DZIP3_MOUSE
ID DZIP3_MOUSE Reviewed; 1204 AA.
AC Q7TPV2; Q148V3; Q80TU4; Q8BYK7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein ligase DZIP3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86Y13};
DE AltName: Full=DAZ-interacting protein 3 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase DZIP3 {ECO:0000305};
GN Name=Dzip3; Synonyms=Kiaa0675;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C3H/He; TISSUE=Osteoblast;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-787 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1133 (ISOFORM 1).
RC TISSUE=Head, and Retina;
RG The MGC Project Team;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1062-1204 (ISOFORM 1).
RA Tanaka T.S., Jaradat S.A., Lim M.K., Kargul G.J., Wang X., Grahovac M.J.,
RA Pantano S., Sano Y., Piao Y., Nagaraja R., Doi H., Wood W.H. III,
RA Becker K.G., Ko M.S.H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 Ubiquitin ligase proteins mediate ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. Able to specifically bind RNA.
CC {ECO:0000250|UniProtKB:Q86Y13}.
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:0000250|UniProtKB:Q86Y13};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probably interacts with DAZL. {ECO:0000250|UniProtKB:Q86Y13}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86Y13}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TPV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPV2-2; Sequence=VSP_010977;
CC Name=3;
CC IsoId=Q7TPV2-3; Sequence=VSP_010973, VSP_010974, VSP_010975,
CC VSP_010976;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65626.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122344; BAC65626.1; ALT_INIT; mRNA.
DR EMBL; BC052893; AAH52893.1; -; mRNA.
DR EMBL; BC117953; AAI17954.1; -; mRNA.
DR EMBL; BC117954; AAI17955.1; -; mRNA.
DR EMBL; AK039172; BAC30265.1; -; mRNA.
DR EMBL; BI736207; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CN535823; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BG070132; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS37353.1; -. [Q7TPV2-2]
DR CCDS; CCDS49866.1; -. [Q7TPV2-1]
DR RefSeq; NP_081617.1; NM_027341.2. [Q7TPV2-2]
DR AlphaFoldDB; Q7TPV2; -.
DR SMR; Q7TPV2; -.
DR BioGRID; 230255; 15.
DR IntAct; Q7TPV2; 2.
DR MINT; Q7TPV2; -.
DR STRING; 10090.ENSMUSP00000113344; -.
DR iPTMnet; Q7TPV2; -.
DR PhosphoSitePlus; Q7TPV2; -.
DR EPD; Q7TPV2; -.
DR MaxQB; Q7TPV2; -.
DR PaxDb; Q7TPV2; -.
DR PRIDE; Q7TPV2; -.
DR ProteomicsDB; 277659; -. [Q7TPV2-1]
DR ProteomicsDB; 277660; -. [Q7TPV2-2]
DR ProteomicsDB; 277661; -. [Q7TPV2-3]
DR Antibodypedia; 32388; 165 antibodies from 21 providers.
DR Ensembl; ENSMUST00000114516; ENSMUSP00000110161; ENSMUSG00000064061. [Q7TPV2-2]
DR GeneID; 224170; -.
DR KEGG; mmu:224170; -.
DR UCSC; uc007zjy.1; mouse. [Q7TPV2-3]
DR UCSC; uc007zjz.2; mouse. [Q7TPV2-2]
DR CTD; 9666; -.
DR MGI; MGI:1917433; Dzip3.
DR VEuPathDB; HostDB:ENSMUSG00000064061; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000161692; -.
DR InParanoid; Q7TPV2; -.
DR PhylomeDB; Q7TPV2; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 224170; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dzip3; mouse.
DR PRO; PR:Q7TPV2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q7TPV2; protein.
DR Bgee; ENSMUSG00000064061; Expressed in superior cervical ganglion and 229 other tissues.
DR ExpressionAtlas; Q7TPV2; baseline and differential.
DR Genevisible; Q7TPV2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033103; DZIP3.
DR InterPro; IPR041249; HEPN_DZIP3.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15727:SF4; PTHR15727:SF4; 1.
