LARP1_CAEEL
ID LARP1_CAEEL Reviewed; 1150 AA.
AC D5MCN2; H2KZ23;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=La-related protein 1;
DE AltName: Full=La ribonucleoprotein domain family member 1;
GN Name=larp-1; ORFNames=R144.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18515547; DOI=10.1261/rna.1066008;
RA Nykamp K., Lee M.H., Kimble J.;
RT "C. elegans La-related protein, LARP-1, localizes to germline P bodies and
RT attenuates Ras-MAPK signaling during oogenesis.";
RL RNA 14:1378-1389(2008).
RN [3]
RP FUNCTION.
RX PubMed=20663921; DOI=10.1242/jcs.066761;
RA Zanin E., Pacquelet A., Scheckel C., Ciosk R., Gotta M.;
RT "LARP-1 promotes oogenesis by repressing fem-3 in the C. elegans
RT germline.";
RL J. Cell Sci. 123:2717-2724(2010).
CC -!- FUNCTION: RNA-binding protein that promotes oogenesis by repressing
CC fem-3 expression during germline development (PubMed:18515547,
CC PubMed:20663921). Binds poly-U and poly-G stretches of RNA in vitro
CC (PubMed:18515547). Regulates target RNAs expression either by
CC regulating their stability or translation (PubMed:20663921).
CC {ECO:0000269|PubMed:18515547, ECO:0000269|PubMed:20663921}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:18515547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D5MCN2-1; Sequence=Displayed;
CC Name=a;
CC IsoId=D5MCN2-2; Sequence=VSP_054252, VSP_054253, VSP_054254;
CC -!- DISRUPTION PHENOTYPE: Oogenesis defects similar to defects due to
CC hyperactive Ras-MAPK signaling. Increased mRNA levels of several
CC components of the MAPK-signaling pathway.
CC {ECO:0000269|PubMed:18515547}.
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DR EMBL; FO080694; CCD65881.2; -; Genomic_DNA.
DR EMBL; FO080694; CCD65882.1; -; Genomic_DNA.
DR RefSeq; NP_001040867.2; NM_001047402.2. [D5MCN2-2]
DR RefSeq; NP_001040868.3; NM_001047403.4. [D5MCN2-1]
DR AlphaFoldDB; D5MCN2; -.
DR SMR; D5MCN2; -.
DR BioGRID; 40913; 11.
DR STRING; 6239.R144.7b; -.
DR EPD; D5MCN2; -.
DR PaxDb; D5MCN2; -.
DR PeptideAtlas; D5MCN2; -.
DR EnsemblMetazoa; R144.7a.1; R144.7a.1; WBGene00020097. [D5MCN2-2]
DR EnsemblMetazoa; R144.7b.1; R144.7b.1; WBGene00020097. [D5MCN2-1]
DR GeneID; 175680; -.
DR KEGG; cel:CELE_R144.7; -.
DR CTD; 175680; -.
DR WormBase; R144.7a; CE44790; WBGene00020097; larp-1. [D5MCN2-2]
DR WormBase; R144.7b; CE48058; WBGene00020097; larp-1. [D5MCN2-1]
DR eggNOG; KOG2590; Eukaryota.
DR GeneTree; ENSGT00940000169209; -.
DR InParanoid; D5MCN2; -.
DR OMA; RHSEKPP; -.
DR OrthoDB; 230069at2759; -.
DR PhylomeDB; D5MCN2; -.
DR PRO; PR:D5MCN2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020097; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:0034046; F:poly(G) binding; IDA:WormBase.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 4: Predicted;
KW Alternative splicing; Cytoplasm; Differentiation; Oogenesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1150
FT /note="La-related protein 1"
FT /id="PRO_0000428732"
FT DOMAIN 573..665
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1140
FT /note="Interaction with mRNA"
FT /evidence="ECO:0000250|UniProtKB:Q6PKG0"
FT COMPBIAS 16..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..256
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_054252"
FT VAR_SEQ 316..332
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_054253"
FT VAR_SEQ 855..913
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_054254"
SQ SEQUENCE 1150 AA; 128268 MW; A9E194A231DA7F92 CRC64;
MAEKQPMLSF AKVVSGQAED ASSPSQQVQH TQDSSHSSTQ NENSQPEKQA HPPHNRREKE
NVGGRSERPR GEGKGKRRNN RKGDRKPRGE TKTEKPAEKV ATEEVKPVEI PVVLEPAPLP
AINAWFKNKE EAEAAAAAAQ KEQKSETAAD QFIITATPVV QKSSAPIPEK KRAVEPTPKQ
AAPIKEKSKS RESKKEPWKT STAPAATAPV TETVTVAATQ DWPTLAKAEL NGHVSPSNSD
DNNESSSNSQ HKTGGKMTKN SWKKVDISVD YGSKGKGAPR GNGGEKGTRR SANDEAVRRR
SGEEDSASGD EQQYWSRSKD NKSPINEMSS DRVVDSGSNG IYYQQGGTHG WKKKVNNKAG
SDMPTPPNST SPHQSESNSP EHLPKDKAPI MNGNAKNAPA ANRNGNNTST AKTGDYWHKN
GGERKEDKSQ PKAYYQRNDR FQARANPHAP PKLTAAQRKE RGPLPRWEDI EAGDDNFDYM
TLMEAQYSQY YGAPQQFEHQ LDPHQASILI QQAQQHMASF APFRPPMPML SPHLMSPPLD
RDGGVTSPVS NGEPINTAIP FAPIYNPPTA PRPVTDDTLK EYVRKQIEYY FSEENLQKDF
FLRRKMGPEG YLPVALIASF PRVRSLTEDY SLILEALKDS TKVDMSPDGL QIRAPVNPTI
WPLMPTVSGA DSLPGPSSQA PQQFRQNGPA ATAAPVESQP QASSSKPQQP EEWEEVKTRK
GKGKGRLTSG SQSTNDNKRQ PQQQQKSLQQ SGSDQPDLDF QFDNEISGGG GSAQTPKRPE
KSKKAFLSAI DSEEIGDDVI SKLIIMTPSR RTLDRTGDFS TRSQNQGEFN EEVEIGLRRY
EEELWTVPQE KDIPTSKVST ISAEQFNEMR GNEDAKKTSD EPPEIPLPSG TQPTPDSVWT
KKAKERAAAS VTVPKSPMQR RESEEQKMNR FYPISKPTAP LDAKSPRKKK TRHSEKPPVE
MPVAWVLGRE DALPAAPIGI AASSSQVPAN HPSISLLQED RFVQNVYSTW RQACLKQRKS
LGYDCAEMNT LYRFWSFFLR DNFNRNMYEE FRKLALEDAE IGSRYGIEAL FRFYSYGLEK
KFRPEIYKNF MKDVTTDVQK GELYGLEKLF AFLQRSKIAK QLVVDDYLTK ELNKYKSTDD
FRNLPQSTKK
