LA_BOVIN
ID LA_BOVIN Reviewed; 404 AA.
AC P10881; Q3ZBL2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Lupus La protein homolog;
DE AltName: Full=La autoantigen homolog;
DE AltName: Full=La ribonucleoprotein;
GN Name=SSB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2468131; DOI=10.1093/nar/17.6.2233;
RA Chan E.K.L., Sullivan K.F., Tan E.M.;
RT "Ribonucleoprotein SS-B/La belongs to a protein family with consensus
RT sequences for RNA-binding.";
RL Nucleic Acids Res. 17:2233-2244(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 in the C-terminal part of the protein.
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DR EMBL; X13698; CAA31986.1; -; mRNA.
DR EMBL; BC103234; AAI03235.1; -; mRNA.
DR PIR; S03849; S03849.
DR RefSeq; NP_788838.1; NM_176665.2.
DR AlphaFoldDB; P10881; -.
DR BMRB; P10881; -.
DR SMR; P10881; -.
DR STRING; 9913.ENSBTAP00000011484; -.
DR PaxDb; P10881; -.
DR PeptideAtlas; P10881; -.
DR PRIDE; P10881; -.
DR Ensembl; ENSBTAT00000011484; ENSBTAP00000011484; ENSBTAG00000008716.
DR GeneID; 338071; -.
DR KEGG; bta:338071; -.
DR CTD; 6741; -.
DR VEuPathDB; HostDB:ENSBTAG00000008716; -.
DR VGNC; VGNC:58554; SSB.
DR eggNOG; KOG4213; Eukaryota.
DR GeneTree; ENSGT00830000128380; -.
DR HOGENOM; CLU_042341_0_0_1; -.
DR InParanoid; P10881; -.
DR OMA; QFERSIY; -.
DR OrthoDB; 882725at2759; -.
DR TreeFam; TF314476; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000008716; Expressed in spermatocyte and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IEA:Ensembl.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IEA:Ensembl.
DR GO; GO:0071045; P:nuclear histone mRNA catabolic process; IEA:Ensembl.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0042780; P:tRNA 3'-end processing; IEA:Ensembl.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:Ensembl.
DR GO; GO:0006409; P:tRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..404
FT /note="Lupus La protein homolog"
FT /id="PRO_0000207598"
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 227..348
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 329..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..394
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 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 341
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32067"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05455"
FT CONFLICT 76
FT /note="K -> E (in Ref. 1; CAA31986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 46534 MW; B918FDB174232E06 CRC64;
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR
LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT
DAALDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFAVFDS IESAKKFVET PGQKYKDTDL
LILFKEDYFT KKNEERKQNK MEAKLRAKQE QEEKQKLAEN AEMKSLEEKI GCLLKFSGDL
DDQTCREDLH TLFSNHGEIK WIHFVRGAKE GIILFKEKAK EALDKAKEAN NGNLQLRNKE
VTWEVLEGDV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQAGS AKGKVQFQGK
KTKFDSDDER DENGASRAVK RAREETDKEP PSKQQKTENG AGDQ
