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CPPED_MOUSE
ID   CPPED_MOUSE             Reviewed;         312 AA.
AC   Q8BFS6; Q3UYF7; Q8BJQ3; Q8BYB7; Q8K236; Q8R3G2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Serine/threonine-protein phosphatase CPPED1;
DE            EC=3.1.3.16;
DE   AltName: Full=Calcineurin-like phosphoesterase domain-containing protein 1;
GN   Name=Cpped1; Synonyms=Cstp1;
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 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Medulla oblongata, Olfactory bulb, Spinal cord, and
RC   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 MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 2-312 (ISOFORM 1).
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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: Protein phosphatase that dephosphorylates AKT family kinase
CC       specifically at 'Ser-473', blocking cell cycle progression and
CC       promoting cell apoptosis. May play an inhibitory role in glucose uptake
CC       by adipocytes (By similarity). {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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BFS6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BFS6-2; Sequence=VSP_031660;
CC       Name=3;
CC         IsoId=Q8BFS6-3; Sequence=VSP_031661, VSP_031663;
CC       Name=4;
CC         IsoId=Q8BFS6-4; Sequence=VSP_031664, VSP_031665;
CC       Name=5;
CC         IsoId=Q8BFS6-5; Sequence=VSP_031659, VSP_031662;
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CPPED1
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK041329; BAC30908.1; -; mRNA.
DR   EMBL; AK032288; BAC27795.1; -; mRNA.
DR   EMBL; AK049721; BAC33892.1; -; mRNA.
DR   EMBL; AK080876; BAC38056.1; -; mRNA.
DR   EMBL; AK134718; BAE22255.1; -; mRNA.
DR   EMBL; BC034347; AAH34347.1; -; mRNA.
DR   EMBL; BC025476; AAH25476.1; ALT_INIT; mRNA.
DR   CCDS; CCDS27964.1; -. [Q8BFS6-1]
DR   RefSeq; NP_666179.2; NM_146067.3. [Q8BFS6-1]
DR   AlphaFoldDB; Q8BFS6; -.
DR   SMR; Q8BFS6; -.
DR   STRING; 10090.ENSMUSP00000093992; -.
DR   iPTMnet; Q8BFS6; -.
DR   PhosphoSitePlus; Q8BFS6; -.
DR   SwissPalm; Q8BFS6; -.
DR   EPD; Q8BFS6; -.
DR   jPOST; Q8BFS6; -.
DR   MaxQB; Q8BFS6; -.
DR   PaxDb; Q8BFS6; -.
DR   PeptideAtlas; Q8BFS6; -.
DR   PRIDE; Q8BFS6; -.
DR   ProteomicsDB; 278022; -. [Q8BFS6-1]
DR   ProteomicsDB; 278023; -. [Q8BFS6-2]
DR   ProteomicsDB; 278024; -. [Q8BFS6-3]
DR   ProteomicsDB; 278025; -. [Q8BFS6-4]
DR   ProteomicsDB; 278026; -. [Q8BFS6-5]
DR   Antibodypedia; 24789; 144 antibodies from 23 providers.
DR   DNASU; 223978; -.
DR   Ensembl; ENSMUST00000073371; ENSMUSP00000089104; ENSMUSG00000065979. [Q8BFS6-3]
DR   Ensembl; ENSMUST00000096272; ENSMUSP00000093992; ENSMUSG00000065979. [Q8BFS6-1]
DR   Ensembl; ENSMUST00000121750; ENSMUSP00000112587; ENSMUSG00000065979. [Q8BFS6-2]
DR   GeneID; 223978; -.
DR   KEGG; mmu:223978; -.
DR   UCSC; uc007yfm.1; mouse. [Q8BFS6-1]
DR   UCSC; uc007yfn.1; mouse. [Q8BFS6-2]
DR   UCSC; uc007yfo.1; mouse. [Q8BFS6-4]
DR   UCSC; uc007yfp.1; mouse. [Q8BFS6-3]
DR   CTD; 55313; -.
DR   MGI; MGI:2443300; Cpped1.
DR   VEuPathDB; HostDB:ENSMUSG00000065979; -.
DR   eggNOG; KOG1378; Eukaryota.
DR   GeneTree; ENSGT00390000008676; -.
DR   HOGENOM; CLU_1712684_0_0_1; -.
DR   InParanoid; Q8BFS6; -.
DR   OMA; YENPSKC; -.
DR   OrthoDB; 908967at2759; -.
DR   PhylomeDB; Q8BFS6; -.
DR   TreeFam; TF329406; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 223978; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Cpped1; mouse.
DR   PRO; PR:Q8BFS6; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8BFS6; protein.
DR   Bgee; ENSMUSG00000065979; Expressed in interventricular septum and 249 other tissues.
DR   ExpressionAtlas; Q8BFS6; baseline and differential.
DR   Genevisible; Q8BFS6; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07395; MPP_CSTP1; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041867; MPP_CSTP1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="Serine/threonine-protein phosphatase CPPED1"
FT                   /id="PRO_0000320557"
FT   REGION          47..250
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRF8"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRF8"
FT   VAR_SEQ         1..138
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031659"
FT   VAR_SEQ         24..37
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031660"
FT   VAR_SEQ         98..153
FT                   /note="TPWRQEQTRDLQRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDD
FT                   YFSF -> GKGKAGGKRKGASEEEPEEEVLGYISSRCFWNSLPSPRPSLSTVLSQAGPQ
FT                   PRDQV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031661"
FT   VAR_SEQ         139..160
FT                   /note="VEEFCQTWGDDYFSFWVGGVLF -> MERSILLRPRRRHSVWTDEG (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031662"
FT   VAR_SEQ         154..312
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031663"
FT   VAR_SEQ         239..266
FT                   /note="IRAVFSGHYHRNAGGTYQNLDMVVSSAI -> NAWGMCMCQPPSATWRSEEG
FT                   TRLGWDRF (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031664"
FT   VAR_SEQ         267..312
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031665"
SQ   SEQUENCE   312 AA;  35248 MW;  F3D4CB7AF800265B CRC64;
     MSAMEAADVF HRARGRTLDA FSSEKEREWK GPFYFVQGAD TQFGLMKAWS TGNCDAGGDE
     WGQEIRLTEQ AVEAINKLNP KPKFFVLCGD LVHAMPGTPW RQEQTRDLQR VLKAVDQDIP
     LVMVSGNHDL GNAPTAETVE EFCQTWGDDY FSFWVGGVLF LVLNSQFLYD ASRCPALKQA
     QDHWLDQQLN IAEQKQCQHA IVFQHIPLFL QSIDEDDDYF NLTKTVRKEL AEKLTRAGIR
     AVFSGHYHRN AGGTYQNLDM VVSSAIGCQL GKDTHGLRVV AITAEKIVHR YYSLDELSQG
     GVEEDLKELL KE
 
 
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