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E3 ubiquitin-protein ligase RNF13 (EC 2.3.2.27) (RING finger protein 13) (RING-type E3 ubiquitin transferase RNF13)

 RNF13_MOUSE             Reviewed;         381 AA.
O54965; O54966; Q6PEA8;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-FEB-2018, entry version 124.
RecName: Full=E3 ubiquitin-protein ligase RNF13;
EC=2.3.2.27;
AltName: Full=RING finger protein 13;
AltName: Full=RING-type E3 ubiquitin transferase RNF13 {ECO:0000305};
Flags: Precursor;
Name=Rnf13; Synonyms=Rzf;
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] (ISOFORMS 1 AND 2).
Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L.;
"The gene for a RING zinc finger protein is expressed in the inner
chick ear after noise exposure.";
Prim. Sens. Neuron 2:305-316(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Inner ear;
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 GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, TOPOGRAPHY, TISSUE SPECIFICITY,
AUTOUBIQUITINATION, GLYCOSYLATION, AND MUTAGENESIS OF CYS-266.
PubMed=19292867; DOI=10.1111/j.1742-4658.2009.06913.x;
Bocock J.P., Carmicle S., Chhotani S., Ruffolo M.R., Chu H.,
Erickson A.H.;
"The PA-TM-RING protein RING finger protein 13 is an endosomal
integral membrane E3 ubiquitin ligase whose RING finger domain is
released to the cytoplasm by proteolysis.";
FEBS J. 276:1860-1877(2009).
[6]
SUBCELLULAR LOCATION.
PubMed=20230530; DOI=10.1111/j.1600-0854.2010.01060.x;
Bocock J.P., Carmicle S., Madamba E., Erickson A.H.;
"Nuclear targeting of an endosomal E3 ubiquitin ligase.";
Traffic 11:756-766(2010).
-!- FUNCTION: E3 ubiquitin-protein ligase that may play a role in
controlling cell proliferation. {ECO:0000269|PubMed:19292867}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBCELLULAR LOCATION: Late endosome membrane; Single-pass membrane
protein. Lysosome membrane. Cytoplasm, cytosol. Nucleus inner
membrane. Note=The mature protein is subjected to extensive
proteolysis that leads to the shedding of the ectodomain into the
lumen of vesicles and the release of the C-terminal fragment into
the cytosol. Not detected in early endosomes. Treatment of the
cells with either PMA or ionomycin stabilizes the full-length
protein which relocalizes to recycling endosomes and to the inner
nuclear membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O54965-1; Sequence=Displayed;
Name=2;
IsoId=O54965-2; Sequence=VSP_005749, VSP_005750;
-!- TISSUE SPECIFICITY: Expressed in the brain, heart, kidney, liver
and spleen. Higher expression in adult tissues compared to the
embryonic counterparts. {ECO:0000269|PubMed:19292867}.
-!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
activity.
-!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:19292867}.
-!- PTM: N-glycosylated and also modified with chondroitin sulfate.
{ECO:0000269|PubMed:19292867}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF037205; AAC03770.1; -; mRNA.
EMBL; AF037206; AAC03771.1; -; mRNA.
EMBL; AK158046; BAE34334.1; -; mRNA.
EMBL; CH466530; EDL35322.1; -; Genomic_DNA.
EMBL; CH466530; EDL35326.1; -; Genomic_DNA.
EMBL; BC058182; AAH58182.1; -; mRNA.
CCDS; CCDS50913.1; -. [O54965-1]
CCDS; CCDS79910.1; -. [O54965-2]
RefSeq; NP_001106884.1; NM_001113413.2. [O54965-1]
RefSeq; NP_036013.1; NM_011883.4. [O54965-2]
RefSeq; XP_006501520.1; XM_006501457.3.
UniGene; Mm.274360; -.
UniGene; Mm.445604; -.
ProteinModelPortal; O54965; -.
SMR; O54965; -.
STRING; 10090.ENSMUSP00000049331; -.
iPTMnet; O54965; -.
PhosphoSitePlus; O54965; -.
MaxQB; O54965; -.
PaxDb; O54965; -.
PeptideAtlas; O54965; -.
PRIDE; O54965; -.
Ensembl; ENSMUST00000041826; ENSMUSP00000049331; ENSMUSG00000036503. [O54965-1]
Ensembl; ENSMUST00000199041; ENSMUSP00000142335; ENSMUSG00000036503. [O54965-2]
GeneID; 24017; -.
KEGG; mmu:24017; -.
UCSC; uc008phj.3; mouse. [O54965-1]
CTD; 11342; -.
MGI; MGI:1346341; Rnf13.
eggNOG; KOG4628; Eukaryota.
eggNOG; ENOG410Z5DF; LUCA.
GeneTree; ENSGT00760000119057; -.
HOGENOM; HOG000234362; -.
HOVERGEN; HBG063762; -.
InParanoid; O54965; -.
KO; K15692; -.
OMA; NMTESSE; -.
OrthoDB; EOG091G08WC; -.
TreeFam; TF317486; -.
UniPathway; UPA00143; -.
PRO; PR:O54965; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000036503; -.
CleanEx; MM_RNF13; -.
ExpressionAtlas; O54965; baseline and differential.
Genevisible; O54965; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF02225; PA; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Endosome;
Glycoprotein; Lysosome; Membrane; Metal-binding; Nucleus;
Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 381 E3 ubiquitin-protein ligase RNF13.
/FTId=PRO_0000056055.
TOPO_DOM 35 182 Lumenal. {ECO:0000255}.
TRANSMEM 183 203 Helical. {ECO:0000255}.
TOPO_DOM 204 381 Cytoplasmic. {ECO:0000255}.
DOMAIN 64 160 PA.
ZN_FING 240 282 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 261 268 AYHCKCVD -> GMSTHTVL (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_005749.
VAR_SEQ 269 381 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_005750.
MUTAGEN 266 266 C->A: Loss of E3 ligase activity.
{ECO:0000269|PubMed:19292867}.
CONFLICT 362 362 S -> I (in Ref. 1; AAC03770).
{ECO:0000305}.
SEQUENCE 381 AA; 42732 MW; 1E0EF4801A2C6FE8 CRC64;
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFED LPARFGYRLP
AEGLKGFLIN SKPENACEPI VPPPLKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI
VHNVDSDDLI SMGSNDIDTL KKIDIPSVFI GESSANSLKD EFTYEKGGHI ILVPELSLPL
EYYLIPFLII VGICLILIVI FMITKFVQDR HRNRRNRLRK DQLKKLPVHK FKKGDEYDVC
AICLEEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
EENQVSEHTP LLPPSASART QSFGSLSESH SHHNMTESSD YEDDDNEETD SSDADNEITD
HSVVVQLQPN GEQDYNIANT V


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