LA_RAT
ID LA_RAT Reviewed; 415 AA.
AC P38656;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 133.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916708; DOI=10.1016/0378-1119(93)90378-g;
RA Semsei I., Troester H., Bartsch H., Schwemmle M., Igloi G.L., Bachmann M.;
RT "Isolation of rat cDNA clones coding for the autoantigen SS-B/La: detection
RT of species-specific variations.";
RL Gene 126:265-268(1993).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- INTERACTION:
CC P38656; Q5I0H3: Sumo1; NbExp=3; IntAct=EBI-15649175, EBI-7253100;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; X67859; CAA48043.1; -; mRNA.
DR PIR; JC1494; JC1494.
DR AlphaFoldDB; P38656; -.
DR SMR; P38656; -.
DR DIP; DIP-46500N; -.
DR IntAct; P38656; 4.
DR STRING; 10116.ENSRNOP00000011175; -.
DR iPTMnet; P38656; -.
DR PhosphoSitePlus; P38656; -.
DR jPOST; P38656; -.
DR PaxDb; P38656; -.
DR PRIDE; P38656; -.
DR UCSC; RGD:620804; rat.
DR RGD; 620804; Ssb.
DR eggNOG; KOG4213; Eukaryota.
DR InParanoid; P38656; -.
DR PhylomeDB; P38656; -.
DR PRO; PR:P38656; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISO:RGD.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:RGD.
DR GO; GO:0071045; P:nuclear histone mRNA catabolic process; ISO:RGD.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0042780; P:tRNA 3'-end processing; ISO:RGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; ISO:RGD.
DR GO; GO:0006409; P:tRNA export from nucleus; ISO:RGD.
DR GO; GO:0008033; P:tRNA processing; IMP:RGD.
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; 2.
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_0000207602"
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..343
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 323..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..356
FT /note="Basic residues"
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:0007744|PubMed:22673903"
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:0000250|UniProtKB:P05455"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32067"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
SQ SEQUENCE 415 AA; 47777 MW; 033FD9CC1E475F98 CRC64;
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE TMIKFNRLNR
LTTDFNVIVQ ALSKSKANLM EVSADKTKIR RSPSRPLPEV TDEYKNDVKN RSVYIKGFPT
DATLDDIKEW LDDKGQILNI QMRRTLHKTF KGSIFAVFDS IQSAKKFVDT PGQKYKDTNL
LILFKEDYFA KKNEERKQSK VEAKLKAKQE HEGRHKPGST ETRALEGKMG CLLKFSGDLD
DQTCREDFHF LFSNHGEIKW IDFVRGAKEG IILFKEKAKD ALEKARSANN GNLLLRNKKV
TWKVLEGHAE KDAMKKITDD QQESLNKWKS KGGHAARRFK GSHVFTAARR FKGRGKGNRP
AYAGAPKGRG QFQGRRTRFD DDDHRRGPVK RGIDGRDREE PASKHKKREN GARDK
