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La-related protein 6 (Acheron) (Achn) (La ribonucleoprotein domain family member 6)

 LARP6_MOUSE             Reviewed;         492 AA.
Q8BN59; Q8C9A3; Q8CA51; Q9CTN3; Q9D3J0;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 113.
RecName: Full=La-related protein 6;
AltName: Full=Acheron;
Short=Achn;
AltName: Full=La ribonucleoprotein domain family member 6;
Name=Larp6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Corpora quadrigemina, Eye, Head, and Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[4]
TISSUE SPECIFICITY.
PubMed=17383118; DOI=10.1016/j.gene.2007.01.033;
Valavanis C., Wang Z., Sun D., Vaine M., Schwartz L.M.;
"Acheron, a novel member of the Lupus antigen family, is induced
during the programmed cell death of skeletal muscles in the moth
Manduca sexta.";
Gene 393:101-109(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-58, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Regulates the coordinated translation of type I collagen
alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs
through high-affinity binding of a stem-loop structure in their 5'
UTR. This regulation requires VIM and MYH10 filaments, and the
helicase DHX9 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts (via the HTH domain) with VIM/vimentin.
Interacts (via C-terminus) with non-muscle myosin MYH10. Interacts
(via C-terminus) with DHX9 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the nucleus and the cytoplasm. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in numerous tissues. Highest
expression in heart and brain, intermediate in kidney, skeletal
muscle and testis, lowest expression in testis (at protein level).
{ECO:0000269|PubMed:17383118}.
-!- DOMAIN: The RRM domain mediates the association with collagen
mRNAs stem-loops. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AK017372; BAB30713.1; -; mRNA.
EMBL; AK020966; BAB32263.1; -; mRNA.
EMBL; AK039614; BAC30400.1; -; mRNA.
EMBL; AK042616; BAC31306.1; -; mRNA.
EMBL; AK087521; BAC39909.1; -; mRNA.
EMBL; BC090615; AAH90615.1; -; mRNA.
CCDS; CCDS23258.1; -.
RefSeq; NP_080511.2; NM_026235.4.
UniGene; Mm.44546; -.
ProteinModelPortal; Q8BN59; -.
SMR; Q8BN59; -.
STRING; 10090.ENSMUSP00000040309; -.
iPTMnet; Q8BN59; -.
PhosphoSitePlus; Q8BN59; -.
MaxQB; Q8BN59; -.
PaxDb; Q8BN59; -.
PRIDE; Q8BN59; -.
Ensembl; ENSMUST00000038407; ENSMUSP00000040309; ENSMUSG00000034839.
GeneID; 67557; -.
KEGG; mmu:67557; -.
UCSC; uc009pzh.1; mouse.
CTD; 55323; -.
MGI; MGI:1914807; Larp6.
eggNOG; KOG1855; Eukaryota.
eggNOG; ENOG4110VUA; LUCA.
GeneTree; ENSGT00830000128323; -.
HOGENOM; HOG000010108; -.
HOVERGEN; HBG070244; -.
InParanoid; Q8BN59; -.
KO; K18733; -.
OMA; TRGFHGG; -.
OrthoDB; EOG091G09LP; -.
PhylomeDB; Q8BN59; -.
TreeFam; TF326594; -.
PRO; PR:Q8BN59; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000034839; -.
CleanEx; MM_LARP6; -.
Genevisible; Q8BN59; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
GO; GO:0017022; F:myosin binding; ISO:MGI.
GO; GO:0035613; F:RNA stem-loop binding; ISO:MGI.
GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
CDD; cd12289; RRM_LARP6; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR006630; La_HTH.
InterPro; IPR034886; LARP6.
InterPro; IPR034880; LARP6_RRM.
InterPro; IPR002344; Lupus_La.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR024642; SUZ-C.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR22792:SF71; PTHR22792:SF71; 1.
Pfam; PF05383; La; 1.
Pfam; PF12901; SUZ-C; 1.
PRINTS; PR00302; LUPUSLA.
SMART; SM00715; LA; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50961; HTH_LA; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Translation regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9BRS8}.
CHAIN 2 492 La-related protein 6.
/FTId=PRO_0000281142.
DOMAIN 86 177 HTH La-type RNA-binding.
{ECO:0000255|PROSITE-ProRule:PRU00332}.
DOMAIN 184 296 RRM.
MOTIF 186 193 Nuclear export signal. {ECO:0000250}.
MOTIF 296 302 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9BRS8}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 58 58 S -> T (in Ref. 1; BAB30713).
{ECO:0000305}.
CONFLICT 107 107 E -> D (in Ref. 1; BAC30400).
{ECO:0000305}.
CONFLICT 314 314 T -> N (in Ref. 1; BAC31306).
{ECO:0000305}.
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


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