UNK_CANLF
ID UNK_CANLF Reviewed; 810 AA.
AC Q6EE22;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=RING finger protein unkempt homolog;
DE AltName: Full=Zinc finger CCCH domain-containing protein 5;
GN Name=UNK; Synonyms=KIAA1753, ZC3H5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15265087; DOI=10.1111/j.1365-2052.2004.01163.x;
RA Casse C., Acland G.M., Aguirre G.D.;
RT "Cloning and mapping of canine KIAA1753.";
RL Anim. Genet. 35:358-359(2004).
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.
CC {ECO:0000250|UniProtKB:Q9C0B0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0B0}.
CC -!- SIMILARITY: Belongs to the unkempt family. {ECO:0000305}.
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DR EMBL; AY422569; AAR32135.1; -; mRNA.
DR RefSeq; NP_001003390.1; NM_001003390.1.
DR AlphaFoldDB; Q6EE22; -.
DR SMR; Q6EE22; -.
DR STRING; 9612.ENSCAFP00000007347; -.
DR PaxDb; Q6EE22; -.
DR GeneID; 444855; -.
DR KEGG; cfa:444855; -.
DR CTD; 85451; -.
DR eggNOG; KOG1100; Eukaryota.
DR eggNOG; KOG1595; Eukaryota.
DR InParanoid; Q6EE22; -.
DR OrthoDB; 720138at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990715; F:mRNA CDS binding; IBA:GO_Central.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..810
FT /note="RING finger protein unkempt homolog"
FT /id="PRO_0000213898"
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 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..723
FT /evidence="ECO:0000255"
FT COMPBIAS 242..256
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar 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:0000250|UniProtKB:Q9C0B0"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B0"
SQ SEQUENCE 810 AA; 88250 MW; AA0C7B8765FF16AF CRC64;
MSKGPGPGGS AASSAPPAAT AQVLQAQPEK PQHYTYLKEF RTEQCPLFVQ HKCTQHRPYT
CFHWHFVNQR RRRSIRRRDG TFNYSPDVYC TKYDEATGLC PEGDECPFLH RTTGDTERRY
HLRYYKTGIC IHETDSKGNC TKNGLHCAFA HGPHDLRSPV YDIRELQAME ALQNGQTTVE
GSIEGQTAGA ASHAMIEKIL SEEPRWQETA YVLGNYKTEP CKKPPRLCRQ GYACPYYHNS
KDRRRSPRKH KYRSSPCPNV KHGDEWGDPG KCENGDACQY CHTRTEQQFH PEIYKSTKCN
DMQQSGSCPR GPFCAFAHVE QPPLSDDLQP SSTVSSPTQP GPVLYMPSAA GDSVPVSPSS
PHAPDLSTLL CRNSNLGSPS NLCGSPPGSI RKPPNLEGIV FPGESGLAPG SYKKAPGFER
EDQVGAEYLK NFKCQAKLKP HSLEPRSQEQ PLLQPKQDML GILPVGSPLT SSISSSITSS
LAATPPSPAG TSSVPGMNAN ALPFYPTSDT VESVIESALD DLDLNEFGVA ALEKTFDNST
VPHPGSITIG GSLLQSSAPV NIPGSLGSSA SFHSASPSPP VSLSSHFLQQ PQGHLSQSEN
TFLGTSASHG SLGLNGMNSS IWEHFASGSF SPGTFPAFLS GPGAAELARL RQELEEANGT
IKQWEESWKQ AKQACDAWKK EAEEAGERAS AAGAECELAR EQRDALEGQV KKLQEELERL
HSGPDPQALP TFSDLEALSL STLYSLQKQL RAHLEQVDKA VFHMQSVKCL KCQEQNRAVL
PCQHAVLCEL CAEGSECPVC QPSRAHTLQS
