SCPL1_CAEEL
ID SCPL1_CAEEL Reviewed; 491 AA.
AC Q8T3G2; A5Z2W8; Q8T3G3;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=CTD small phosphatase-like protein 1 {ECO:0000303|PubMed:18337465};
DE Short=SCP-like 1 {ECO:0000303|PubMed:18337465};
DE EC=3.1.3.16 {ECO:0000305|PubMed:18337465};
GN Name=scpl-1 {ECO:0000303|PubMed:18337465, ECO:0000312|WormBase:B0379.4b};
GN ORFNames=B0379.4 {ECO:0000312|WormBase:B0379.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH UNC-89, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18337465; DOI=10.1091/mbc.e08-01-0053;
RA Qadota H., McGaha L.A., Mercer K.B., Stark T.J., Ferrara T.M., Benian G.M.;
RT "A novel protein phosphatase is a binding partner for the protein kinase
RT domains of UNC-89 (Obscurin) in Caenorhabditis elegans.";
RL Mol. Biol. Cell 19:2424-2432(2008).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-89 AND LIM-9, AND DISRUPTION PHENOTYPE.
RX PubMed=19244614; DOI=10.1016/j.jmb.2009.01.016;
RA Xiong G., Qadota H., Mercer K.B., McGaha L.A., Oberhauser A.F.,
RA Benian G.M.;
RT "A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein
RT kinase regions of UNC-89 (obscurin) in Caenorhabditis elegans muscle.";
RL J. Mol. Biol. 386:976-988(2009).
RN [4] {ECO:0000305}
RP INTERACTION WITH CPNA-1.
RX PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA Benian G.M.;
RT "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT is required for myofilament stability in Caenorhabditis elegans.";
RL Mol. Biol. Cell 24:601-616(2013).
CC -!- FUNCTION: Phosphatase which may play a role in the egg laying muscles.
CC {ECO:0000269|PubMed:18337465, ECO:0000269|PubMed:19244614}.
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 Evidence={ECO:0000305|PubMed:18337465};
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 Evidence={ECO:0000305|PubMed:18337465};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18337465};
CC Note=May also use Mn(2+). {ECO:0000269|PubMed:18337465};
CC -!- ACTIVITY REGULATION: Inhibited by beryllium trifluoride (BeF(3-)) and
CC tetrafluoroaluminate (AlF(4-)) but not by sodium fluoride (NaF) or
CC sodium orthovanadate (Na3VO4). {ECO:0000269|PubMed:18337465}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:18337465};
CC -!- SUBUNIT: May interact (via phosphatase domain) with cpna-1
CC (PubMed:23283987). Isoform a and isoform b may interact with lim-9 (via
CC LIM zinc-binding domain) (PubMed:19244614). Isoform a and isoform b may
CC interact (via FCP1 homology domain) with unc-89 (via fibronectin type-
CC III domain 1, Ig-like C2-type domain 48/49 and protein kinase domain 1
CC or Ig-like C2-type domain 50, fibronectin type-III domain 2 and protein
CC kinase domain 2); the interaction may act as a molecular bridge to
CC bring two unc-89 molecules together or to stabilize a loop between the
CC 2 protein kinase domains (PubMed:18337465, PubMed:19244614).
CC {ECO:0000269|PubMed:18337465, ECO:0000269|PubMed:19244614,
CC ECO:0000269|PubMed:23283987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:18337465}. Note=Colocalizes with unc-89 at M line.
CC {ECO:0000269|PubMed:18337465}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:B0379.4b};
CC IsoId=Q8T3G2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:B0379.4a};
CC IsoId=Q8T3G2-2; Sequence=VSP_058740;
CC Name=c {ECO:0000312|WormBase:B0379.4c};
CC IsoId=Q8T3G2-3; Sequence=VSP_058739;
CC -!- TISSUE SPECIFICITY: [Isoform b]: Expressed in pharyngeal, vulval and
CC body wall muscles. {ECO:0000269|PubMed:18337465}.
CC -!- DISRUPTION PHENOTYPE: Both RNAi-mediated knockdown of isoform a and of
CC isoform b decreases egg laying triggered by serotonin treatment
CC (PubMed:18337465). Causes no visible defects in unc-89 and cpna-1
CC localization in body wall muscles (PubMed:19244614, PubMed:23283987).
CC {ECO:0000269|PubMed:18337465, ECO:0000269|PubMed:19244614,
CC ECO:0000269|PubMed:23283987}.
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DR EMBL; BX284601; CAD30428.2; -; Genomic_DNA.
DR EMBL; BX284601; CAD30429.2; -; Genomic_DNA.
DR EMBL; BX284601; CAN99655.1; -; Genomic_DNA.
DR RefSeq; NP_001122411.1; NM_001128939.1. [Q8T3G2-3]
DR RefSeq; NP_740911.2; NM_170917.4.
