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SLU7_BOVIN
ID   SLU7_BOVIN              Reviewed;         586 AA.
AC   Q3ZBE5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Pre-mRNA-splicing factor SLU7;
GN   Name=SLU7;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-505.
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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; BC103394; AAI03395.1; ALT_TERM; mRNA.
DR   RefSeq; NP_001160089.1; NM_001166617.1.
DR   AlphaFoldDB; Q3ZBE5; -.
DR   SMR; Q3ZBE5; -.
DR   STRING; 9913.ENSBTAP00000011131; -.
DR   PaxDb; Q3ZBE5; -.
DR   PRIDE; Q3ZBE5; -.
DR   Ensembl; ENSBTAT00000011131; ENSBTAP00000011131; ENSBTAG00000008457.
DR   GeneID; 512318; -.
DR   KEGG; bta:512318; -.
DR   CTD; 10569; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008457; -.
DR   VGNC; VGNC:34971; SLU7.
DR   eggNOG; KOG2560; Eukaryota.
DR   GeneTree; ENSGT00390000002292; -.
DR   HOGENOM; CLU_019317_2_0_1; -.
DR   InParanoid; Q3ZBE5; -.
DR   OMA; KKPFYVD; -.
DR   OrthoDB; 816947at2759; -.
DR   TreeFam; TF105691; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008457; Expressed in thymus and 111 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IEA:Ensembl.
DR   GO; GO:0000386; F:second spliceosomal transesterification activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0000389; P:mRNA 3'-splice site recognition; IEA:Ensembl.
DR   GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
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_0000289193"
FT   ZN_FING         118..135
FT                   /note="CCHC-type"
FT   REGION          1..103
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;  68203 MW;  09E0E6674755C81C CRC64;
     MSAAAVDAAN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
     PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQYSSSGE WYKRGVKENS ITTKYRKGAC
     ENCGAMTHKK KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK
     IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQTE KDHNSEDEDE
     DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
     GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK
     KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE
     EDVKINNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KEIANSEECI INDATGEESV
     KKPQTLMEIH QEKLKEEKKK KKKKKRKHRK SSSESDDEEK KHEKLKKALN AEEARLLHVK
     EIMQIDERKR PYNSIYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ
 
 
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