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E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.27) (Double ring-finger protein) (Dorfin) (Gametogenesis-expressed protein GEG-154) (RING finger protein 19A) (UBCM4-interacting protein 117) (UIP117) (XY body protein) (XYbp)

 RN19A_MOUSE             Reviewed;         840 AA.
P50636; Q3UGT2; Q9QUJ5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
10-OCT-2018, entry version 147.
RecName: Full=E3 ubiquitin-protein ligase RNF19A;
EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
AltName: Full=Double ring-finger protein;
Short=Dorfin;
AltName: Full=Gametogenesis-expressed protein GEG-154;
AltName: Full=RING finger protein 19A;
AltName: Full=UBCM4-interacting protein 117;
Short=UIP117;
AltName: Full=XY body protein;
Short=XYbp;
Name=Rnf19a; Synonyms=Geg-154, Rnf19, Xybp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=SWR/J; TISSUE=Testis;
PubMed=10585566; DOI=10.1016/S0925-4773(99)00223-3;
Parraga M., del Mazo J.;
"XYbp, a novel RING-finger protein, is a component of the XY body of
spermatocytes and centrosomes.";
Mech. Dev. 90:95-101(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Melanocyte;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 87-245, AND FUNCTION.
STRAIN=CD-1;
PubMed=10431818; DOI=10.1016/S0014-5793(99)00823-6;
Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
"A family of structurally related RING finger proteins interacts
specifically with the ubiquitin-conjugating enzyme UbcM4.";
FEBS Lett. 454:257-261(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 380-840, AND DEVELOPMENTAL
STAGE.
STRAIN=SWR/J; TISSUE=Ovary;
PubMed=7616504; DOI=10.1530/jrf.0.1030323;
Lopez-Alanon D.M., del Mazo J.;
"Cloning and characterization of genes expressed during gametogenesis
of female and male mice.";
J. Reprod. Fertil. 103:323-329(1995).
[6]
INTERACTION WITH VCP.
PubMed=15456787; DOI=10.1074/jbc.M406683200;
Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
Kakizuka A., Tanaka K., Sobue G.;
"Physical and functional interaction between dorfin and valosin-
containing protein that are colocalized in ubiquitylated inclusions in
neurodegenerative disorders.";
J. Biol. Chem. 279:51376-51385(2004).
-!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of
a thioester and then directly transfers the ubiquitin to targeted
substrates, such as SNCAIP or CASR. {ECO:0000250,
ECO:0000269|PubMed:10431818}.
-!- CATALYTIC ACTIVITY: [E2 ubiquitin-conjugating enzyme]-S-
ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2
ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-
N(6)-ubiquitinyl-L-lysine. {ECO:0000250|UniProtKB:O60260}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with UBE2L3 and UBE2L6. Also interacts with
transcription factor Sp1. Interacts with SNCAIP and CASR (By
similarity). Interacts with VCP. {ECO:0000250,
ECO:0000269|PubMed:15456787}.
-!- INTERACTION:
Q9Z0P7:Sufu; NbExp=3; IntAct=EBI-3508340, EBI-3508336;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10585566}.
Note=Expressed primarily in the XY body of pachytene spermatocytes
and in the centrosome of somatic and germ cells in all phases of
the cell cycle.
-!- DEVELOPMENTAL STAGE: Preferentially expressed in both sexes during
gametogenesis. {ECO:0000269|PubMed:7616504}.
-!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
interact with the E2 conjugating enzyme UBE2L3 and function like
HECT-type E3 enzymes: they bind E2s via the first RING domain, but
require an obligate trans-thiolation step during the ubiquitin
transfer, requiring a conserved cysteine residue in the second
RING domain. {ECO:0000250|UniProtKB:O60260}.
-!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA50643.1; Type=Frameshift; Positions=778; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF120206; AAF18302.1; -; mRNA.
EMBL; AF120207; AAF18303.1; -; mRNA.
EMBL; AK147768; BAE28125.1; -; mRNA.
EMBL; BC040769; AAH40769.1; -; mRNA.