DR RefSeq; NP_740912.2; NM_170918.4. [Q8T3G2-1]
DR AlphaFoldDB; Q8T3G2; -.
DR SMR; Q8T3G2; -.
DR DIP; DIP-25609N; -.
DR STRING; 6239.B0379.4b; -.
DR EPD; Q8T3G2; -.
DR PaxDb; Q8T3G2; -.
DR PeptideAtlas; Q8T3G2; -.
DR EnsemblMetazoa; B0379.4a.1; B0379.4a.1; WBGene00007054. [Q8T3G2-2]
DR EnsemblMetazoa; B0379.4b.1; B0379.4b.1; WBGene00007054. [Q8T3G2-1]
DR EnsemblMetazoa; B0379.4c.1; B0379.4c.1; WBGene00007054. [Q8T3G2-3]
DR GeneID; 181944; -.
DR UCSC; B0379.4c; c. elegans.
DR CTD; 181944; -.
DR WormBase; B0379.4a; CE34243; WBGene00007054; scpl-1. [Q8T3G2-2]
DR WormBase; B0379.4b; CE34244; WBGene00007054; scpl-1. [Q8T3G2-1]
DR WormBase; B0379.4c; CE41191; WBGene00007054; scpl-1. [Q8T3G2-3]
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_041593_0_0_1; -.
DR InParanoid; Q8T3G2; -.
DR OMA; YPFLTEQ; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q8T3G2; -.
DR PRO; PR:Q8T3G2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007054; Expressed in larva and 3 other tissues.
DR GO; GO:0031674; C:I band; IDA:WormBase.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0019900; F:kinase binding; IPI:WormBase.
DR GO; GO:0030274; F:LIM domain binding; IPI:WormBase.
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:0016791; F:phosphatase activity; IDA:WormBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:WormBase.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..491
FT /note="CTD small phosphatase-like protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438739"
FT DOMAIN 307..465
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT ACT_SITE 319
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT SITE 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT SITE 411
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT VAR_SEQ 1..292
FT /note="MTYAESTRSAVVYSSIVPPPRTPVGPPMLKDGVRKGSASQPLQPKNGANSLD
FT YWSKSEDEKSGITCYYSRHNIQFPPPQRKMKPVKPNPVGRSTINGFTPSTSSPQNGLRY
FT PPFPQNTPESVMSPPVGIYRNIPAMPRAKLTKDEKNGGKMNRDGGGENPKNVVWGGTSR
FT KDDDTASTPLNSFSANASIEKKRSTARRKPRWARCFQTLFCCVTPPREIEKIQSSQRTN
FT STNNNHQNGRPSTPTNTGPPIQLITQVHRDGTVTGLPTTGQACQQNGSGDGVTPYDKIA
FT NDSV -> MREPQHVKRKQLMFQDEFDYRLNYRELIEWKPGRTPSALEIIELGLLHCKK
FT (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058739"
FT VAR_SEQ 1..187
FT /note="MTYAESTRSAVVYSSIVPPPRTPVGPPMLKDGVRKGSASQPLQPKNGANSLD
FT YWSKSEDEKSGITCYYSRHNIQFPPPQRKMKPVKPNPVGRSTINGFTPSTSSPQNGLRY
FT PPFPQNTPESVMSPPVGIYRNIPAMPRAKLTKDEKNGGKMNRDGGGENPKNVVWGGTSR
FT KDDDTASTPLNSFSANA -> MNNGYGVQAATETTISDSSADVSFVKPIGQVAGADFIK
FT QTS (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058740"
SQ SEQUENCE 491 AA; 54372 MW; 03077E0FE6536CA1 CRC64;
MTYAESTRSA VVYSSIVPPP RTPVGPPMLK DGVRKGSASQ PLQPKNGANS LDYWSKSEDE
KSGITCYYSR HNIQFPPPQR KMKPVKPNPV GRSTINGFTP STSSPQNGLR YPPFPQNTPE
SVMSPPVGIY RNIPAMPRAK LTKDEKNGGK MNRDGGGENP KNVVWGGTSR KDDDTASTPL
NSFSANASIE KKRSTARRKP RWARCFQTLF CCVTPPREIE KIQSSQRTNS TNNNHQNGRP
STPTNTGPPI QLITQVHRDG TVTGLPTTGQ ACQQNGSGDG VTPYDKIAND SVGTINEKPL
LPPLLPQDSN KKCLVIDLDE TLVHSSFKPV KNPDFVIPVE IDGVEHQVYV LKRPYVDEFL
AKVGEHFECI LFTASLAKYA DPVADLLDKK RVFRGRLFRE ACVFHKGNYV KDLSRLGRNL
NQTLIIDNSP ASYAFHPENA VPVTTWFDDP SDTELLDILP SLEHLNGFSS IYDLYRPEEG
PQSELLNHCS C
