PP1R7_MOUSE
ID PP1R7_MOUSE Reviewed; 361 AA.
AC Q3UM45; Q9CV31; Q9Z105;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN Name=Ppp1r7; Synonyms=Sds22;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10231361; DOI=10.1046/j.1432-1327.1999.00344.x;
RA Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M., Stalmans W.,
RA Bollen M.;
RT "Structure and splice products of the human gene encoding sds22, a putative
RT mitotic regulator of protein phosphatase-1.";
RL Eur. J. Biochem. 262:36-42(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ;
RA Ceulemans H., Stalmans W., Bollen M.;
RT "Cloning, genomic structure and splice products of the mouse PPP1R7 gene,
RT encoding sds22, a putative mitotic regulator of protein phosphatase-1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP PROTEIN SEQUENCE OF 224-242 AND 246-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12972598; DOI=10.1128/mcb.23.19.6780-6789.2003;
RA Katschinski D.M., Marti H.H., Wagner K.F., Shibata J., Eckhardt K.,
RA Martin F., Depping R., Paasch U., Gassmann M., Ledermann B.,
RA Desbaillets I., Wenger R.H.;
RT "Targeted disruption of the mouse PAS domain serine/threonine kinase
RT PASKIN.";
RL Mol. Cell. Biol. 23:6780-6789(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-45 AND
RP SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Regulatory subunit of protein phosphatase 1. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G. {ECO:0000250}.
CC -!- INTERACTION:
CC Q3UM45; P62137: Ppp1ca; NbExp=3; IntAct=EBI-8318179, EBI-357187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high level in testis.
CC Expression increases during puberty. Expressed in spermatids and
CC probably also in spermatozoa. {ECO:0000269|PubMed:12972598}.
CC -!- SIMILARITY: Belongs to the SDS22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26554.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF067129; AAK08624.1; -; Genomic_DNA.
DR EMBL; AF222867; AAK00624.1; -; mRNA.
DR EMBL; AK009870; BAB26554.1; ALT_FRAME; mRNA.
DR EMBL; AK145136; BAE26253.1; -; mRNA.
DR EMBL; AK162517; BAE36954.1; -; mRNA.
DR EMBL; BC013524; AAH13524.1; -; mRNA.
DR CCDS; CCDS15187.1; -.
DR RefSeq; NP_075689.1; NM_023200.2.
DR AlphaFoldDB; Q3UM45; -.
DR SMR; Q3UM45; -.
DR BioGRID; 211432; 22.
DR IntAct; Q3UM45; 7.
DR STRING; 10090.ENSMUSP00000027494; -.
DR iPTMnet; Q3UM45; -.
DR PhosphoSitePlus; Q3UM45; -.
DR REPRODUCTION-2DPAGE; Q3UM45; -.
DR CPTAC; non-CPTAC-3864; -.
DR EPD; Q3UM45; -.
DR jPOST; Q3UM45; -.
DR MaxQB; Q3UM45; -.
DR PaxDb; Q3UM45; -.
DR PeptideAtlas; Q3UM45; -.
DR PRIDE; Q3UM45; -.
DR ProteomicsDB; 291642; -.
DR DNASU; 66385; -.
DR Ensembl; ENSMUST00000027494; ENSMUSP00000027494; ENSMUSG00000026275.
DR GeneID; 66385; -.
DR KEGG; mmu:66385; -.
DR UCSC; uc007cdv.1; mouse.
DR CTD; 5510; -.
DR MGI; MGI:1913635; Ppp1r7.
DR VEuPathDB; HostDB:ENSMUSG00000026275; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000162473; -.
DR HOGENOM; CLU_044236_1_1_1; -.
DR InParanoid; Q3UM45; -.
DR OMA; YDNLIAH; -.
DR OrthoDB; 968788at2759; -.
DR PhylomeDB; Q3UM45; -.
DR TreeFam; TF105538; -.
DR BioGRID-ORCS; 66385; 22 hits in 70 CRISPR screens.
DR ChiTaRS; Ppp1r7; mouse.
DR PRO; PR:Q3UM45; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UM45; protein.
DR Bgee; ENSMUSG00000026275; Expressed in embryonic post-anal tail and 268 other tissues.
DR ExpressionAtlas; Q3UM45; baseline and differential.
DR Genevisible; Q3UM45; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IDA:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR Pfam; PF12799; LRR_4; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT CHAIN 2..361
FT /note="Protein phosphatase 1 regulatory subunit 7"
FT /id="PRO_0000239614"
FT REPEAT 78..99
FT /note="LRR 1"
FT REPEAT 100..121
FT /note="LRR 2"
FT REPEAT 122..143
FT /note="LRR 3"
FT REPEAT 144..165
FT /note="LRR 4"
FT REPEAT 166..187
FT /note="LRR 5"
FT REPEAT 188..209
FT /note="LRR 6"
FT REPEAT 210..231
FT /note="LRR 7"
FT REPEAT 232..253
FT /note="LRR 8"
FT REPEAT 254..275
FT /note="LRR 9"
FT REPEAT 276..297
FT /note="LRR 10"
FT REPEAT 298..319
FT /note="LRR 11"
FT DOMAIN 332..361
FT /note="LRRCT"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15435"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 39
FT /note="G -> S (in Ref. 3; BAE26253)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="D -> E (in Ref. 3; BAE26253)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="V -> L (in Ref. 3; BAE26253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41292 MW; A31206AFB3BD0F30 CRC64;
MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHGGGGI VANLSEQSLK DGVDRGAEDP
EEEHELAVDM ETINLDRDAE DVDLTHYRIG KIEGLEVLKK VKSLCLRQNL IKCIENLEEL
QSLRELDLYD NQIKKIENLE ALTELEVLDI SFNMLRNIEG IDKLTQLKKL FLVNNKINKI
ENISNLHQLQ MLELGSNRIR AIENIDTLTN LESLFLGKNK ITKLQNLDAL TNLTVLSVQS
NRLAKIEGLQ SLVNLRELYL SNNGIEVIEG LENNNKLTML DIASNRIKKI ENISHLTELQ
EFWMNDNLLE SWSDLDELKG ARSLETVYLE RNPLQKDPQY RRKVMLALPS VRQIDATYVR
F
