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Database: UniProt
Entry: A2VDN6
LinkDB: A2VDN6
Original site: A2VDN6 
ID   SF3A1_BOVIN             Reviewed;         793 AA.
AC   A2VDN6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   01-OCT-2014, entry version 57.
DE   RecName: Full=Splicing factor 3A subunit 1;
GN   Name=SF3A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Subunit of the splicing factor SF3A required for 'A'
CC       complex assembly formed by the stable binding of U2 snRNP to the
CC       branchpoint sequence (BPS) in pre-mRNA. Sequence independent
CC       binding of SF3A/SF3B complex upstream of the branch site is
CC       essential, it may anchor U2 snRNP to the pre-mRNA. May also be
CC       involved in the assembly of the 'E' complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC       Component of splicing factor SF3A which is composed of three
CC       subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates
CC       with the splicing factor SF3B and a 12S RNA unit to form the U2
CC       small nuclear ribonucleoproteins complex (U2 snRNP). Interacts
CC       with SF3A3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Contains 2 SURP motif repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00263}.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00214}.
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DR   EMBL; BC133328; AAI33329.1; -; mRNA.
DR   RefSeq; NP_001074979.1; NM_001081510.1.
DR   RefSeq; XP_005218090.1; XM_005218033.1.
DR   UniGene; Bt.7260; -.
DR   ProteinModelPortal; A2VDN6; -.
DR   SMR; A2VDN6; 48-110, 134-217, 704-789.
DR   STRING; 9913.ENSBTAP00000004398; -.
DR   PaxDb; A2VDN6; -.
DR   PRIDE; A2VDN6; -.
DR   Ensembl; ENSBTAT00000004398; ENSBTAP00000004398; ENSBTAG00000003390.
DR   GeneID; 504381; -.
DR   KEGG; bta:504381; -.
DR   CTD; 10291; -.
DR   eggNOG; NOG300902; -.
DR   GeneTree; ENSGT00730000111077; -.
DR   HOGENOM; HOG000238941; -.
DR   HOVERGEN; HBG059993; -.
DR   InParanoid; A2VDN6; -.
DR   KO; K12825; -.
DR   OMA; VMQQQQT; -.
DR   OrthoDB; EOG7JDQX9; -.
DR   TreeFam; TF105705; -.
DR   Reactome; REACT_205948; mRNA Splicing - Major Pathway.
DR   NextBio; 20866634; -.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   InterPro; IPR022030; PRP21-like.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR000626; Ubiquitin-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF12230; PRP21_like_P; 1.
DR   Pfam; PF01805; Surp; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00648; SWAP; 2.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF109905; SSF109905; 2.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50128; SURP; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome.
FT   CHAIN         1    793       Splicing factor 3A subunit 1.
FT                                /FTId=PRO_0000295296.
FT   REPEAT       52     94       SURP motif 1.
FT   REPEAT      166    208       SURP motif 2.
FT   DOMAIN      707    793       Ubiquitin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   COMPBIAS    118    122       Poly-Gln.
FT   COMPBIAS    260    267       Poly-Glu.
FT   COMPBIAS    369    372       Poly-Pro.
FT   COMPBIAS    557    560       Poly-Pro.
FT   COMPBIAS    672    675       Poly-Pro.
FT   SITE        169    169       Critical for binding to SF3A3.
FT                                {ECO:0000250}.
FT   MOD_RES      55     55       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     320    320       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     329    329       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     359    359       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     413    413       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     451    451       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     456    456       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     759    759       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   793 AA;  88786 MW;  6FA0AD2E622056FD CRC64;
     MPAGPVQAVP PPPPAATEPK QPTEEEASSK EDSTPSKPVV GIIYPPPEVR NIVDKTASFV
     ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ
     QQASQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ
     FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFTKLK KEAENPREVL
     DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
     PEELGARILI QERYEKFGES EEVEMEVESD EEDEKQEKAE EPPSQLDQDT QVQDMDEGSD
     DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI
     PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE
     ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD
     TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP AMPPPVRTTV VSAVPVMPRP
     PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP
     VPAPAPMPPV HPPPPMEDEP ASKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW
     KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV
     IHLALKERGG RKK
//
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