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Database: UniProt
Entry: A0A1D5R1K1_MACMU
LinkDB: A0A1D5R1K1_MACMU
Original site: A0A1D5R1K1_MACMU 
ID   A0A1D5R1K1_MACMU        Unreviewed;       377 AA.
AC   A0A1D5R1K1; A0A1D5R2U6;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000256|ARBA:ARBA00039277};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING finger protein 34 {ECO:0000256|ARBA:ARBA00041475};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000256|ARBA:ARBA00042270};
GN   Name=RNF34 {ECO:0000313|Ensembl:ENSMMUP00000054185.1,
GN   ECO:0000313|VGNC:VGNC:76750};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000054185.1, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000054185.1}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000054185.1};
RG   Ensembl;
RL   Submitted (NOV-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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC       cytosol {ECO:0000256|ARBA:ARBA00004514}. Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}. Nucleus speckle
CC       {ECO:0000256|ARBA:ARBA00004324}.
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DR   RefSeq; XP_015008461.1; XM_015152975.1.
DR   PaxDb; 9544-ENSMMUP00000028397; -.
DR   Ensembl; ENSMMUT00000060166.2; ENSMMUP00000054185.1; ENSMMUG00000021563.4.
DR   Ensembl; ENSMMUT00000074026.2; ENSMMUP00000054631.2; ENSMMUG00000021563.4.
DR   GeneID; 700062; -.
DR   CTD; 80196; -.
DR   VEuPathDB; HostDB:ENSMMUG00000021563; -.
DR   VGNC; VGNC:76750; RNF34.
DR   GeneTree; ENSGT00390000012719; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000006718; Chromosome 11.
DR   Bgee; ENSMMUG00000021563; Expressed in fibroblast and 21 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   CDD; cd15769; FYVE_CARP1; 1.
DR   CDD; cd16706; RING-HC_CARP1; 1.
DR   Gene3D; 1.10.720.140; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR049320; CARP1_2_FYVE.
DR   InterPro; IPR049323; CARP1_FYVE.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR14879:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF34; 1.
DR   Pfam; PF21272; FYVE_CARP1-2; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          330..365
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          195..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..245
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   377 AA;  42299 MW;  5248F46A901CC119 CRC64;
     MRKAGATSMW ASCCGLLNEV MGTGAVRGQQ SGFAGATGPF RFTPNPEFST YPPAATEGPN
     IVCKACGLSF SVFRKKHVCC DCKKDFCSVC SVLQENLRRC STCHLLQETA FQRPQLMRLK
     VKDLRQYLIL RNIPIDTCRE KEDLVDLVLC HHGLGSEDDM DTSSLNSSRS QTSSFFTRSF
     FSNYTAPSAT MSSFQGELMD GDQTSRSGVP AQVQSEITSA NTEDDDDDDD EEEEEEDDDD
     EENVEDRNPG LSKERARASL SDLSSLDDVE GMSVRQLKEI LARNFVNYSG CCEKWELVEK
     VNRLYKENEE NQKSYGERLQ LQDEEDDSLC RICMDAVIDC VLLECGHMVT CTKCGKRMSE
     CPICRQYVVR AVHVFKS
//
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