ID   LAA_XENLA               Reviewed;         428 AA.
AC   P28048;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   09-APR-2025, entry version 123.
DE   RecName: Full=Lupus La protein homolog A;
DE   AltName: Full=La autoantigen homolog A;
DE   AltName: Full=La ribonucleoprotein A;
GN   Name=ssb-a; Synonyms=laa1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=8510143; DOI=10.1006/jmbi.1993.1275;
RA   Scherly D., Stutz F., Lin-Marq N., Clarkson S.G.;
RT   "La proteins from Xenopus laevis. cDNA cloning and developmental
RT   expression.";
RL   J. Mol. Biol. 231:196-204(1993).
CC   -!- FUNCTION: La protein plays a role in the transcription of RNA
CC       polymerase III. It is most probably a transcription termination factor.
CC       Binds to the 3' termini of virtually all nascent polymerase III
CC       transcripts (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Barely detectable in stage I/II oocytes,
CC       accumulate in stage III/IV oocytes, then exhibit a roughly constant
CC       steady state level in mature oocytes, eggs, and early embryos.
CC   -!- PTM: Phosphorylated. {ECO:0000305}.
CC   -!- MISCELLANEOUS: There are two forms of La, LaA and LaB, in Xenopus.
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DR   EMBL; X68817; CAA48715.1; -; mRNA.
DR   PIR; S33818; S33818.
DR   RefSeq; NP_001081021.1; NM_001087552.1.
DR   AlphaFoldDB; P28048; -.
DR   SMR; P28048; -.
DR   DNASU; 394333; -.
DR   GeneID; 394333; -.
DR   KEGG; xla:394333; -.
DR   AGR; Xenbase:XB-GENE-6254453; -.
DR   CTD; 394333; -.
DR   Xenbase; XB-GENE-6254453; ssb.S.
DR   OrthoDB; 439993at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 394333; Expressed in egg cell and 19 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   FunFam; 1.10.10.10:FF:000336; lupus La protein homolog; 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:SF166; 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   Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..428
FT                   /note="Lupus La protein homolog A"
FT                   /id="PRO_0000207603"
FT   DOMAIN          7..99
FT                   /note="HTH La-type RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT   DOMAIN          111..203
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          227..349
FT                   /note="xRRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT   REGION          187..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           196..212
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           316..332
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        328..343
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..361
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..377
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  48864 MW;  AEB3A38B7D2E3EC3 CRC64;
     MAENGDKEQK LDSDTKICEQ IEYYFGDHNL PRDKFLKQQI LLDDGWVPLE TMIKFNRLSK
     LTTDFNTILQ ALKKSKTELL EINEEKCKIR RSPAKPLPEL NDEYKNSLKH KSVYIKGFPT
     SAILDDVKEW LKDKGPIENI QMRRTLQREF KGSIFIIFNT DDDAKKFLEN RNLKYKDNDM
     TVLSREEYHA KKNEERKLNK SEEKAKSKQV KKEAQKQAED AERKLVEERV GSLLKFSGDL
     DNMTSREDLH ALFQTHGDIE WIDFSRGAKE GIVLFKMNAK EALDKAKAAN SDNLKLKGKD
     VKWELIEGDT EKEALKKILE GKQESFNKRK GRDGRKFKGK GRGGKGNDSS SRKRTQFQGK
     KKTFDSSDDE DDMEESESPQ KASVKAEESA GTKNGAAAAP GSPKKRSLDD KAEDGPAVKQ
     SKTEVGDQ
//