UNK_MOUSE
ID UNK_MOUSE Reviewed; 810 AA.
AC Q8BL48; A2A853; Q8BVI6; Q99JZ8; Q99LL9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RING finger protein unkempt homolog;
DE AltName: Full=Zinc finger CCCH domain-containing protein 5;
GN Name=Unk; Synonyms=Kiaa1753, Zc3h5, Zc3hdc5;
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 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Medulla oblongata;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-394, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND RNA-BINDING.
RX PubMed=25737280; DOI=10.1101/gad.258483.115;
RA Murn J., Zarnack K., Yang Y.J., Durak O., Murphy E.A., Cheloufi S.,
RA Gonzalez D.M., Teplova M., Curk T., Zuber J., Patel D.J., Ule J.,
RA Luscombe N.M., Tsai L.H., Walsh C.A., Shi Y.;
RT "Control of a neuronal morphology program by an RNA-binding zinc finger
RT protein, Unkempt.";
RL Genes Dev. 29:501-512(2015).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which plays an
CC important role in the establishment and maintenance of the early
CC morphology of cortical neurons during embryonic development. Acts as a
CC translation repressor and controls a translationally regulated cell
CC morphology program to ensure proper structuring of the nervous system.
CC Translational control depends on recognition of its binding element
CC within target mRNAs which consists of a mandatory UAG trimer upstream
CC of a U/A-rich motif. Associated with polysomes (PubMed:25737280).
CC {ECO:0000269|PubMed:25737280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25737280}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BL48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BL48-2; Sequence=VSP_010274;
CC -!- DEVELOPMENTAL STAGE: First expressed at 12 dpc and then expression
CC declines postnatally. Highly expressed in the developing CNS (at
CC protein level). {ECO:0000269|PubMed:25737280}.
CC -!- SIMILARITY: Belongs to the unkempt family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98248.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129438; BAC98248.1; ALT_INIT; mRNA.
DR EMBL; AK046395; BAC32702.1; -; mRNA.
DR EMBL; AK078095; BAC37123.1; -; mRNA.
DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003195; AAH03195.1; -; mRNA.
DR EMBL; BC005545; AAH05545.1; -; mRNA.
DR EMBL; BC054452; AAH54452.1; -; mRNA.
DR CCDS; CCDS25655.1; -. [Q8BL48-1]
DR CCDS; CCDS70351.1; -. [Q8BL48-2]
DR RefSeq; NP_766157.1; NM_172569.4. [Q8BL48-1]
DR PDB; 5ELH; X-ray; 1.80 A; A/B=31-174.
DR PDB; 5ELK; X-ray; 2.30 A; A=204-335.
DR PDBsum; 5ELH; -.
DR PDBsum; 5ELK; -.
DR AlphaFoldDB; Q8BL48; -.
DR SMR; Q8BL48; -.
DR BioGRID; 229889; 263.
DR IntAct; Q8BL48; 2.
DR MINT; Q8BL48; -.
DR STRING; 10090.ENSMUSP00000021116; -.
DR iPTMnet; Q8BL48; -.
DR PhosphoSitePlus; Q8BL48; -.
DR EPD; Q8BL48; -.
DR jPOST; Q8BL48; -.
DR MaxQB; Q8BL48; -.
DR PaxDb; Q8BL48; -.
DR PRIDE; Q8BL48; -.
DR ProteomicsDB; 275388; -. [Q8BL48-1]
DR ProteomicsDB; 275389; -. [Q8BL48-2]
DR Antibodypedia; 32266; 79 antibodies from 16 providers.
DR DNASU; 217331; -.
DR Ensembl; ENSMUST00000021116; ENSMUSP00000021116; ENSMUSG00000020770. [Q8BL48-1]
DR Ensembl; ENSMUST00000106452; ENSMUSP00000102060; ENSMUSG00000020770. [Q8BL48-2]
DR GeneID; 217331; -.
DR KEGG; mmu:217331; -.
DR UCSC; uc007mjp.2; mouse. [Q8BL48-1]
DR CTD; 85451; -.
DR MGI; MGI:2442456; Unk.
DR VEuPathDB; HostDB:ENSMUSG00000020770; -.
