LA_MOUSE
ID LA_MOUSE Reviewed; 415 AA.
AC P32067;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Lupus La protein homolog;
DE AltName: Full=La autoantigen homolog;
DE AltName: Full=La ribonucleoprotein;
GN Name=Ssb; Synonyms=Ss-b;
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 [MRNA].
RX PubMed=8454877;
RA Topfer F., Gordon T., McCluskey J.;
RT "Characterization of the mouse autoantigen La (SS-B). Identification of
RT conserved RNA-binding motifs, a putative ATP binding site and reactivity of
RT recombinant protein with poly(U) and human autoantibodies.";
RL J. Immunol. 150:3091-3100(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-11.
RA Groelz D., Bachmann M.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327 AND LYS-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase
CC III transcripts, protecting them from exonuclease digestion and
CC facilitating their folding and maturation.
CC -!- SUBUNIT: Interacts with DDX15. May interact with RUFY1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L00993; AAA39415.1; -; mRNA.
DR EMBL; BC003820; AAH03820.1; -; mRNA.
DR EMBL; Y07951; CAA69249.1; -; mRNA.
DR CCDS; CCDS16101.1; -.
DR RefSeq; NP_001103615.1; NM_001110145.1.
DR RefSeq; NP_033304.1; NM_009278.4.
DR AlphaFoldDB; P32067; -.
DR SMR; P32067; -.
DR BioGRID; 203508; 40.
DR DIP; DIP-37706N; -.
DR IntAct; P32067; 5.
DR MINT; P32067; -.
DR STRING; 10090.ENSMUSP00000088365; -.
DR iPTMnet; P32067; -.
DR PhosphoSitePlus; P32067; -.
DR SwissPalm; P32067; -.
DR EPD; P32067; -.
DR jPOST; P32067; -.
DR PaxDb; P32067; -.
DR PeptideAtlas; P32067; -.
DR PRIDE; P32067; -.
DR ProteomicsDB; 264979; -.
DR Antibodypedia; 2797; 556 antibodies from 38 providers.
DR DNASU; 20823; -.
DR Ensembl; ENSMUST00000090852; ENSMUSP00000088365; ENSMUSG00000068882.
DR Ensembl; ENSMUST00000166411; ENSMUSP00000130313; ENSMUSG00000068882.
DR GeneID; 20823; -.
DR KEGG; mmu:20823; -.
DR UCSC; uc008jyt.2; mouse.
DR CTD; 6741; -.
DR MGI; MGI:98423; Ssb.
DR VEuPathDB; HostDB:ENSMUSG00000068882; -.
DR eggNOG; KOG4213; Eukaryota.
DR GeneTree; ENSGT00830000128380; -.
DR HOGENOM; CLU_042341_0_0_1; -.
DR InParanoid; P32067; -.
DR OMA; QFERSIY; -.
DR OrthoDB; 882725at2759; -.
DR PhylomeDB; P32067; -.
DR TreeFam; TF314476; -.
DR BioGRID-ORCS; 20823; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Ssb; mouse.
DR PRO; PR:P32067; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P32067; protein.
DR Bgee; ENSMUSG00000068882; Expressed in embryonic post-anal tail and 258 other tissues.
DR ExpressionAtlas; P32067; baseline and differential.
DR Genevisible; P32067; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0071045; P:nuclear histone mRNA catabolic process; ISO:MGI.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0042780; P:tRNA 3'-end processing; ISO:MGI.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISO:MGI.
DR GO; GO:0006409; P:tRNA export from nucleus; ISO:MGI.
DR GO; GO:0008033; P:tRNA processing; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
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 Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08777; RRM_3; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..415
FT /note="Lupus La protein homolog"
FT /id="PRO_0000207600"
FT DOMAIN 7..99
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 111..187
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 226..346
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 349..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 327
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
SQ SEQUENCE 415 AA; 47756 MW; 2D75197692FDC933 CRC64;
MAENGDNEKM TALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE TMIKFNRLNR
LTTDFNVIVQ ALSKSKAKLM EVSADKTKIR RSPSRPLPEV TDEYKNDVKN RSVYIKGFPT
DATLDDIKEW LDDKGQILNI QMRRTLHKTF KGSIFAVFDS IQSAKKFVEI PGQKYKDTNL
LILFKEDYFA KKNEERKQSK VEAKLKAKQE HEGRHKPGST ETRALEGKMG CLLKFSGDLD
DQTCREDLHF LFSNHGEIKW VDFARGAKEG IILFKEKAKE ALEKARNANN GNLLLRNKKV
TWKVLEGHAE KEALKKITDD QQESLNKWKS KGGHAGGRFK GSHVFTAARR FKGKGKGNRP
GYAGAPKGRG QFHGRRTRFD DDDRRRGPMK RGRDGRDREE PASKHKKREN GARDK
