CCPG1_MOUSE
ID CCPG1_MOUSE Reviewed; 753 AA.
AC Q640L3; Q05BJ9; Q8C692; Q922W9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cell cycle progression protein 1;
GN Name=Ccpg1;
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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Head, and 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 INTERACTION WITH MCF2; MCF2L; ARHGEF1; BCR; VAV1; FGD1; CDC42 AND SRC,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
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: Acts as an assembly platform for Rho protein signaling
CC complexes. Limits guanine nucleotide exchange activity of MCF2L toward
CC RHOA, which results in an inhibition of both its transcriptional
CC activation ability and its transforming activity. Does not inhibit
CC activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA
CC or CDC42. May be involved in cell cycle regulation.
CC {ECO:0000269|PubMed:17000758}.
CC -!- SUBUNIT: Interacts with MCF2L. May interact with MCF2, ARHGEF1, BCR,
CC VAV1 and FGD1, but not with TIAM1. Interacts with GTP-bound CDC42 and
CC SRC. {ECO:0000269|PubMed:17000758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC {ECO:0000269|PubMed:17000758}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17000758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q640L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q640L3-2; Sequence=VSP_029318;
CC Name=3;
CC IsoId=Q640L3-3; Sequence=VSP_029317;
CC -!- SIMILARITY: Belongs to the CCPG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK076325; BAC36301.2; -; mRNA.
DR EMBL; BC006717; AAH06717.1; ALT_INIT; mRNA.
DR EMBL; BC043049; AAH43049.1; -; mRNA.
DR EMBL; BC082602; AAH82602.1; -; mRNA.
DR CCDS; CCDS23334.1; -. [Q640L3-3]
DR CCDS; CCDS52855.1; -. [Q640L3-1]
DR CCDS; CCDS72278.1; -. [Q640L3-2]
DR RefSeq; NP_001107800.1; NM_001114328.2. [Q640L3-1]
DR RefSeq; NP_001273473.1; NM_001286544.1. [Q640L3-2]
DR RefSeq; NP_001273474.1; NM_001286545.1.
DR RefSeq; NP_001273475.1; NM_001286546.1.
DR RefSeq; NP_082457.3; NM_028181.5. [Q640L3-3]
DR AlphaFoldDB; Q640L3; -.
DR SMR; Q640L3; -.
DR IntAct; Q640L3; 1.
DR STRING; 10090.ENSMUSP00000122966; -.
DR iPTMnet; Q640L3; -.
DR PhosphoSitePlus; Q640L3; -.
DR MaxQB; Q640L3; -.
DR PaxDb; Q640L3; -.
DR PRIDE; Q640L3; -.
DR ProteomicsDB; 279946; -. [Q640L3-1]
DR ProteomicsDB; 279947; -. [Q640L3-2]
DR ProteomicsDB; 279948; -. [Q640L3-3]
DR Antibodypedia; 57643; 66 antibodies from 19 providers.
DR DNASU; 72278; -.
DR Ensembl; ENSMUST00000037977; ENSMUSP00000045669; ENSMUSG00000034563. [Q640L3-3]
DR Ensembl; ENSMUST00000085350; ENSMUSP00000082458; ENSMUSG00000034563. [Q640L3-2]
DR Ensembl; ENSMUST00000150826; ENSMUSP00000122966; ENSMUSG00000034563. [Q640L3-1]
DR GeneID; 72278; -.
DR KEGG; mmu:72278; -.
DR UCSC; uc009qqm.3; mouse. [Q640L3-1]
DR UCSC; uc009qqo.3; mouse. [Q640L3-3]
DR UCSC; uc009qqp.3; mouse. [Q640L3-2]
DR CTD; 9236; -.
DR MGI; MGI:1196419; Ccpg1.
DR VEuPathDB; HostDB:ENSMUSG00000034563; -.
DR eggNOG; ENOG502QWDZ; Eukaryota.
DR GeneTree; ENSGT00940000160497; -.
