HRPK1_CAEEL
ID HRPK1_CAEEL Reviewed; 397 AA.
AC P91277; Q8I7G7; Q8I7G8; Q8I7G9; Q8T3B5;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K homolog {ECO:0000312|WormBase:F26B1.2a};
DE Short=hnRNP K {ECO:0000305};
GN Name=hrpk-1 {ECO:0000312|WormBase:F26B1.2a};
GN ORFNames=F26B1.2 {ECO:0000312|WormBase:F26B1.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15654100; DOI=10.1534/genetics.104.036137;
RA Holway A.H., Hung C., Michael W.M.;
RT "Systematic, RNA-interference-mediated identification of mus-101 modifier
RT genes in Caenorhabditis elegans.";
RL Genetics 169:1451-1460(2005).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ALG-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=31584932; DOI=10.1371/journal.pgen.1008067;
RA Li L., Veksler-Lublinsky I., Zinovyeva A.;
RT "HRPK-1, a conserved KH-domain protein, modulates microRNA activity during
RT Caenorhabditis elegans development.";
RL PLoS Genet. 15:E1008067-E1008067(2019).
CC -!- FUNCTION: RNA-binding protein which functions together with alg-1, a
CC component of the miRNA loading complex, to modulate the processing and
CC activity of specific miRNAs such as miR-58 and let-7 to regulate gene
CC expression at the post-transcriptional level during embryonic,
CC hypodermal and neuronal development (PubMed:31584932). Promotes the
CC lsy-6-mediated repression of cog-1 in uterine cells (PubMed:31584932).
CC In embryos, may play a role in the DNA damage response
CC (PubMed:15654100). {ECO:0000269|PubMed:15654100,
CC ECO:0000269|PubMed:31584932}.
CC -!- SUBUNIT: Interacts with alg-1; the interaction is direct and may be
CC strengthened through RNA-protein association.
CC {ECO:0000269|PubMed:31584932}.
CC -!- INTERACTION:
CC P91277; Q9GRY9: nova-1; NbExp=3; IntAct=EBI-320476, EBI-320508;
CC P91277; Q9XVS2: sup-46; NbExp=3; IntAct=EBI-320476, EBI-311961;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31584932}. Cytoplasm
CC {ECO:0000269|PubMed:31584932}. Note=Localizes to the cytoplasm and
CC nucleus in the germline, oocytes and early embryos (PubMed:31584932).
CC Does not localize to the cytoplasm of somatic cells (PubMed:31584932).
CC {ECO:0000269|PubMed:31584932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000312|WormBase:F26B1.2a};
CC IsoId=P91277-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F26B1.2b};
CC IsoId=P91277-2; Sequence=VSP_060454, VSP_060456, VSP_060457;
CC Name=c {ECO:0000312|WormBase:F26B1.2c};
CC IsoId=P91277-3; Sequence=VSP_060454;
CC Name=d {ECO:0000312|WormBase:F26B1.2d};
CC IsoId=P91277-4; Sequence=VSP_060454, VSP_060455, VSP_060458;
CC Name=e {ECO:0000312|WormBase:F26B1.2e};
CC IsoId=P91277-5; Sequence=VSP_060459;
CC -!- TISSUE SPECIFICITY: Expressed in gut, muscle, neuronal and hypodermal
CC tissues (PubMed:31584932). Highly expressed in the germline and oocytes
CC (PubMed:31584932). {ECO:0000269|PubMed:31584932}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout development
CC (PubMed:31584932). Highly expressed in early embryos (PubMed:31584932).
CC {ECO:0000269|PubMed:31584932}.
CC -!- DISRUPTION PHENOTYPE: Temperature sensitive with 35% embryonic
CC lethality at 20 degrees Celsius and 80% at 25 degrees Celsius
CC (PubMed:31584932). Of the surviving offspring, 30% are sterile at 20
CC degrees Celsius and 76% are sterile at 25 degrees Celsius
CC (PubMed:31584932). The majority of non-sterile animals have a reduced
CC brood size (PubMed:31584932). In addition, animals have gonadal
CC formation defects and display a bursting vulva phenotype
CC (PubMed:31584932). Reduced number of miRNAs including miR-58 in embryos
CC and L4 larvae (PubMed:31584932). Defective neuronal cell fate
CC switching, whereby fewer ASEL neurons adopt an ASER cell fate in an
CC lsy-6 mutant background (PubMed:31584932). In young adults, increased
CC number of seam cells and enhanced hypodermal development defects in the
CC double miR-48 and miR-241 mutant (PubMed:31584932). The majority of
CC mutants are embryonic lethal in a miR-35-42 mutant background
CC (PubMed:31584932). Enhanced defects in hypodermal development and alae
CC formation in a let-7 mutant background (PubMed:31584932). RNAi-mediated
CC knockdown relieves the lys-6-mediated repression of cog-1 in uterine
CC cells (PubMed:31584932). RNAi-mediated knockdown results in increased
CC sensitivity to the DNA-damage agent methyl methanesulfonate in embryos,
CC but does not disrupt the morphology of the nucleus (PubMed:15654100).
