SLU7_MACFA
ID SLU7_MACFA Reviewed; 586 AA.
AC Q4R4P2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Pre-mRNA-splicing factor SLU7;
GN Name=SLU7; ORFNames=QtrA-13902;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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. Shuttling
CC between the nucleus and the cytoplasm is regulated by the CCHC-type
CC zinc finger. Upon UV-C stress stimulus, the nuclear concentration of
CC the protein decreases, affecting alternative splicing. Translocates
CC from the nucleus to the cytoplasm after heat shock cell treatment.
CC Accumulates in cytoplasmic vesicle-like organelles after heat shock
CC treatment, which may represent stress granules.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- DOMAIN: The CCHC-type zinc finger is required to retain the protein
CC within the nucleus and prevent its shuttle back to the cytoplasm via
CC the CRM1 pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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DR EMBL; AB169852; BAE01933.1; -; mRNA.
DR RefSeq; NP_001270446.1; NM_001283517.1.
DR AlphaFoldDB; Q4R4P2; -.
DR SMR; Q4R4P2; -.
DR STRING; 9541.XP_005558493.1; -.
DR GeneID; 101925694; -.
DR CTD; 10569; -.
DR eggNOG; KOG2560; Eukaryota.
DR OrthoDB; 816947at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
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 Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CHAIN 2..586
FT /note="Pre-mRNA-splicing factor SLU7"
FT /id="PRO_0000289195"
FT ZN_FING 118..135
FT /note="CCHC-type"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..169
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95391"
SQ SEQUENCE 586 AA; 68339 MW; BE14773AF1DC546B CRC64;
MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS IITKYRKGAC
ENCGAMTHKK KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK
IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQTE KDHNSEDEDE
DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDRGSE VHLQADPTKL ELLYKSFKVK
KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE
EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KEIVNSEECI INDITGDESV
KKPQTLMELH QEKLKEEKKK KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK
ETMQIDERKR PYNSIYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ
