ID   CTSL2_RAT               Reviewed;         465 AA.
AC   Q5XIK8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=CTD small phosphatase-like protein 2;
DE            Short=CTDSP-like 2;
DE            EC=3.1.3.-;
GN   Name=Ctdspl2;
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=Testis;
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-28, AND IDENTIFICATION BY
RP   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: Probable phosphatase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CTDSPL2 family. {ECO:0000305}.
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DR   EMBL; BC083672; AAH83672.1; -; mRNA.
DR   RefSeq; NP_001014070.1; NM_001014048.1.
DR   AlphaFoldDB; Q5XIK8; -.
DR   SMR; Q5XIK8; -.
DR   STRING; 10116.ENSRNOP00000033786; -.
DR   iPTMnet; Q5XIK8; -.
DR   PhosphoSitePlus; Q5XIK8; -.
DR   PaxDb; Q5XIK8; -.
DR   GeneID; 311368; -.
DR   KEGG; rno:311368; -.
DR   UCSC; RGD:1309219; rat.
DR   CTD; 51496; -.
DR   RGD; 1309219; Ctdspl2.
DR   eggNOG; KOG1605; Eukaryota.
DR   InParanoid; Q5XIK8; -.
DR   OrthoDB; 1176152at2759; -.
DR   PhylomeDB; Q5XIK8; -.
DR   PRO; PR:Q5XIK8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISO:RGD.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
DR   GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
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   Pfam; PF03031; NIF; 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   Acetylation; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..465
FT                   /note="CTD small phosphatase-like protein 2"
FT                   /id="PRO_0000331466"
FT   DOMAIN          282..441
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05D32"
SQ   SEQUENCE   465 AA;  52783 MW;  37589AEB721874BF CRC64;
     MKLRTRKASQ QSSPIQTQRT ARAKRKYSEV DDSLPSGGEK PSKNETGLLS SIKKFIKGST
     PKEERENPSK RSRIERDIDN NLITSTPRTG EKPDKQLSRV RRKSPVNGEA GSYEMTNQHI
     KQNGKLEDNP CSGSPPRTTL LGTIFSPVFN FFSPANKNGT SGSDSPGQAV EAEEIVKQLD
     MEQVDEITTS TTSANGAAYS NQAVQVRPSL NNGLEEAEET VTRDIPPLTA PVAPESGYSS
     AHAEATYEED WEVFDPYYFI KHVPPLTEEQ LNRKPALPLK TRSTPEFSLV LDLDETLVHC
     SLNELEDAAL TFPVLFQDVI YQVYVRLRPF FREFLERMSQ MYEIILFTAS KKVYADKLLN
     ILDPKKQLVR HRLFREHCVC VQGNYIKDLN ILGRDLSKTI IIDNSPQAFA YQLSNGIPIE
     SWFMDKNDNE LLKLIPFLEK LVELNEDVRP HIRDRFRLHD LLPPD