RWDD3_MOUSE
ID RWDD3_MOUSE Reviewed; 267 AA.
AC Q8VIL2; Q9CXQ2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=RWD domain-containing protein 3;
DE AltName: Full=RWD domain-containing sumoylation enhancer;
DE Short=RSUME {ECO:0000303|PubMed:22009797};
GN Name=Rwdd3; Synonyms=Rsume, X2cr1;
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].
RA Paez-Pereda M., Perez-Castro C., Carbia-Nagashima A., Stalla G.K., Arzt E.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-267.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP FUNCTION.
RX PubMed=22009797; DOI=10.1530/erc-11-0211;
RA Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M., Buchfelder M.,
RA Losa M., Stalla G.K., Arzt E., Renner U.;
RT "RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour
RT cells.";
RL Endocr. Relat. Cancer 19:13-27(2012).
CC -!- FUNCTION: Enhancer of SUMO conjugation. Via its interaction with
CC UBE2I/UBC9, increases SUMO conjugation to proteins by promoting the
CC binding of E1 and E2 enzymes, thioester linkage between SUMO and
CC UBE2I/UBC9 and transfer of SUMO to specific target proteins which
CC include HIF1A, PIAS, NFKBIA, NR3C1 and TOP1. Positively regulates the
CC NF-kappa-B signaling pathway by enhancing the sumoylation of NF-kappa-B
CC inhibitor alpha (NFKBIA), promoting its stabilization which
CC consequently leads to an increased inhibition of NF-kappa-B
CC transcriptional activity. Negatively regulates the hypoxia-inducible
CC factor-1 alpha (HIF1A) signaling pathway by increasing the sumoylation
CC of HIF1A, promoting its stabilization, transcriptional activity and the
CC expression of its target gene VEGFA during hypoxia. Has no effect on
CC ubiquitination. {ECO:0000269|PubMed:22009797}.
CC -!- SUBUNIT: Interacts with UBE2I/UBC9, NFKBIA, HIF1A and NCOA2.
CC {ECO:0000250|UniProtKB:Q9Y3V2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3V2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y3V2}. Note=Colocalizes with UBC9/UBE2I in
CC nuclear spots. {ECO:0000250}.
CC -!- DOMAIN: The RWD domain is required for the sumoylation enhancement
CC activity. {ECO:0000250}.
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DR EMBL; AF439556; AAL35585.1; -; mRNA.
DR EMBL; AK014130; BAB29171.2; -; mRNA.
DR CCDS; CCDS17798.1; -.
DR AlphaFoldDB; Q8VIL2; -.
DR SMR; Q8VIL2; -.
DR PhosphoSitePlus; Q8VIL2; -.
DR PaxDb; Q8VIL2; -.
DR PRIDE; Q8VIL2; -.
DR ProteomicsDB; 255428; -.
DR MGI; MGI:1920420; Rwdd3.
DR eggNOG; ENOG502S87K; Eukaryota.
DR InParanoid; Q8VIL2; -.
DR PhylomeDB; Q8VIL2; -.
DR Reactome; R-MMU-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR PRO; PR:Q8VIL2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VIL2; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1902073; P:positive regulation of hypoxia-inducible factor-1alpha signaling pathway; IMP:MGI.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR038840; RWDD3.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR15628; PTHR15628; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..267
FT /note="RWD domain-containing protein 3"
FT /id="PRO_0000097546"
FT DOMAIN 7..114
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 13..15
FT /note="Interaction with UBE2I/UBC9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3V2"
FT REGION 100..102
FT /note="Interaction with UBE2I/UBC9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3V2"
FT CONFLICT 121
FT /note="V -> A (in Ref. 2; BAB29171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29890 MW; E600189E342EE8F4 CRC64;
MAEEVRQELS ALAAIFCGPN EWEMLSCSET DGAVFRIHTT AEGLVGEDVP LELAFHLPVG
YPLCLPGISV TSEHLTRAQC VTAKEKLLGE ARKLVSEPMV HELVLWIQQN LRLVLSQPET
VSSHEKCTLP ESATGDDGPW MTLLRLDHMR ARTKYVKAVE KWASELRLTG RLMFMGKLIL
ILLQGDRSNI KEYLILQKTS KVDVDSSGKK CKEKMISVLS ETKVQTEHKR FLAFEVKEYS
TLEELQKEFG AAGLGELFSE CVLGLVK
