LARP6_MOUSE
ID LARP6_MOUSE Reviewed; 492 AA.
AC Q8BN59; Q8C9A3; Q8CA51; Q9CTN3; Q9D3J0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=La-related protein 6;
DE AltName: Full=Acheron;
DE Short=Achn;
DE AltName: Full=La ribonucleoprotein domain family member 6;
GN Name=Larp6;
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].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Eye, Head, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17383118; DOI=10.1016/j.gene.2007.01.033;
RA Valavanis C., Wang Z., Sun D., Vaine M., Schwartz L.M.;
RT "Acheron, a novel member of the Lupus antigen family, is induced during the
RT programmed cell death of skeletal muscles in the moth Manduca sexta.";
RL Gene 393:101-109(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Regulates the coordinated translation of type I collagen
CC alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through
CC high-affinity binding of a stem-loop structure in their 5' UTR. This
CC regulation requires VIM and MYH10 filaments, and the helicase DHX9 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the HTH domain) with VIM/vimentin. Interacts
CC (via C-terminus) with non-muscle myosin MYH10. Interacts (via C-
CC terminus) with DHX9 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC nucleus and the cytoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues. Highest expression
CC in heart and brain, intermediate in kidney, skeletal muscle and testis,
CC lowest expression in testis (at protein level).
CC {ECO:0000269|PubMed:17383118}.
CC -!- DOMAIN: The RRM domain mediates the association with collagen mRNAs
CC stem-loops. {ECO:0000250}.
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DR EMBL; AK017372; BAB30713.1; -; mRNA.
DR EMBL; AK020966; BAB32263.1; -; mRNA.
DR EMBL; AK039614; BAC30400.1; -; mRNA.
DR EMBL; AK042616; BAC31306.1; -; mRNA.
DR EMBL; AK087521; BAC39909.1; -; mRNA.
DR EMBL; BC090615; AAH90615.1; -; mRNA.
DR CCDS; CCDS23258.1; -.
DR RefSeq; NP_080511.2; NM_026235.4.
DR AlphaFoldDB; Q8BN59; -.
DR SMR; Q8BN59; -.
DR BioGRID; 212276; 1.
DR STRING; 10090.ENSMUSP00000040309; -.
DR iPTMnet; Q8BN59; -.
DR PhosphoSitePlus; Q8BN59; -.
DR MaxQB; Q8BN59; -.
DR PaxDb; Q8BN59; -.
DR PRIDE; Q8BN59; -.
DR ProteomicsDB; 265043; -.
DR Antibodypedia; 14073; 131 antibodies from 18 providers.
DR DNASU; 67557; -.
DR Ensembl; ENSMUST00000038407; ENSMUSP00000040309; ENSMUSG00000034839.
DR GeneID; 67557; -.
DR KEGG; mmu:67557; -.
DR UCSC; uc009pzh.1; mouse.
DR CTD; 55323; -.
DR MGI; MGI:1914807; Larp6.
DR VEuPathDB; HostDB:ENSMUSG00000034839; -.
DR eggNOG; KOG1855; Eukaryota.
DR GeneTree; ENSGT00940000159103; -.
DR HOGENOM; CLU_015330_1_0_1; -.
DR InParanoid; Q8BN59; -.
DR OMA; WIGGLWR; -.
DR OrthoDB; 1179659at2759; -.
DR PhylomeDB; Q8BN59; -.
DR TreeFam; TF326594; -.
DR BioGRID-ORCS; 67557; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8BN59; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BN59; protein.
DR Bgee; ENSMUSG00000034839; Expressed in pontine nuclear group and 170 other tissues.
DR Genevisible; Q8BN59; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035613; F:RNA stem-loop binding; ISO:MGI.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd12289; RRM_LARP6; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR034886; LARP6.
DR InterPro; IPR034880; LARP6_RRM.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR024642; SUZ-C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR PANTHER; PTHR22792:SF71; PTHR22792:SF71; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF12901; SUZ-C; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS51938; SUZ_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS8"
FT CHAIN 2..492
FT /note="La-related protein 6"
FT /id="PRO_0000281142"
FT DOMAIN 86..177
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 184..296
FT /note="RRM"
FT DOMAIN 427..485
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..193
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 296..302
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS8"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 58
FT /note="S -> T (in Ref. 1; BAB30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="E -> D (in Ref. 1; BAC30400)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="T -> N (in Ref. 1; BAC31306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54873 MW; AA78A6BBCADDE231 CRC64;
MAQLGEQTLP GPETTVQIRV AIQEAEDLED LEEEDEGTSA RAAGDPARYL SPGWGSASEE
EPSRGHSSAT TSGGENDRED LEPEWRPPDE ELIRKLVDQI EFYFSDENLE KDAFLLKHVR
RNKLGYVSVK LLTSFKKVKH LTRDWRTTAH ALKYSVTLEL NEDHRKVRRT TPVPLFPNEN
LPSKMLLVYD LHLSPKLWAL ATPQKNGRVQ EKVMEHLLKL FGTFGVISSV RILKPGRELP
PDIRRISSRY SQVGTQECAI VEFEEVDAAI KAHEFMVTES QSKENMKAVL IGMKPPKKKP
LKDKNHDDEA TAGTHLSRSL NKRVEELQYM GDESSANSSS DPESNPTSPM AGRRHAASNK
LSPSGHQNIF LSPNASPCSS PWSSPLAQRK GVSRKSPLAE EGRLNFSTSP EIFRKCMDYS
SDSSITPSGS PWVRRRRQAE MGTQEKSPGA SPLLSRRMQT ADGLPVGVLR LPRGPDNTRG
FHGGHERGRA CV
