CTSL2_MOUSE
ID CTSL2_MOUSE Reviewed; 465 AA.
AC Q8BG15; A2ARL6; Q3TF86; Q3TQW7; Q3TV36; Q7TPZ9; Q8BPR3; Q8C9S0; Q8CEG6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=CTD small phosphatase-like protein 2;
DE Short=CTDSP-like 2;
DE EC=3.1.3.-;
GN Name=Ctdspl2; Synonyms=D2Ertd485e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Egg, Eye, Head, Kidney, Lung, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable phosphatase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8BG15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG15-2; Sequence=VSP_033220;
CC Name=3;
CC IsoId=Q8BG15-3; Sequence=VSP_033223;
CC Name=4;
CC IsoId=Q8BG15-4; Sequence=VSP_033219, VSP_033224;
CC Name=5;
CC IsoId=Q8BG15-5; Sequence=VSP_033222;
CC Name=6;
CC IsoId=Q8BG15-6; Sequence=VSP_033221;
CC -!- SIMILARITY: Belongs to the CTDSPL2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK028251; BAC25842.1; ALT_INIT; mRNA.
DR EMBL; AK030085; BAC26775.1; -; mRNA.
DR EMBL; AK033382; BAC28257.1; -; mRNA.
DR EMBL; AK041422; BAC30939.1; -; mRNA.
DR EMBL; AK049463; BAC33759.1; -; mRNA.
DR EMBL; AK053513; BAC35412.1; -; mRNA.
DR EMBL; AK082646; BAC38557.1; -; mRNA.
DR EMBL; AK160431; BAE35784.1; -; mRNA.
DR EMBL; AK163262; BAE37265.1; -; mRNA.
DR EMBL; AK169248; BAE41012.1; -; mRNA.
DR EMBL; AL845457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052660; AAH52660.1; -; mRNA.
DR CCDS; CCDS16652.1; -. [Q8BG15-1]
DR CCDS; CCDS71130.1; -. [Q8BG15-2]
DR RefSeq; NP_001277920.1; NM_001290991.1. [Q8BG15-2]
DR RefSeq; NP_001277921.1; NM_001290992.1.
DR RefSeq; NP_997615.1; NM_212450.4. [Q8BG15-1]
DR AlphaFoldDB; Q8BG15; -.
DR SMR; Q8BG15; -.
DR STRING; 10090.ENSMUSP00000047543; -.
DR iPTMnet; Q8BG15; -.
DR PhosphoSitePlus; Q8BG15; -.
DR EPD; Q8BG15; -.
DR jPOST; Q8BG15; -.
DR MaxQB; Q8BG15; -.
DR PaxDb; Q8BG15; -.
DR PeptideAtlas; Q8BG15; -.
DR PRIDE; Q8BG15; -.
DR ProteomicsDB; 285420; -. [Q8BG15-1]
DR ProteomicsDB; 285421; -. [Q8BG15-2]
DR ProteomicsDB; 285422; -. [Q8BG15-3]
DR ProteomicsDB; 285423; -. [Q8BG15-4]
DR ProteomicsDB; 285424; -. [Q8BG15-5]
DR ProteomicsDB; 285425; -. [Q8BG15-6]
DR Antibodypedia; 42444; 147 antibodies from 27 providers.
DR DNASU; 329506; -.
DR Ensembl; ENSMUST00000036647; ENSMUSP00000047543; ENSMUSG00000033411. [Q8BG15-1]
DR Ensembl; ENSMUST00000110572; ENSMUSP00000106201; ENSMUSG00000033411. [Q8BG15-6]
DR Ensembl; ENSMUST00000110574; ENSMUSP00000106203; ENSMUSG00000033411. [Q8BG15-1]
DR Ensembl; ENSMUST00000110578; ENSMUSP00000106207; ENSMUSG00000033411. [Q8BG15-2]
DR GeneID; 329506; -.
DR KEGG; mmu:329506; -.
DR UCSC; uc008lzw.2; mouse. [Q8BG15-1]
DR UCSC; uc008lzx.2; mouse. [Q8BG15-4]
DR UCSC; uc008maa.2; mouse. [Q8BG15-2]
DR CTD; 51496; -.
DR MGI; MGI:1196405; Ctdspl2.
DR VEuPathDB; HostDB:ENSMUSG00000033411; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_034042_4_0_1; -.
DR InParanoid; Q8BG15; -.
DR OMA; PKKQLVX; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q8BG15; -.
DR TreeFam; TF354278; -.
DR BioGRID-ORCS; 329506; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Ctdspl2; mouse.
DR PRO; PR:Q8BG15; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BG15; protein.
DR Bgee; ENSMUSG00000033411; Expressed in undifferentiated genital tubercle and 226 other tissues.
DR Genevisible; Q8BG15; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISO:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IMP:MGI.
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; Alternative splicing; Hydrolase; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..465
FT /note="CTD small phosphatase-like protein 2"
FT /id="PRO_0000331465"
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 REGION 218..239
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:0000250|UniProtKB:Q05D32"
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:0007744|PubMed:21183079"
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"
FT VAR_SEQ 109..158
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033219"
FT VAR_SEQ 109
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033220"
FT VAR_SEQ 159..229
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_033221"
FT VAR_SEQ 257..465
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033222"
FT VAR_SEQ 323..465
FT /note="VYVRLRPFFREFLERMSQMYEIILFTASKKVYADKLLNILDPKKQLVRHRLF
FT REHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDNELLK
FT LIPFLEKLVELNEDVRPHIRDRFRLHDLLPPD -> QVEARNTDTDPQEQLATLRQGFC
FT LYFSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033223"
FT VAR_SEQ 324..465
FT /note="YVRLRPFFREFLERMSQMYEIILFTASKKVYADKLLNILDPKKQLVRHRLFR
FT EHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDNELLKL
FT IPFLEKLVELNEDVRPHIRDRFRLHDLLPPD -> ILSLIFKPLGNILSEENFFCDVQC
FT VFL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033224"
FT CONFLICT 104
FT /note="S -> N (in Ref. 3; AAH52660)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="I -> V (in Ref. 1; BAE37265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52813 MW; D3498BFA68B2DE15 CRC64;
MKLRTRKASQ QSSPIQTQRT ARAKRKYSEV DDSLPSGGEK PSKNETGLLS SIKKFIKGST
PKEERENPSK RSRIERDIDN NLITSTPRTG EKPDKQLSRV RRKSPVNGEA GSYEMTNQHI
KQNGKLEDNP CSGSPPRTTL LGTIFSPVFN FFSPANKNGT SGSDSPGQAV EAEEIVKQLD
MEQVDEITTS TTSANGAAYS NQAVQVRPSL NNGLEEAEET VTRDIPPLTA PVTPESGYSS
AHAEATYEED WEVFDPYYFI KHVPPLTEEQ LNRKPALPLK TRSTPEFSLV LDLDETLVHC
SLNELEDAAL TFPVLFQDVI YQVYVRLRPF FREFLERMSQ MYEIILFTAS KKVYADKLLN
ILDPKKQLVR HRLFREHCVC VQGNYIKDLN ILGRDLSKTI IIDNSPQAFA YQLSNGIPIE
SWFMDKNDNE LLKLIPFLEK LVELNEDVRP HIRDRFRLHD LLPPD
