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   27-MAR-2024, entry version 157.
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; 9913-ENSBTAP00000011484; -.
DR   PeptideAtlas; P10881; -.
DR   Ensembl; ENSBTAT00000011484.5; ENSBTAP00000011484.4; ENSBTAG00000008716.6.
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; 5477115at2759; -.
DR   TreeFam; TF314476; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000008716; Expressed in spermatocyte and 104 other cell types or tissues.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0045727; P:positive regulation of translation; IBA:GO_Central.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   CDD; cd08028; LARP_3; 1.
DR   CDD; cd12291; RRM1_La; 1.
DR   CDD; cd12541; RRM2_La; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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:SF172; LUPUS LA PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR22792; LUPUS LA PROTEIN-RELATED; 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; SSF54928; RNA-binding domain, RBD; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
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
//