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Database: UniProt
Entry: A0A2R8Z9D6_PANPA
LinkDB: A0A2R8Z9D6_PANPA
Original site: A0A2R8Z9D6_PANPA 
ID   A0A2R8Z9D6_PANPA        Unreviewed;       418 AA.
AC   A0A2R8Z9D6;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Splicing factor 1 {ECO:0000256|RuleBase:RU367126};
GN   Name=SF1 {ECO:0000313|Ensembl:ENSPPAP00000001480.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000001480.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000001480.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000001480.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Necessary for the splicing of pre-mRNA. Has a role in the
CC       recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract
CC       and the 3'-splice site at the 3'-end of introns.
CC       {ECO:0000256|RuleBase:RU367126}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU367126}.
CC   -!- SIMILARITY: Belongs to the BBP/SF1 family.
CC       {ECO:0000256|ARBA:ARBA00010382, ECO:0000256|RuleBase:RU367126}.
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DR   EMBL; AJFE02101236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8Z9D6; -.
DR   Ensembl; ENSPPAT00000007269.1; ENSPPAP00000001480.1; ENSPPAG00000002799.1.
DR   GeneTree; ENSGT00940000157258; -.
DR   Proteomes; UP000240080; Chromosome 11.
DR   Bgee; ENSPPAG00000002799; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0045131; F:pre-mRNA branch point binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR   CDD; cd22382; KH-I_SF1; 1.
DR   Gene3D; 6.10.140.1790; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR045071; BBP-like.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR032570; SF1-HH.
DR   InterPro; IPR047086; SF1-HH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR   PANTHER; PTHR11208:SF45; SPLICING FACTOR 1; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF16275; SF1-HH; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367126};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|RuleBase:RU367126};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW   ECO:0000256|RuleBase:RU367126};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367126};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Spliceosome {ECO:0000256|RuleBase:RU367126};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367126};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00047}.
FT   DOMAIN          273..287
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..355
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  46032 MW;  8C4AC8A6318477FC CRC64;
     SLPLDFPSKK RKRSRWNQDT MEQKTVIPGM PTVIPPGLTR EQERAYIVQL QIEDLTRKLR
     TGDLGIPPNP EDRSPSPEPI YNSEGKRLNT REFRTRKKLE EERHNLITEM VALNPDFKPP
     ADYKPPATRV SDKVMIPQDE YPEINFVGLL IGPRGNTLKN IEKECNAKIM IRGKGSVKEG
     KVGRKDGQML PGEDEPLHAL VTANTMENVK KAVEQIRNIL KQGIETPEDQ NDLRKMQLRE
     LARLNGTLRE DDNRILRPWQ SSETRSITNT TVCTKCGGAG HIASDCKFQR PGDPQSAQDK
     ARMDKEYLSL MAELGEAPVP ASVGSTSGPA TTPLASAPRP AAPANNPPPP SLMSTTQSRP
     PWMNSGPSES RPYHGMHGGG PGGPGGGPHS FPHPLPSLTG GTTPMDPHPL GCSHHHHR
//
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