDILE LGARIFVNSI KNRMWCRGII TEIIPSKTKN IRKPCSPTKF SVCEISLIQI
FMVDFGNSEV LIITGVGDTH EGPEHDGEQH ITLSDFCLLL MKSEPYSEEL LKDIPHLAHL
CSLKDIVPYN STEGWEKEAK VEFLKMVNKK AVLMKVFGEE DDVLIVDLQK PPTNKISSDM
PVSLRDALVF MELARFRSQS PRSHSEKNTT LCYHPPILPE EMTEVSVMVC HINSPTDFYL
QLMENLDFLS LLKTIEEFYK GEDGENLEIL CPLQNQACVA KFEDGIWYRA KVIGLPGHRE
VEVKYVDFGN TAKITLKDMR KIKDEFLEPP EKAIKCKLAY VEPSKKSQWS KKAKEKFEEK
TQDKFVTCSV IKILENNVLL VELFDSRAPG KSAVSINDQL VKEGLASYEA GYTLKDNSKK
HLEVWDPSPE EIITSEINNL SPLSVKSLPN ENFQSLYNKE LPVNICNVIS PEKIYVQWLL
TENLLNSLEE KMVAAYEHSE WKPVKWECDM HCAVKVPAKN QWRRGQILRM VTDKLVEVLL
YDVGVELVVN IHCLRELQEN LKTMGRLSLE CSLVDIRPTG GSDKWTATAC DCLSLHLTGA
IATIILQESN TTWPLPVKIF CRDEKGERVD VSKYLIKKGL ALRERRVSKS SNSHSPEKSL
EIPLEQGDSV VTKCFKINFD TNKKIADKVN EHKVPDSKGK KSESRSTGCY RPPAVPNTSS
FEAIVTCIGD DGTIFVVPKL SEFELIKMMD EIQSNLKCLG LLEPYSWKKG EPCAVRGSDT
LWYRGKVMEV VGGTIRVQYL DHGFTEKIPQ CHLYPILLYP DTPQFCIPCQ LYQTLPVGNT
WQPDAIELLQ ELLSKREVDI HIMELPNNSW GKLSVHLYFD GMSLSHFMAH HKYCIFEHTE
EIFKEKPRGQ NKKYEDENWK IRFEDLLLPE MEAPVLPPYL SSLLPPPEEL FAVQVKHIVS
PDEMYICLDS EDSYTQFNHH GDTDDSGVSW ESESENLEEA LQRFNKNVET FPPLTDFSSE
MPCLAEYADG LWYRAKIISI KEFNPLSVLV LFVDYGCTEK LTINRLRQIP VQLMQYPAQA
IKVLLAGFKP PLSDSGKTRI PYCPKWSMEA LWTMIDCLQG KQLYASSVAQ APEQIVTLYE
DEQYPVHMSL VEMGLADKDE