EMBL; AF360999; AAK51469.1; -; mRNA.
EMBL; AF071560; AAG37798.1; -; Genomic_DNA.
EMBL; X71642; CAA50643.1; ALT_FRAME; mRNA.
CCDS; CCDS27427.1; -.
PIR; I48361; I48361.
RefSeq; NP_038951.1; NM_013923.2.
UniGene; Mm.5181; -.
ProteinModelPortal; P50636; -.
SMR; P50636; -.
BioGrid; 206022; 5.
IntAct; P50636; 4.
STRING; 10090.ENSMUSP00000022890; -.
iPTMnet; P50636; -.
PhosphoSitePlus; P50636; -.
MaxQB; P50636; -.
PaxDb; P50636; -.
PRIDE; P50636; -.
Ensembl; ENSMUST00000022890; ENSMUSP00000022890; ENSMUSG00000022280.
GeneID; 30945; -.
KEGG; mmu:30945; -.
UCSC; uc007vmq.1; mouse.
CTD; 25897; -.
MGI; MGI:1353623; Rnf19a.
eggNOG; KOG1815; Eukaryota.
eggNOG; ENOG410XP9Y; LUCA.
GeneTree; ENSGT00840000129738; -.
HOGENOM; HOG000059258; -.
HOVERGEN; HBG052073; -.
InParanoid; P50636; -.
KO; K11972; -.
OMA; SNMKINE; -.
OrthoDB; EOG091G0503; -.
PhylomeDB; P50636; -.
TreeFam; TF324777; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Rnf19a; mouse.
PRO; PR:P50636; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022280; Expressed in 255 organ(s), highest expression level in testis.
CleanEx; MM_RNF19A; -.
Genevisible; P50636; MM.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR031127; E3_UB_ligase_RBR.
InterPro; IPR002867; IBR_dom.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR11685; PTHR11685; 1.
Pfam; PF01485; IBR; 2.
SMART; SM00647; IBR; 2.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 840 E3 ubiquitin-protein ligase RNF19A.
/FTId=PRO_0000056062.
TRANSMEM 368 388 Helical. {ECO:0000255}.
TRANSMEM 424 444 Helical. {ECO:0000255}.
ZN_FING 132 179 RING-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 199 264 IBR-type.
ZN_FING 301 332 RING-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 660 840 Interaction with CASR. {ECO:0000250}.
ACT_SITE 316 316 {ECO:0000250|UniProtKB:Q9Y4X5}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NV58}.
CONFLICT 207 207 R -> G (in Ref. 2; BAE28125).
{ECO:0000305}.
CONFLICT 466 466 N -> D (in Ref. 2; BAE28125).
{ECO:0000305}.
SEQUENCE 840 AA; 90632 MW; AC117A35849C023A CRC64;
MQEQEISFIF KYNEGLCMNI DSDSILMSIL DMSLHQQMGS DRDLQSSTSS VSLPSVKKAP
KQRRISIGSL FRRKKDSKRK SRELNGGVDG IASIESIHSE MCADKNSIFS TNTSSDNGLT
SISKQIGDFI ECPLCLLRHS KDRFPDIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT
ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT
CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK
ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAIAGGV
TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI
NVGGTNAAID TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGTIRD NLSETASTMA
LAGASITGSL SGSAMVNCFN RLEVQADVQK ERCSLSGESG TVSLGTVSDN ASTKAMAGSI
LNSYIPLDRE GNSMEVQVDI ESKPFKFRHN SGSSSVDDSG ATRGHTGGAS SGLPEGKSSA
TKWSKEATGG KKSKSGKLRK KGNMKINETR EDMDAQLLEQ QSTNSSEFEA PSLSDSMPSV
ADSHSSHFSE FSCSDLESMR TSCSHGSSDC HARFTAVNTL PEVENDRLEN SPHQCSSALL
SKAASCSDVP QPSHAADEHG TSRSGGKPMV DLCFGDALRE TNNNHSHQTA DLKVAVQTEI


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