SRRM1_PONAB
ID SRRM1_PONAB Reviewed; 917 AA.
AC Q5R5Q2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Serine/arginine repetitive matrix protein 1;
GN Name=SRRM1;
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 -!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes.
CC Involved in numerous pre-mRNA processing events. Promotes constitutive
CC and exonic splicing enhancer (ESE)-dependent splicing activation by
CC bridging together sequence-specific (SR family proteins, SFRS4, SFRS5
CC and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the
CC spliceosome. Stimulates mRNA 3'-end cleavage independently of the
CC formation of an exon junction complex. Binds both pre-mRNA and spliced
CC mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with
CC low sequence specificity and has similar preference for either
CC double- or single-stranded nucleic acid substrates.
CC {ECO:0000250|UniProtKB:Q8IYB3}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Found in a pre-mRNA
CC splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2.
CC Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRP70,
CC SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA splicing-dependent exon
CC junction complex (EJC) with DEK, PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and
CC ALYREF/THOC4. Interacts with DDX39B, CPSF1, RBM8A, RNPS1, and
CC ALYREF/THOC4. Seems to be a compound of RNA export complexes that are
CC released from speckles in a ATP-dependent manner.
CC {ECO:0000250|UniProtKB:Q8IYB3}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues by DYRK3
CC during the G2-to-M transition, after the nuclear-envelope breakdown.
CC Phosphorylation by DYRK3 promotes disassembly of nuclear speckles.
CC {ECO:0000250|UniProtKB:Q8IYB3}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q52KI8}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; CR860804; CAH92914.1; -; mRNA.
DR RefSeq; NP_001126712.1; NM_001133240.1.
DR AlphaFoldDB; Q5R5Q2; -.
DR BMRB; Q5R5Q2; -.
DR SMR; Q5R5Q2; -.
DR STRING; 9601.ENSPPYP00000001983; -.
DR PRIDE; Q5R5Q2; -.
DR GeneID; 100173713; -.
DR KEGG; pon:100173713; -.
DR CTD; 10250; -.
DR eggNOG; KOG2146; Eukaryota.
DR InParanoid; Q5R5Q2; -.
DR OrthoDB; 1210775at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR PROSITE; PS51025; PWI; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Citrullination; DNA-binding; Isopeptide bond; mRNA processing;
KW mRNA splicing; Phosphoprotein; Reference proteome; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..917
FT /note="Serine/arginine repetitive matrix protein 1"
FT /id="PRO_0000076328"
FT DOMAIN 27..126
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 1..156
FT /note="Necessary for mRNA 3'-end cleavage and cytoplasmic
FT accumulation"
FT /evidence="ECO:0000250"
FT REGION 1..151
FT /note="Necessary for DNA and RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 139..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..702
FT /note="Necessary for speckles and matrix localization"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..349
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..848
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 7
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 610
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KI8"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 731
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q52KI8"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 806
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 885
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYB3"
SQ SEQUENCE 917 AA; 103898 MW; 40A269536325A4FB CRC64;
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL
GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP
SAFLELKKEE IKQRQIEQEK LASMKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP
SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS
TSDILKVPKP EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR
RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR SSASLSGSSS
SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR PSPPATPPPK TRHSPTPQQS
NRTRKSRVSV SPGRTSGKVT KHKGTEKRES PSPAPKPRKV ELSESEEDKG GKMAAADSVQ
QRRQYRRQNQ QSSSDSGSSS SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET
SPRMQMGKRW QSPVTKSGRR RRSPSPPPTR RRRSPSPAPP PRRRRTPTPP PRRRTPSPPP
RRRSPSPRRY SPPIQRRYSP SPPPKRRTAS PPPPPKRRAS PSPPPKRRVS HSPPPKQRSS
PVTKRRSPSL SSKHRKGSSP SRSTREARSP QPNKRHSPSP RPRAPQTSSP PPVRRGASSS
PQRRQSPSPS TRPIRRVSRT PEPKKIKKAA SPSPQSVRRV SSSRSVSGSP EPAAKKPPAP
TSPVQSQSPS TNWSPAVPVK KAKSPTPSPS PPRNSDQEGG GKKKKKKKDK KHKKDKKHKK
HKKHKKEKAV AAAAAAAVTP AAIAAATTTL AQEEPVAAPE PKKETESEAE DNLDDLEKHL
REKALRSMRK AQVSPQS
