LAB_XENLA
ID LAB_XENLA Reviewed; 427 AA.
AC P28049;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Lupus La protein homolog B;
DE AltName: Full=La autoantigen homolog B;
DE AltName: Full=La ribonucleoprotein B;
GN Name=ssb-b; Synonyms=lab1;
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; X68818; CAA48716.1; -; mRNA.
DR PIR; S33817; S33817.
DR AlphaFoldDB; P28049; -.
DR SMR; P28049; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 2.
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 Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..427
FT /note="Lupus La protein homolog B"
FT /id="PRO_0000207604"
FT DOMAIN 6..98
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 110..202
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 226..348
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 193..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 315..331
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 339..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 48996 MW; 45F3146F8934A355 CRC64;
MAENGDKEQL DLDTKICEQI EYYFGDHNLP RDKFLKQQVL LDNGWVPLET MIKFNRLSKL
TTDFNIILQA LKKSKTELLE INEEKCKIRR SPAKPLPELN EDYKNSFKHR SVYIKGFPTI
TNLDEIKEWL NDKGPIENIQ MRRTLQREFK GSVFLVFNTE DGAKKFLEDK NLKYKDNDMI
ILSREEYFAK KNEERKLNKS EEKAKSKQEK EEAQKQAEDA ERKLMEERVG CLLKFSGDLD
NMTSREDLHA LFQTHGEIEW IDFSRGAKEG IVLFKMNAKE ALDKAKAANN DNLKLKGKNV
KWELIEGDAE KEALKKIMEG KQESFNKRKG RDGRKFKGKG RGGKGNDSSP RKKIQFQGKK
KTFDSSDDED DMEESESPQK VTIKAKETAG PKNGASAAPG SPKKRALDDK AEDGPAVKQS
KTEVGDQ