DR eggNOG; KOG1100; Eukaryota.
DR eggNOG; KOG1595; Eukaryota.
DR GeneTree; ENSGT00940000159360; -.
DR HOGENOM; CLU_014526_1_0_1; -.
DR InParanoid; Q8BL48; -.
DR OMA; TAPVMYM; -.
DR OrthoDB; 720138at2759; -.
DR PhylomeDB; Q8BL48; -.
DR TreeFam; TF314982; -.
DR BioGRID-ORCS; 217331; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Unk; mouse.
DR PRO; PR:Q8BL48; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BL48; protein.
DR Bgee; ENSMUSG00000020770; Expressed in dorsal pancreas and 242 other tissues.
DR ExpressionAtlas; Q8BL48; baseline and differential.
DR Genevisible; Q8BL48; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990715; F:mRNA CDS binding; IDA:MGI.
DR GO; GO:1905538; F:polysome binding; IDA:MGI.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR040594; Unkempt_Znf.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14493; PTHR14493; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18384; zf_CCCH_5; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..810
FT /note="RING finger protein unkempt homolog"
FT /id="PRO_0000213900"
FT ZN_FING 84..113
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 124..154
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 215..241
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 251..285
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 293..321
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 766..801
FT /note="RING-type; degenerate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..727
FT /evidence="ECO:0000255"
FT COMPBIAS 242..256
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
FT VAR_SEQ 356..369
FT /note="VSPSSPHAPDLSAL -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010274"
FT CONFLICT 634
FT /note="T -> A (in Ref. 2; BAC37123)"
FT /evidence="ECO:0000305"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:5ELH"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5ELH"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5ELH"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5ELH"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5ELH"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5ELH"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:5ELH"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:5ELH"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5ELH"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:5ELH"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:5ELK"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5ELK"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5ELK"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:5ELK"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:5ELK"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5ELK"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5ELK"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5ELK"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5ELK"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:5ELK"
FT TURN 291..295
FT /evidence="ECO:0007829|PDB:5ELK"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:5ELK"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5ELK"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5ELK"
SQ SEQUENCE 810 AA; 88058 MW; 78BA9F07530E92B5 CRC64;
MSKGPGPGGS AASSAPPAAT AQVLQAQPEK PQHYTYLKEF RTEQCPLFVQ HKCTQHRPYT
CFHWHFVNQR RRRSIRRRDG TFNYSPDVYC TKYDEATGLC PEGDECPFLH RTTGDTERRY
HLRYYKTGIC IHETDSKGNC TKNGLHCAFA HGPHDLRSPV YDIRELQAME ALQNGQTTVE
GSIEGQSAGA ASHAMIEKIL SEEPRWQETA YVLGNYKTEP CKKPPRLCRQ GYACPYYHNS
KDRRRSPRKH KYRSSPCPNV KHGDEWGDPG KCENGDACQY CHTRTEQQFH PEIYKSTKCN
DMQQAGSCPR GPFCAFAHIE PPPLSDDVQP SSAVSSPTQP GPVLYMPSAA GDSVPVSPSS
PHAPDLSALL CRNSGLGSPS HLCSSPPGPS RKASNLEGLV FPGESSLAPG SYKKAPGFER
EDQVGAEYLK NFKCQAKLKP HSLEPRSQEQ PLLQPKQDVL GILPVGSPLT SSISSSITSS
LAATPPSPAG TNSTPGMNAN ALPFYPTSDT VESVIESALD DLDLNEFGVA ALEKTFDNSA
VPHPSSVTIG GSLLQSSAPV NIPGSLGSSA SFHSASPSPP VSLSSHFLQQ PQGHLSQSEN
TFLGTSASHG SLGLNGMNSS IWEHFASGSF SPGTSPAFLS GPGAAELARL RQELDEANGT
IKQWEESWKQ AKQACDAWKK EAEEAGERAS AAGAECELAR EQRDALELRV KKLQEELERL
HTVPEAQTLP AAPDLEALSL STLYSIQKQL RVHLEQVDKA VFHMQSVKCL KCQEQTRAVL
PCQHAVLCEL CAEGSECPVC QPSRAHALQS
