ID D3ZWU9_RAT Unreviewed; 391 AA.
AC D3ZWU9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Rmnd5a {ECO:0000313|Ensembl:ENSRNOP00000032033.4,
GN ECO:0000313|RGD:1309766};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000032033.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000032033.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000032033.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000032033.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000032033.4};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000900};
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DR RefSeq; XP_232051.4; XM_232051.9.
DR AlphaFoldDB; D3ZWU9; -.
DR SMR; D3ZWU9; -.
DR STRING; 10116.ENSRNOP00000032033; -.
DR PhosphoSitePlus; D3ZWU9; -.
DR jPOST; D3ZWU9; -.
DR PaxDb; 10116-ENSRNOP00000032033; -.
DR PeptideAtlas; D3ZWU9; -.
DR Ensembl; ENSRNOT00000038912.7; ENSRNOP00000032033.4; ENSRNOG00000028422.7.
DR UCSC; RGD:1309766; rat.
DR AGR; RGD:1309766; -.
DR RGD; 1309766; Rmnd5a.
DR eggNOG; KOG2817; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_020227_3_1_1; -.
DR InParanoid; D3ZWU9; -.
DR OMA; CRQGMDD; -.
DR OrthoDB; 208500at2759; -.
DR PhylomeDB; D3ZWU9; -.
DR TreeFam; TF315176; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000028422; Expressed in quadriceps femoris and 18 other cell types or tissues.
DR Genevisible; D3ZWU9; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16794; dRING_RMD5A; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037680; RMD5A_dRING.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR PANTHER; PTHR12170:SF5; E3 UBIQUITIN-PROTEIN TRANSFERASE RMND5A; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:D3ZWU9};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 153..210
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 336..377
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 336..377
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 391 AA; 43993 MW; A6043EBEED61FBB7 CRC64;
MDQCVTVERE LEKVLHKFSG YGQLCERGLE ELIDYTGGLK HEILQSHGQD AELSGTLSLV
LTQCCKRIKD TVQKLASDHK DIHSSVSRVG KAIDKNFDSD ISSVGIDGCW QADSQRLLNE
VMVEHFFRQG MLDVAEELCQ ESGLSVDPSQ KEPFVELNRI LEALKVRVLR PALEWAVSNR
EMLIAQNSSL EFKLHRLYFI SLLMGGTTNQ REALQYAKNF QPFALNHQKD IQVLMGSLVY
LRQGIENSPY VHLLDANQWA DICDIFTRDA CALLGLSVES PLSVSFSAGC VALPALINIK
AVIEQRQCTG VWNQKDELPI EVDLGKKCWY HSIFACPILR QQTTDNNPPM KLVCGHIISR
DALNKMFNGS KLKCPYCPME QSPGDAKQIF F
//