DR Pfam; PF19179; DUF5861; 1.
DR Pfam; PF18738; HEPN_DZIP3; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Reference proteome; RNA-binding; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1204
FT /note="E3 ubiquitin-protein ligase DZIP3"
FT /id="PRO_0000055899"
FT ZN_FING 1144..1184
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 746..861
FT /evidence="ECO:0000255"
FT COILED 906..941
FT /evidence="ECO:0000255"
FT COMPBIAS 1098..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..889
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010973"
FT VAR_SEQ 382..587
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010977"
FT VAR_SEQ 890..899
FT /note="QLARVTHMAA -> MFPLCLLFYI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010974"
FT VAR_SEQ 1135..1153
FT /note="DNEEEEEEPCVICHENLSP -> VRPNLLTVNTFRSERKRMV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010975"
FT VAR_SEQ 1154..1204
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010976"
FT CONFLICT 306
FT /note="D -> G (in Ref. 2; AAH52893)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="V -> I (in Ref. 2; AAH52893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1204 AA; 138021 MW; 9522730708DB570C CRC64;
MDSLAEEFFV SGNPDVEEQT KEETEIIAEK PVTQLDKQKM DISADPEPVN ALLEIKKVLN
PISALPKGVF PNIEKFIQED FSFQTMQREV TTHSQTGEEI VPALTLHFLI TQLEMALRNI
QASNYTAQQI NVGYYLTLLF LYGVALTERA KKEDCIEAEN KFLVMKMVIQ ESEICENFMC
LVYFGRGLLR CAQKRYNGAL LEFYKSLQEI GDTDDNWFEV DPTDDEDLPT TFKDSLNNFI
KTTESNIMKE TICSYLDCER SCEADILKNT NYKGFFQLMC SKSCCIYFHK ICWKKFKNLK
YPGESDQSFS GQKCLKEGCP GDMVRMLQCD VPGIVKILFE VVRKDEYITI ENLGASYKNL
MSLELTDTDI RPKFNLKPNT KDEVPIFKLD YNYFYHLLHI IIISGTDMVR QIFDEAMPPT
LLKKELLIHK NVLEPYYNHL WTNHPLGGSW HLLYPPNKEL PQSKQFDLCL LLALIKHLNV
FPAPRKGWDM EPPSSDLSKS ADILRLCKYR DILLSEILMN GLTELQFNSI WKKVSDILLR
LGMKQDDLDK VKENPIENIS LDYHQLSIYL GIPVPEIIQR MLSCYQQGIT LQSITGSQRL
DVEEFQNDEE DLSPPVMEYN IDVKSNTEIQ LAEINKDVAS IPSESSTESV KDLQEVKSKT
KKKKRTKSNK KDKDSEDEQV SYMVEKDDQL ETEQVDVNTL STYMKTDTSD AQEDSAAEDK
FCSLDELHIL DMVEQGSSGK ESTDFKETEK ERLAHQHQLY KLQYECEDYK RQLKTVTFRW
QENQMLIKKK EKIIVSLNQQ VAFGINKMSK LQRQIHAKDD EIKNLKDQLS LKRSQWEMEK
HNLESTVKTY LNKLNAETSR ALTAEVYFLQ CRRDFGLLHL EQTEKECLNQ LARVTHMAAS
NLESLQLKAA VDSWNAIVAD VRNKIAFLRT QYNEQINKVK QGFALSTLPP VQLPPPPPSP
EILIQQFLGR PLVKESFFRP ILTVPQMPAV CPGVISAAVQ PRPPLMPGIT WAMPTPIGDT
VSPSASLCSE PLMINWERIT DRLKTAFPQQ TRKELTDFLQ QLKDSHGKSV SRLTFDEIVY
KISQMIEPKK SESEEKSAQD GNNASPSHTA SQPNAPQDPK SAQGSATWEG DKDMDNEEEE
EEPCVICHEN LSPENLSVLP CAHKFHSQCI RPWLMQQGTC PTCRLHVLQP EEFPGHPNGQ
LPKI
