NSRP1_RAT
ID NSRP1_RAT Reviewed; 547 AA.
AC Q4FZU3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Nuclear speckle splicing regulatory protein 1;
DE AltName: Full=Coiled-coil domain-containing protein 55;
DE AltName: Full=Nuclear speckle-related protein 70;
DE Short=NSrp70;
GN Name=Nsrp1; Synonyms=Ccdc55, Nsrp70;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-447, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC splicing regulation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SRSF1. Interacts (via C-
CC terminus) with SRSF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Note=Colocalizes with splicing factors SRSF1 and SRSF2
CC in speckles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NSRP1 family. {ECO:0000305}.
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DR EMBL; BC099120; AAH99120.1; -; mRNA.
DR RefSeq; NP_001032266.1; NM_001037189.1.
DR AlphaFoldDB; Q4FZU3; -.
DR SMR; Q4FZU3; -.
DR STRING; 10116.ENSRNOP00000036224; -.
DR iPTMnet; Q4FZU3; -.
DR PhosphoSitePlus; Q4FZU3; -.
DR PaxDb; Q4FZU3; -.
DR PRIDE; Q4FZU3; -.
DR Ensembl; ENSRNOT00000107073; ENSRNOP00000087935; ENSRNOG00000062400.
DR GeneID; 303346; -.
DR KEGG; rno:303346; -.
DR CTD; 84081; -.
DR RGD; 1309863; Nsrp1.
DR eggNOG; KOG2117; Eukaryota.
DR GeneTree; ENSGT00940000154049; -.
DR HOGENOM; CLU_548527_0_0_1; -.
DR InParanoid; Q4FZU3; -.
DR OMA; IYDEMQQ; -.
DR OrthoDB; 1613087at2759; -.
DR PhylomeDB; Q4FZU3; -.
DR TreeFam; TF319359; -.
DR PRO; PR:Q4FZU3; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000022502; Expressed in lung and 19 other tissues.
DR Genevisible; Q4FZU3; RN.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR042816; Nsrp1.
DR InterPro; IPR018612; NSRP1_N.
DR PANTHER; PTHR31938; PTHR31938; 1.
DR Pfam; PF09745; DUF2040; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..547
FT /note="Nuclear speckle splicing regulatory protein 1"
FT /id="PRO_0000240436"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..169
FT /note="Necessary for alternative splicing activity"
FT /evidence="ECO:0000250"
FT REGION 188..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..177
FT /evidence="ECO:0000255"
FT COILED 376..417
FT /evidence="ECO:0000255"
FT COMPBIAS 198..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 276
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5NCR9"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
SQ SEQUENCE 547 AA; 64180 MW; 903500D92DB17BCC CRC64;
MAIPGRQYGL ILPKKTQPLN RVLQKPSVFG NDSDDDEASV SESLQREAAK KQAMRQTKLE
IQKALAEDST VYEYDSIYDE MQKKKEENNP KLLMGKDRKP KYIHNLLKAV EIRKKEQEKR
MEKKIQRERE MEKGEFDDKE AFVTSAYKKK LEERAEEEER EKRAAALEAR LDVTKQKDLS
GFYRHLLNQA VGEEAVPKSS FREARTVIKE EKLRGYPDET NSENRPQQNC ALQSGVEEAE
ENPDADSDSE ESCDDGERGD HKVKSRGEED TGASTKYLKH HKNHTHSRSS SEEGGLSTKY
HSRSSQSRGH EHKGGQHQDR QSRDQESCHK DRSHREEKSS HRHREASHKD HHWKRHEHED
KPKGRGQGER QDREWKREKY SSREQEKDRQ WNDHDRYSEK EKKGKEKEEH RKARRERCED
GAKYRERKKP EGSGQSSERH RDRRESSPRP RPEDDLLDQE RSSKARNTEK DKGEQGKPPR
SETSLATKHR LTEERPEKGS QPERPPEAVS KFAKRSNEET VMSARDRYLA RQMARINAKT
YIEKEDD
