ID   CCPG1_PONAB             Reviewed;         806 AA.
AC   Q5R6R3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Cell cycle progression protein 1;
GN   Name=CCPG1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCPG1 family. {ECO:0000305}.
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DR   EMBL; CR860422; CAH92547.1; -; mRNA.
DR   AlphaFoldDB; Q5R6R3; -.
DR   SMR; Q5R6R3; -.
DR   STRING; 9601.ENSPPYP00000007368; -.
DR   eggNOG; ENOG502QWDZ; Eukaryota.
DR   InParanoid; Q5R6R3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:2001106; P:regulation of Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   InterPro; IPR033588; CCPG1.
DR   PANTHER; PTHR28638:SF2; PTHR28638:SF2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Coiled coil; Membrane; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..806
FT                   /note="Cell cycle progression protein 1"
FT                   /id="PRO_0000310540"
FT   TOPO_DOM        1..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..806
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..307
FT                   /note="Interaction with MCF2L and SRC"
FT                   /evidence="ECO:0000250"
FT   REGION          80..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          305..449
FT                   /evidence="ECO:0000255"
FT   COILED          503..529
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        152..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULG6"
SQ   SEQUENCE   806 AA;  93471 MW;  68606A828E64DBC3 CRC64;
     MSENSSDSDS SCGWTVISHE GSDIEMLNSV TPTNSCEPAP ECSSLEQEEL QALQLEQGES
     SQNGTVLMEE TAYPALEETS STIEAEEEKI PEDNIYIGTA SDDSDIVTLE PPKLEEIGNQ
     EVVIVEEAQS SEDFNMGSSS SSQYTFCQPE TVFSSQPSDD ESSSDETSNQ PSPAFRRRRA
     RKKTVSTSES EDRLVAEQET EPSKESKRQF SSGLNKCVIL ALVIAVSMGF GHFYGTIQIQ
     KRQQLVRKIH EDELNDMKDY LSQCQQEQGS FIDYKSLKEN LARCWTLTEA EKMSFETQKT
     NLATENQYLR VSLEKEEKAL SSLQEELNKL REQIRILEDK GTSTELVKEN QKLKQHLEEE
     KQKKHSFLSQ RETLLTEAKM LKRELERERL VTTALRGELQ QLSGSQLHGK SDSPNVYTEK
     KEIAILRERL TELERKLTFE QQRSDLWERL YVEAKDQSGK QETDGKKKVG RGNHRAKNKS
     KETFLGSVKE TFDAMKNSTK EFVRHHKEKI KQAKEAVKEN LKKFSDSVKS TFRHFKDTTK
     NIFDEKGNKR FGATKAAAEK PRTVFSDYLH PQYKAPTENH HNRGPTMQND GRKEKPVHFK
     EFRKNTNSRK CSPGHACREN SHSFRKACYG VFDCAQQESI SLFNTVVNPI RMDEFRQIIQ
     RYMLKELDTF CHWNELDRFI NKFFLNGVFI HDQKLFTDFV NDVKDYLRNM KEYQVDNDGV
     FEKLDEYIYR HFFGHTFSPP YGPSRPDKKQ RMVNIENSRH RKQEQKHLQP QPYKREGKWH
     KYGRTNGRQM ANLEIELGQL PFDPQY