ID V9L0P4_CALMI Unreviewed; 431 AA.
AC V9L0P4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Splicing factor U2AF subunit {ECO:0000256|RuleBase:RU364135};
DE AltName: Full=U2 snRNP auxiliary factor large subunit {ECO:0000256|RuleBase:RU364135};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP04384.1};
RN [1] {ECO:0000313|EMBL:AFP04384.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:AFP04384.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA.
CC {ECO:0000256|RuleBase:RU364135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364135}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family.
CC {ECO:0000256|RuleBase:RU364135}.
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DR EMBL; JW871866; AFP04384.1; -; mRNA.
DR AlphaFoldDB; V9L0P4; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12230; RRM1_U2AF65; 1.
DR CDD; cd12231; RRM2_U2AF65; 1.
DR CDD; cd12232; RRM3_U2AF65; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR006529; U2AF_lg.
DR NCBIfam; TIGR01642; U2AF_lg; 1.
DR PANTHER; PTHR23139; RNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR23139:SF9; SPLICING FACTOR U2AF 65 KDA SUBUNIT; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU364135};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU364135};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364135};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 109..191
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 219..297
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 322..422
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP04384.1"
SQ SEQUENCE 431 AA; 47645 MW; 123356BD247591E3 CRC64;
WAEEGAGGGG GDGRGGSRSR ERPNRERRSN SPRERRRRSR SPRRVQKKKP YKYWDVAPPG
FEHITPMQYK AMQGQIPATA LLPTVTPDGL AVTPTQVPVV GSQMTRQARR LYVGNIPFGV
TEEAMADFFN AQMRLAALSQ AAGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ
GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV STVVPDSPHK LFIGGLPNYL NDDQVKELLT
SFGPLKAFNL VKDSATGLSK GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL IVQRASVGAK
NATPNTINQT PVTLQVPGLV STQVQMAGLP TEILCLMNMI SPEELIDDEE YEEIVEDVRE
ECSKYGIVKS IEIPRPIDGL EVPGCGKIFV EFVSVMDCQK AMQGLAGRKF ANRVVVTKYC
EPDCYHRRDF W
//
