NSRP1_BOVIN
ID NSRP1_BOVIN Reviewed; 559 AA.
AC Q2KIC0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; BC112694; AAI12695.1; -; mRNA.
DR RefSeq; NP_001039927.1; NM_001046462.1.
DR AlphaFoldDB; Q2KIC0; -.
DR SMR; Q2KIC0; -.
DR STRING; 9913.ENSBTAP00000025760; -.
DR PaxDb; Q2KIC0; -.
DR PRIDE; Q2KIC0; -.
DR Ensembl; ENSBTAT00000025760; ENSBTAP00000025760; ENSBTAG00000019341.
DR GeneID; 539841; -.
DR KEGG; bta:539841; -.
DR CTD; 84081; -.
DR VEuPathDB; HostDB:ENSBTAG00000019341; -.
DR VGNC; VGNC:32284; NSRP1.
DR eggNOG; KOG2117; Eukaryota.
DR GeneTree; ENSGT00940000154049; -.
DR InParanoid; Q2KIC0; -.
DR OMA; IYDEMQQ; -.
DR OrthoDB; 1613087at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000019341; Expressed in intramuscular adipose tissue and 105 other tissues.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..559
FT /note="Nuclear speckle splicing regulatory protein 1"
FT /id="PRO_0000240433"
FT REGION 22..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..171
FT /note="Necessary for alternative splicing activity"
FT /evidence="ECO:0000250"
FT REGION 195..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..179
FT /evidence="ECO:0000255"
FT COILED 379..428
FT /evidence="ECO:0000255"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..534
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:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU3"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0G5"
SQ SEQUENCE 559 AA; 66431 MW; EB2256D23F3806CB CRC64;
MAIPGRQYGL ILPKKAQQLH PVLQKPSVFG NDSDDDDDET SVSESLQREA AKKQAMKQTK
LEIQKALAED STVYEYDSIY DEMQKKKEES NPKLLLGKDR KPKYIHNLLK AVEIRKKEQE
KRMEKKIQRE REMEKGEFDD KEAFVTSAYK KKLQERAEEE ERERRAAALE ARLDVTKQRD
LSGFYRHLLN QAVGEEEVPT CSFREARSEI KEEKSKGYSD EVSSESRIPP ENCIRQTGVK
VEENPDADSD FDAKSSENDE MEGDKGNCRR EKGTETLSSH SKHHRNPARS PSSSEEREHG
TQCHTKSSRS RGHEKREDEH QERPAREQDS YHTDRDSRKE KRDSHRHRES SHRDSHWKRH
EEERLRGRDE RERNDREWKR EKDREKYPSR EQERHRQRNN YDRHNEKGCE KEEKSKEKEE
HVKARKERYE NSDKYRDREK REVSVESSER NRDRKESSPN SRAKDRFVNQ ERASKMRDME
KDKERNPEKP SSSEASLGAK HRITEECQET GKEQERLHET VNKFAKRSNE ETVTSARDRY
LARQMARINA KTYIEKEDD