CC RNAi-mediated knockdown enhances the bursting vulva phenotype in a let-
CC 7 mutant background (PubMed:31584932). {ECO:0000269|PubMed:15654100,
CC ECO:0000269|PubMed:31584932}.
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DR EMBL; BX284601; CCD64191.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD64192.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD64193.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD64194.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD64195.1; -; Genomic_DNA.
DR PIR; T30168; T30168.
DR RefSeq; NP_491825.2; NM_059424.5.
DR RefSeq; NP_740869.1; NM_170880.4. [P91277-1]
DR RefSeq; NP_740870.2; NM_170881.4.
DR RefSeq; NP_871833.1; NM_182033.3.
DR RefSeq; NP_871834.1; NM_182034.3. [P91277-5]
DR AlphaFoldDB; P91277; -.
DR SMR; P91277; -.
DR DIP; DIP-27318N; -.
DR IntAct; P91277; 9.
DR STRING; 6239.F26B1.2a; -.
DR EPD; P91277; -.
DR PaxDb; P91277; -.
DR PeptideAtlas; P91277; -.
DR EnsemblMetazoa; F26B1.2a.1; F26B1.2a.1; WBGene00017816. [P91277-1]
DR EnsemblMetazoa; F26B1.2b.1; F26B1.2b.1; WBGene00017816. [P91277-2]
DR EnsemblMetazoa; F26B1.2b.2; F26B1.2b.2; WBGene00017816. [P91277-2]
DR EnsemblMetazoa; F26B1.2b.3; F26B1.2b.3; WBGene00017816. [P91277-2]
DR EnsemblMetazoa; F26B1.2b.4; F26B1.2b.4; WBGene00017816. [P91277-2]
DR EnsemblMetazoa; F26B1.2c.1; F26B1.2c.1; WBGene00017816. [P91277-3]
DR EnsemblMetazoa; F26B1.2d.1; F26B1.2d.1; WBGene00017816. [P91277-4]
DR EnsemblMetazoa; F26B1.2d.2; F26B1.2d.2; WBGene00017816. [P91277-4]
DR EnsemblMetazoa; F26B1.2e.1; F26B1.2e.1; WBGene00017816. [P91277-5]
DR GeneID; 172330; -.
DR KEGG; cel:CELE_F26B1.2; -.
DR UCSC; F26B1.2c.3; c. elegans.
DR CTD; 172330; -.
DR WormBase; F26B1.2a; CE09674; WBGene00017816; hrpk-1. [P91277-1]
DR WormBase; F26B1.2b; CE33057; WBGene00017816; hrpk-1. [P91277-2]
DR WormBase; F26B1.2c; CE33058; WBGene00017816; hrpk-1. [P91277-3]
DR WormBase; F26B1.2d; CE33059; WBGene00017816; hrpk-1. [P91277-4]
DR WormBase; F26B1.2e; CE33060; WBGene00017816; hrpk-1. [P91277-5]
DR eggNOG; KOG2192; Eukaryota.
DR GeneTree; ENSGT00940000153434; -.
DR HOGENOM; CLU_2401624_0_0_1; -.
DR InParanoid; P91277; -.
DR OMA; GTEQQIH; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; P91277; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:P91277; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00017816; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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 Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..397
FT /note="Heterogeneous nuclear ribonucleoprotein K homolog"
FT /id="PRO_0000448779"
FT DOMAIN 49..111
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 124..189
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 316..379
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform b, isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060454"
FT VAR_SEQ 79..88
FT /note="FNAHVQVPDS -> VSFTGILLCF (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060455"
FT VAR_SEQ 79..84
FT /note="FNAHVQ -> RLHRYC (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060456"
FT VAR_SEQ 85..397
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060457"
FT VAR_SEQ 89..397
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060458"
FT VAR_SEQ 94..397
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060459"
SQ SEQUENCE 397 AA; 42211 MW; DC00A065F2753E70 CRC64;
MMIKVGAAIN GTDSPKAMKR EHDNDDGDRT GRHKRPKTDG FTEAIQQGKF EVRLLVSSKS
AGAIIGKGGE NIKRLRAEFN AHVQVPDSNT PERVCTVTAD EKTVLNILKD VLPRLEDNFS
ERDPCEVRML VHQSHAGALI GRNGSKIKEL REKCSARLKI FTGCAPGSTD RVLITSGEQK
NVLGIIEEVM KELKEIPIKG SATPYLPAFN YDPSNISDYG GFPGNMPAGG PPNNRGPAPQ
RGGQGPPGGP RSYGGAITQG GGQRSFEAGD FQQFRGGPGP VPGYAMSAPG YPPQQGQFGA
PNNAGYGYGP GGGGPVTTAQ VTIPSDLGGT IIGRGGERIA RIRQESGAQI TLEQSNGQPE
RIITIKGTEQ QIHSAQYLLQ QCVRNSTQGR ERFGGSV