DR HOGENOM; CLU_018722_0_0_1; -.
DR InParanoid; Q640L3; -.
DR OMA; LDAFHHW; -.
DR OrthoDB; 667993at2759; -.
DR PhylomeDB; Q640L3; -.
DR TreeFam; TF333202; -.
DR BioGRID-ORCS; 72278; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ccpg1; mouse.
DR PRO; PR:Q640L3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q640L3; protein.
DR Bgee; ENSMUSG00000034563; Expressed in granulocyte and 253 other tissues.
DR ExpressionAtlas; Q640L3; baseline and differential.
DR Genevisible; Q640L3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:2001106; P:regulation of Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR InterPro; IPR033588; CCPG1.
DR PANTHER; PTHR28638:SF2; PTHR28638:SF2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..753
FT /note="Cell cycle progression protein 1"
FT /id="PRO_0000310539"
FT TOPO_DOM 1..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..753
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..307
FT /note="Interaction with MCF2L and SRC"
FT /evidence="ECO:0000269|PubMed:17000758"
FT REGION 57..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..449
FT /evidence="ECO:0000255"
FT COILED 503..529
FT /evidence="ECO:0000255"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG6"
FT VAR_SEQ 630..753
FT /note="GMFECAGQEAISPVNKASPVRMNDFKQLIHWYLLNELETFHHWKELDQFISP
FT FFPNGVFRHDQQLFADFVDDVKGYLKSIKEYRVEDGNLEKLDGCIYRHFGHVFALPFGP
FT RSVYIKPCYYNSF -> VDLIKSNVW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029317"
FT VAR_SEQ 741..753
FT /note="RSVYIKPCYYNSF -> SRPDKKQRMVTIENARHRKQEQKHLHPQPYEREGK
FT WQKYGRANGRHTANLELELGQLPFDPKY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029318"
FT CONFLICT 156
FT /note="S -> C (in Ref. 1; BAC36301)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> R (in Ref. 1; BAC36301)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> S (in Ref. 2; AAH82602)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Missing (in Ref. 2; AAH82602)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="P -> S (in Ref. 2; AAH82602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 86126 MW; EBE1C35E53A7CC5F CRC64;
MSESSSDSDS SCGWTVINHE GSDIEIVNSA TASDNCGLTL ECSLVEQEEL PVLYVGHGGE
ESSANNTSSV GETMLSSMRE TKSAAEVEEA PSPEDNVYFG TTSDDSDIVT LEPPKLEEMG
NQEVTIQEAP SSDDLNMGSS SSSQYAFCQP EPVFSSQPSD EESSSDDTSH EPSPAPRRRR
NRKKTVSISE SEEPPLAEPE DEPSKEPSKR HFSRGLNKCV ILALVIAVSM GFGHFYGTIQ
IQKQLVRKTH EDELDGVKGY LSQRKQEQES FLDFKSLKEN LERCWTVTES EKITFETQKK
NLAAENQYLR ISLEKEEQAL SSLQEELRQL REQIRLLEDK GTSTQLVREN QVLKQYLEVE
KQKTDSFLRE REMLLEEARM LKRDLEREQL TAMALRAELE QFIPGQAQSR AESPSVQTEE
KEVGLLQQRL AELEQKLIFE QQRSDLWERL YVEAKDQHGK QETDGRKRGS RGSHRAKSKS
KETFLGTVKE TFDAMKNSTK EFVRHHKEKI KQAKEAVKEN LKKFSDSVKS TFRHFKDTTK
NIFDEKGSKR FRAPKEAATE KTRTAYSYSS YSQQEAPNQN QNCRRPSAQR DGGREKPSHS
EEIRKNANSY TYKAKSDCRG THSTRRVCSG MFECAGQEAI SPVNKASPVR MNDFKQLIHW
YLLNELETFH HWKELDQFIS PFFPNGVFRH DQQLFADFVD DVKGYLKSIK EYRVEDGNLE
KLDGCIYRHF GHVFALPFGP RSVYIKPCYY NSF
