CTDSL_CHICK
ID CTDSL_CHICK Reviewed; 275 AA.
AC Q9PTJ6; Q9PTJ7; Q9PTJ8; Q9PTJ9;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CTD small phosphatase-like protein;
DE Short=CTDSP-like;
DE EC=3.1.3.16;
DE AltName: Full=Nuclear LIM interactor-interacting factor 1;
DE Short=NLI-interacting factor 1;
DE AltName: Full=Small C-terminal domain phosphatase 3;
GN Name=NFI1; Synonyms=NIF;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=Brown leghorn; TISSUE=Neuroretina;
RA Mikhailik A., Dezelee P., Calothy G.;
RT "NLI/Ldb1/CLIM interacting factor.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5'
CC within the tandem 7 residue repeats in the C-terminal domain (CTD) of
CC the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA
CC polymerase II transcription, possibly by controlling the transition
CC from initiation/capping to processive transcript elongation. Recruited
CC by REST to neuronal genes that contain RE-1 elements, leading to
CC neuronal gene silencing in non-neuronal cells (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with LDB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist. A not yet characterized
CC isoform having a longer N-terminus as seen in human and mouse might
CC exist.;
CC Name=1; Synonyms=T1;
CC IsoId=Q9PTJ6-1; Sequence=Displayed;
CC Name=2; Synonyms=T2;
CC IsoId=Q9PTJ6-2; Sequence=VSP_003564, VSP_003566;
CC Name=3; Synonyms=T3;
CC IsoId=Q9PTJ6-3; Sequence=VSP_003565;
CC Name=4; Synonyms=R5;
CC IsoId=Q9PTJ6-4; Sequence=VSP_003564;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF189773; AAF17481.1; -; mRNA.
DR EMBL; AF189774; AAF17482.1; -; mRNA.
DR EMBL; AF189775; AAF17483.1; -; mRNA.
DR EMBL; AF189776; AAF17484.1; -; mRNA.
DR RefSeq; NP_001001316.1; NM_001001316.1. [Q9PTJ6-1]
DR RefSeq; XP_015136538.1; XM_015281052.1. [Q9PTJ6-4]
DR AlphaFoldDB; Q9PTJ6; -.
DR SMR; Q9PTJ6; -.
DR STRING; 9031.ENSGALP00000041927; -.
DR PaxDb; Q9PTJ6; -.
DR Ensembl; ENSGALT00000009158; ENSGALP00000009144; ENSGALG00000005710. [Q9PTJ6-1]
DR Ensembl; ENSGALT00000042703; ENSGALP00000041927; ENSGALG00000005710. [Q9PTJ6-4]
DR Ensembl; ENSGALT00000083911; ENSGALP00000058763; ENSGALG00000005710. [Q9PTJ6-2]
DR Ensembl; ENSGALT00000086976; ENSGALP00000061223; ENSGALG00000005710. [Q9PTJ6-3]
DR GeneID; 408252; -.
DR KEGG; gga:408252; -.
DR CTD; 10217; -.
DR VEuPathDB; HostDB:geneid_408252; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_4_0_1; -.
DR InParanoid; Q9PTJ6; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q9PTJ6; -.
DR TreeFam; TF313556; -.
DR PRO; PR:Q9PTJ6; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000005710; Expressed in kidney and 13 other tissues.
DR ExpressionAtlas; Q9PTJ6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..275
FT /note="CTD small phosphatase-like protein"
FT /id="PRO_0000212571"
FT DOMAIN 101..259
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT ACT_SITE 111
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 167
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VAR_SEQ 78..88
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003564"
FT VAR_SEQ 173..275
FT /note="YADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSP
FT ASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSKEEEVYSMLHKLCNR -> CVLC
FT LLVCGMQTQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003565"
FT VAR_SEQ 275
FT /note="R -> SSFKCKLWGGHSCQKCYSRSSCYIGHKGQS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003566"
SQ SEQUENCE 275 AA; 31244 MW; F68C357769809347 CRC64;
MDNPSIITQV TNPKEEEILS CTQDKVSQCN ISLKKQRSRS IFSTLFCCFR DYNVEPPSTN
STSALPPLVE ENGGLQKGDQ MQVMPIPSPP AKYLLPELTA SDYGKKCVVI DLDETLVHSS
FKPISNADFI VPVEIDGTIH QVYVLKRPHV DEFLQRMGEL FECVLFTASL AKYADPVADL
LDRWGVFRAR LFRESCVFHR GNYVKDLSRL GRELSKVIIV DNSPASYIFH PENAVPVQSW
FDDMTDTELL DLIPFFEGLS KEEEVYSMLH KLCNR
