SR140_PONAB
ID SR140_PONAB Reviewed; 1028 AA.
AC Q5R7X2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=U2 snRNP-associated SURP motif-containing protein;
DE AltName: Full=140 kDa Ser/Arg-rich domain protein;
DE AltName: Full=U2-associated protein SR140;
GN Name=U2SURP; Synonyms=SR140;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with ERBB4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; CR859987; CAH92138.1; -; mRNA.
DR RefSeq; NP_001127512.1; NM_001134040.1.
DR AlphaFoldDB; Q5R7X2; -.
DR SMR; Q5R7X2; -.
DR STRING; 9601.ENSPPYP00000015859; -.
DR GeneID; 100174588; -.
DR KEGG; pon:100174588; -.
DR CTD; 23350; -.
DR eggNOG; KOG0151; Eukaryota.
DR InParanoid; Q5R7X2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd12223; RRM_SR140; 1.
DR Gene3D; 1.10.10.790; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR035009; SR140_RRM.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF08312; cwf21; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM01115; cwf21; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF109905; SSF109905; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50128; SURP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CHAIN 2..1028
FT /note="U2 snRNP-associated SURP motif-containing protein"
FT /id="PRO_0000280072"
FT DOMAIN 273..354
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 429..472
FT /note="SURP motif"
FT DOMAIN 533..678
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..121
FT /evidence="ECO:0000255"
FT COILED 192..232
FT /evidence="ECO:0000255"
FT COILED 779..809
FT /evidence="ECO:0000255"
FT COILED 836..914
FT /evidence="ECO:0000255"
FT COMPBIAS 7..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..805
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1028
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 718
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 759
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 930
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 759
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 821
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 828
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
FT CROSSLNK 831
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15042"
SQ SEQUENCE 1028 AA; 118236 MW; 626B4D7DCC200332 CRC64;
MADKTPGGSQ KASSKTRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP RKHNYRNESA
RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE QEELKKKEDE KAAAEIYEEF
LAAFEGSDGN KVKTFVRGGV VNAAKEEHET DEKRGKIYKP SSRFADQKNP PNQSSNERPP
SLLVIETKKP PLKKGEKEKK KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG
QRRSMDAPSR RNRSSVLDDY APGSHDVGDP STTNLYLGNI NPQMNEEMLC QEFGRFGPLA
SVKIMWPRTD EERARERNCG FVAFMNRRDA ERALKNLNGK MIMSFEMKLG WGKAVPIPPH
PIYIPPSMME HTLPPPPSGL PFNAQPRERL KNPNAPMLPP PKNKEDFEKT LSQAIVKVVI
PTERNLLALI HRMIEFVVRE GPMFEAMIMN REINNPMFRF LFENQTPAHV YYRWKLYSIL
QGDSPTKWRT EDFRMFKNGS FWRPPPLNPY LHGMSEEQET EAFVEEPSKK GALKEEQRDK
LEEILRGLTP RKNDIGDAMV FCLNNAEAAE EIVDCITESL SILKTPLPKK IARLYLVSDV
LYNSSAKVAN ASYYRKFFET KLCQIFSDLN ATYRTIQGHL QSENFKQRVM TCFRAWEDWA
IYPEPFLIKL QNIFLGLVNI IEEKETEDVP DDLDGAPIEE ELDGAPLEDV DGIPIDATPI
DDLDGVPIKS LDDDLDGVPL DATEDSKKNE PIFKVAPSKW EAVDESELEA QAVTTSKWEL
FDQHEESEEE ENQNQEEESE DEEDTQSSKS EEHHLYSNPI KEEMTESKFS KYSEMSEEKR
AKLREIELKV MKFQDELESG KRPKKPGQSF QEQVEHYRDK LLQREKEKEL ERERERDKKD
KEKLESRSKD EKEKDECTPT RKERKRRHST SPSPSRSSSG RRVKSPSPKS ERSERSERSH
KESSRSRSSH KDSPRDVSKK AKRSPSGSRT PKRSRRSRSR SPKKSGKKSR SQSRSPHRSH
KKSKKNKH
