UNKL_MOUSE
ID UNKL_MOUSE Reviewed; 727 AA.
AC Q5FWH2; Q6RUT6; Q9DBK4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative E3 ubiquitin-protein ligase UNKL;
DE EC=2.3.2.-;
DE AltName: Full=RING finger protein unkempt-like;
GN Name=Unkl;
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 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RA Brathwaite M., Waeltz P., Dudekula D., Nagaraja R.;
RT "Genomic sequence analysis in the mouse t-complex region.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 26-727 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP TISSUE SPECIFICITY (ISOFORM 3).
RX PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
RA Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
RT "The SWI/SNF protein BAF60b is ubiquitinated through a signalling process
RT involving Rac GTPase and the RING finger protein Unkempt.";
RL FEBS J. 277:1453-1464(2010).
CC -!- FUNCTION: May participate in a protein complex showing an E3 ligase
CC activity regulated by Rac1. Ubiquitination is directed towards itself
CC and possibly other substrates, such as Baf60b/Smarcd2. Intrinsic E3
CC ligase activity has not been proven. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the GTP-bound form of Rac1. Interacts with
CC Baf60b/Smarcd2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Primarily localized in the cytoplasm but has the ability to
CC shuttle between the nucleus and the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q5FWH2-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5FWH2-1; Sequence=VSP_039444;
CC Name=2;
CC IsoId=Q5FWH2-2; Sequence=VSP_039445, VSP_039446, VSP_039447;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Although this protein contains a RING domain, intrinsic E3
CC ligase activity has not been proven. {ECO:0000250}.
CC -!- PTM: Ubiquitination is enhanced by activated Rac1. The presence of the
CC RING finger domain is not essential for ubiquitination to occur (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the unkempt family. {ECO:0000305}.
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DR EMBL; AK004898; BAB23653.1; -; mRNA.
DR EMBL; AY491413; AAS21649.1; -; Genomic_DNA.
DR EMBL; BC089378; AAH89378.1; -; mRNA.
DR EMBL; BC059910; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS28510.1; -. [Q5FWH2-2]
DR CCDS; CCDS57058.1; -. [Q5FWH2-3]
DR RefSeq; NP_001183953.1; NM_001197024.1. [Q5FWH2-3]
DR RefSeq; NP_083065.1; NM_028789.3. [Q5FWH2-2]
DR RefSeq; XP_017173186.1; XM_017317697.1. [Q5FWH2-1]
DR RefSeq; XP_017173187.1; XM_017317698.1. [Q5FWH2-1]
DR AlphaFoldDB; Q5FWH2; -.
DR SMR; Q5FWH2; -.
DR BioGRID; 216531; 1.
DR IntAct; Q5FWH2; 1.
DR MINT; Q5FWH2; -.
DR iPTMnet; Q5FWH2; -.
DR PhosphoSitePlus; Q5FWH2; -.
DR EPD; Q5FWH2; -.
DR MaxQB; Q5FWH2; -.
DR PaxDb; Q5FWH2; -.
DR PRIDE; Q5FWH2; -.
DR ProteomicsDB; 275385; -. [Q5FWH2-3]
DR ProteomicsDB; 275386; -. [Q5FWH2-1]
DR ProteomicsDB; 275387; -. [Q5FWH2-2]
DR Antibodypedia; 34818; 113 antibodies from 19 providers.
DR DNASU; 74154; -.
DR Ensembl; ENSMUST00000015271; ENSMUSP00000015271; ENSMUSG00000015127. [Q5FWH2-2]
DR Ensembl; ENSMUST00000039734; ENSMUSP00000039670; ENSMUSG00000015127. [Q5FWH2-3]
DR GeneID; 74154; -.
DR KEGG; mmu:74154; -.
DR UCSC; uc008baa.2; mouse. [Q5FWH2-2]
DR UCSC; uc012ana.2; mouse. [Q5FWH2-3]
DR CTD; 64718; -.
DR MGI; MGI:1921404; Unkl.
DR VEuPathDB; HostDB:ENSMUSG00000015127; -.
DR eggNOG; KOG1100; Eukaryota.
DR GeneTree; ENSGT00940000158822; -.
DR HOGENOM; CLU_014526_1_0_1; -.
DR InParanoid; Q5FWH2; -.
DR OMA; FAHIEKS; -.
DR OrthoDB; 720138at2759; -.
DR PhylomeDB; Q5FWH2; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 74154; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Unkl; mouse.
DR PRO; PR:Q5FWH2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5FWH2; protein.
DR Bgee; ENSMUSG00000015127; Expressed in otolith organ and 209 other tissues.
DR ExpressionAtlas; Q5FWH2; baseline and differential.
DR Genevisible; Q5FWH2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR040594; Unkempt_Znf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14493; PTHR14493; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18384; zf_CCCH_5; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..727
FT /note="Putative E3 ubiquitin-protein ligase UNKL"
FT /id="PRO_0000278668"
FT ZN_FING 75..104
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 115..145
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 243..277
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 285..313
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 686..721
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..496
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039444"
FT VAR_SEQ 1..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039445"
FT VAR_SEQ 413..419
FT /note="NTVGAVI -> MRPPTLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039446"
FT VAR_SEQ 449..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039447"
FT CONFLICT 629
FT /note="K -> T (in Ref. 2; AAS21649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 79636 MW; 4A5A50A449BE9C8E CRC64;
MPSVSKAAAA ALSGSPPQTE KPTHYRYLKE FRTEQCSLFL QHKCSQHRPF TCFHWHFLNQ
RRRRPLRRRD GTFNYSPDIY CSKYDEATGL CPDGDECPYL HRTTGDTERK YHLRYYKTGT
CIHETDARGH CVKNGLHCAF AHGPLDLRPP VCDIRELQAQ EALQNGQLSG GDGVPDLQPG
VLASQAMIEK ILGEDPRWQD SNFVLGSYKT EQCPKPPRLC RQGYACPHYH NSRDRRRNPR
RFQYRSTPCP SVKHGDEWGE PSRCDGGDSC QYCHSRTEQQ FHPEIYKSTK CNDMRQTGYC
PRGPFCAFAH TEKSLAMVNE WSCRDLSSNS TSAYSSQPGS AKRKDSPSEG SQKATEDSKQ
NHLAVFSVAH PLAHSISSSV ASSLASSTGS GSSSPTTLPT LPARALPLDP AGNTVGAVIG
SALDLRLSDI NIASLDKDLE EQDLGLTGPR SLAGSAPVTI PGSLPRSPSL HSSSSLSTSP
LSSLSQSLSG PLVSSAMTPP QQPPPLRSEP ATLGSAASSY SSLGLNGVPG SIWDFVSGSF
SPSPSPILNS GPSASSSASP NSAELARVRR QLDEAKRKIR QWEESWQQVK QACDAWQREA
QEAKERARVA DSDRQLALQR KEEVEAKVKQ LQEELEGLGL SSLPGLQSLG DISDIPLPKL
HSLQSKLRLD LEAVDGVIFQ LRAKQCVACQ ERAHGTVLRP CQHRVLCEPC AASTPECPYC
KGQPLPW
