HNRPK_CHICK
ID HNRPK_CHICK Reviewed; 427 AA.
AC Q5ZIQ3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
DE Short=hnRNP K;
GN Name=HNRNPK; Synonyms=HNRPK; ORFNames=RCJMB04_24e23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously
CC to poly(C) sequences. Likely to play a role in the nuclear metabolism
CC of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich
CC sequences. Can also bind poly(C) single-stranded DNA. May play an
CC important role in p53/TP53 response to DNA damage, acting at the level
CC of both transcription activation and repression (By similarity). As
CC part of a ribonucleoprotein complex, may negatively regulate the
CC transcription of genes involved in neuronal differentiation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61978}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P61978}.
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DR EMBL; AJ720731; CAG32390.1; -; mRNA.
DR RefSeq; NP_001026556.1; NM_001031385.1.
DR AlphaFoldDB; Q5ZIQ3; -.
DR SMR; Q5ZIQ3; -.
DR BioGRID; 686119; 1.
DR STRING; 9031.ENSGALP00000023165; -.
DR PaxDb; Q5ZIQ3; -.
DR GeneID; 426516; -.
DR KEGG; gga:426516; -.
DR CTD; 426516; -.
DR VEuPathDB; HostDB:geneid_426516; -.
DR eggNOG; KOG2192; Eukaryota.
DR InParanoid; Q5ZIQ3; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; Q5ZIQ3; -.
DR PRO; PR:Q5ZIQ3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR033090; hnRNP_K.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012987; ROK_N.
DR PANTHER; PTHR10288:SF262; PTHR10288:SF262; 2.
DR Pfam; PF00013; KH_1; 3.
DR Pfam; PF08067; ROKNT; 1.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
KW Transcription regulation.
FT CHAIN 1..427
FT /note="Heterogeneous nuclear ribonucleoprotein K"
FT /id="PRO_0000288797"
FT DOMAIN 39..101
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 51..73
FT /note="1-1"
FT REPEAT 56..59
FT /note="3-1"
FT DOMAIN 117..182
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 218..223
FT /note="2-1"
FT REPEAT 230..233
FT /note="3-2"
FT REPEAT 240..243
FT /note="3-3"
FT REPEAT 268..271
FT /note="3-4"
FT REPEAT 297..302
FT /note="2-2"
FT DOMAIN 351..415
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 363..385
FT /note="1-2"
FT REPEAT 368..371
FT /note="3-5"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..385
FT /note="2 X 22 AA approximate repeats"
FT REGION 56..371
FT /note="5 X 4 AA repeats of G-X-G-G"
FT REGION 209..246
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 218..302
FT /note="2 X 6 AA approximate repeats"
FT REGION 221..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 47278 MW; 21325ADDFA421A28 CRC64;
METEQQEETF TNTETNGKRP AEDMEEEQAF KRSRNTDEMV ELRILLQSKN AGAVIGKGGK
NIKALRTDYN ASVSVPDSSG PERILSISAD TETIGEILKK IIPTLEEYQH YKGSDFDCEL
RLLIHQSLAG GIIGVKGAKI KELRENTQTT IKLFQECCPH STDRVVLIGG KPDRVVECIK
IILDLISESP IKGRAQPYDP NFYDETYDYG GFTMMFDDRR GRPVGFPMRG RGGFDRMPPN
RGGRPMPPSR RDYDDMSPRR GPPPPPPGRG GRGGSRARNL PLPPPPPPRG GDLMSYDRRG
RPGDRYDGMM MQCHVDACDD MQPPELFEGG SGYDYSYAGG RGSYGDLGGP IITTQVTIPK
DLAGSIIGKG GQRIKQIRHE SGASIKIDEP LEGSEDRIIT ITGTQDQIQN AQYLLQNSVK
QYSGKFF
