ID   SLU7_XENLA              Reviewed;         580 AA.
AC   Q3KQD1; Q6INW6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Pre-mRNA-splicing factor SLU7;
GN   Name=slu7;
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 [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome. Participates in the second catalytic step of pre-mRNA
CC       splicing, when the free hydroxyl group of exon I attacks the 3'-splice
CC       site to generate spliced mRNA and the excised lariat intron. Required
CC       for holding exon 1 properly in the spliceosome and for correct AG
CC       identification when more than one possible AG exists in 3'-splicing
CC       site region. May be involved in the activation of proximal AG. Probably
CC       also involved in alternative splicing regulation.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SUBUNIT: Component of pre-catalytic, catalytic and post-catalytic
CC       spliceosomes. Associates with the spliceosome prior to recognition of
CC       the 3'-splice site for step II, probably during catalysis of step I.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95391}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:O95391}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O95391}. Note=Predominantly nuclear.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72156.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI06271.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC072156; AAH72156.1; ALT_INIT; mRNA.
DR   EMBL; BC106270; AAI06271.1; ALT_FRAME; mRNA.
DR   RefSeq; XP_018107530.1; XM_018252041.1.
DR   RefSeq; XP_018107531.1; XM_018252042.1.
DR   AlphaFoldDB; Q3KQD1; -.
DR   SMR; Q3KQD1; -.
DR   IntAct; Q3KQD1; 1.
DR   PRIDE; Q3KQD1; -.
DR   GeneID; 432205; -.
DR   KEGG; xla:432205; -.
DR   CTD; 432205; -.
DR   Xenbase; XB-GENE-994052; slu7.L.
DR   OMA; KKPFYVD; -.
DR   OrthoDB; 816947at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 432205; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   InterPro; IPR021715; Slu7_dom.
DR   InterPro; IPR039974; Splicing_factor_SLU7.
DR   PANTHER; PTHR12942; PTHR12942; 1.
DR   Pfam; PF11708; Slu7; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..580
FT                   /note="Pre-mRNA-splicing factor SLU7"
FT                   /id="PRO_0000289200"
FT   ZN_FING         115..132
FT                   /note="CCHC-type"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  67405 MW;  A606A245210A8BD5 CRC64;
     MLGGTDIMAT PQGGEPGGLE EPKKMTREDW RKKKELEEQR KLGNAPAEVD EEGKDINPHI
     PQYISSVPWY VDPSKRPTLK HQRPQDEKQK YFSQMDEWYK KGVKEGSITT KYRQGACENC
     GSLTHKKKDC FERPRRVGAR FTGVSIAPDE YEQPQLMLDY DGKRDRWNGY NPEEHTRIVE
     EHSKVDLAKR TLKAQKLQEE LASGKLSEQV SSPRHQWGED EQNSQTEKDR NSEDEDEDKY
     ADDIDMPGQN FDSKRRITVR NLRIREDTAK YLRNLNLNSA YYDPKTRAMR GNPYADAGKT
     PEEVSYAGDN FVRYTGDTIS MAQTQLFAWE AYEKGSDVHL QADPTKLEVL AQSFKVKKED
     FEHEQKKSIL EKYGGQEHLN IPPVELLLAQ TEDYVEYSRH GTVIKGQEKA VAKSKYEEDI
     LINNHTCIWG SYWKDGRWGY KCCHSFVKMS YCTGEAGKDI NNTDICEEDL MPTEEEMTKP
     KTLVEIHQEK LKDKKKKKKH RKSGDSDSDN DEKKKKDKLK KALNAEEARL KQVEEMMQLD
     ERKRGYNSVY ESREPTEEEM EAYRMKRLRP DDPMASFLGK