Q9WVM1 (RGAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 108. History...
Names and origin
|Protein names||Recommended name:|
Rac GTPase-activating protein 1
Male germ cell RacGap
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||628 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. Ref.1 Ref.2 Ref.3 Ref.6
Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct By similarity.
Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Cytoplasmic vesicle › secretory vesicle › acrosome. Cleavage furrow By similarity. Midbody By similarity. Note: During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody. Colocalizes with RHOA at the myosin contractile ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalizes with Cdc42 to spindle microtubules from prometaphase to telophase By similarity. Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome. Ref.7
Highly expressed in testis, thymus and spleen and weakly expressed in brain, heart, skeletal muscle and kidney. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Not detected in adult liver. Also expressed in fetal liver and in several hematopoietic cell lines. Ref.2 Ref.3 Ref.6
At E6.5 expressed in primitive endoderm, embryonic ectoderm, extraembryonic ectoderm and the ectoplacental cone. By E7.5, a widespread expression was observed in all intra- and extraembryonic tissues and also in the giant cells lining the inner boundary of the deciduum. At E9.5, expression was elevated in the neuroepithelium of the brain ventricles and the neural tube. By E12.5, expression remains widespread and in the brain higher levels were observed in the ventricular zone of the two telencephalic lobes, and in the mesencephalon and diencephalon, with the exception of the median sulcus. In adult brain, highest levels of expression were detected in cerebellum, specifically the Purkinje cell layer extending into the molecular layer. Ref.3
Expression is down-regulated during macrophage differentiation of M1 cells. Ref.2
The coiled coil region is indispensible for localization to the midbody during cytokinesis By similarity. UniProtKB Q9P2W2
Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on Ser-388 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation By similarity.
Contains 1 phorbol-ester/DAG-type zinc finger.
Contains 1 Rho-GAP domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 628||628||Rac GTPase-activating protein 1||PRO_0000228809|
|Domain||350 – 540||191||Rho-GAP|
|Zinc finger||287 – 336||50||Phorbol-ester/DAG-type|
|Region||107 – 286||180||Interaction with SLC26A8 By similarity|
|Coiled coil||33 – 110||78||Potential|
Amino acid modifications
|Modified residue||150||1||Phosphoserine; by PLK1 By similarity|
|Modified residue||155||1||Phosphoserine By similarity|
|Modified residue||158||1||Phosphoserine; by PLK1 By similarity|
|Modified residue||162||1||Phosphothreonine By similarity|
|Modified residue||165||1||Phosphoserine; by PLK1 By similarity|
|Modified residue||171||1||Phosphoserine; by PLK1 By similarity|
|Modified residue||204||1||Phosphoserine By similarity|
|Modified residue||207||1||Phosphoserine By similarity|
|Modified residue||215||1||Phosphoserine By similarity|
|Modified residue||258||1||Phosphoserine By similarity|
|Modified residue||343||1||Phosphothreonine By similarity|
|Modified residue||388||1||Phosphoserine; by AURKB By similarity|
|Modified residue||411||1||Phosphoserine; by AURKB By similarity|
|Modified residue||564||1||Phosphothreonine By similarity|
|Modified residue||577||1||Phosphothreonine By similarity|
|Modified residue||585||1||Phosphothreonine By similarity|
|Modified residue||602||1||Phosphothreonine By similarity|
|Sequence conflict||29 – 31||3||IEF → MES in BAE38561. Ref.4|
|Sequence conflict||100||1||Q → E in BAE40131. Ref.4|
|Sequence conflict||100||1||Q → E in BAE40010. Ref.4|
|Sequence conflict||398||1||K → E in BAE40005. Ref.4|
|Sequence conflict||623||1||P → T in BAE40005. Ref.4|
|||"Identification and characterization of a transcript for a novel Rac GTPase-activating protein in terminally differentiating 3T3-L1 adipocytes."|
Wooltorton E.J., Haliotis T., Mueller C.R.
DNA Cell Biol. 18:265-273(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
|||"MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells."|
Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y., Nosaka T., Kitamura T.
Blood 96:2116-2124(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
|||"Mice with a homozygous gene trap vector insertion in mgcRacGAP die during pre-implantation development."|
Van de Putte T., Zwijsen A., Lonnoy O., Rybin V., Cozijnsen M., Francis A., Baekelandt V., Kozak C.A., Zerial M., Huylebroeck D.
Mech. Dev. 102:33-44(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
|||"The transcriptional landscape of the mammalian genome."|
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J, DBA/2 and NOD.
Tissue: Heart and Lung.
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
|||"Structure and expression of murine mgcRacGAP: its developmental regulation suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis."|
Arar C., Ott M.-O., Toure A., Gacon G.
Biochem. J. 343:225-230(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
|||"Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells."|
Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G.
Biochem. J. 372:105-112(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
|+||Additional computationally mapped references.|
|AF079974 mRNA. Translation: AAD40487.1.|
AB030252 mRNA. Translation: BAA90248.1.
AF212320 mRNA. Translation: AAG43539.1.
AF212321 mRNA. Translation: AAG43540.1.
AK144608 mRNA. Translation: BAE25967.1.
AK154929 mRNA. Translation: BAE32931.1.
AK165897 mRNA. Translation: BAE38446.1.
AK166084 mRNA. Translation: BAE38561.1.
AK168020 mRNA. Translation: BAE40005.1.
AK168025 mRNA. Translation: BAE40010.1.
AK168170 mRNA. Translation: BAE40131.1.
AK168679 mRNA. Translation: BAE40528.1.
BC010715 mRNA. Translation: AAH10715.1.
|RefSeq||NP_001240737.1. NM_001253808.1. |
3D structure databases
|SMR||Q9WVM1. Positions 283-547. |
Protein-protein interaction databases
|IntAct||Q9WVM1. 9 interactions.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000023756; ENSMUSP00000023756; ENSMUSG00000023015. |
ENSMUST00000171702; ENSMUSP00000126417; ENSMUSG00000023015.
|UCSC||uc007xpx.1. mouse. |
|MGI||MGI:1349423. Racgap1. |
Gene expression databases
|GermOnline||ENSMUSG00000023015. Mus musculus. |
Family and domain databases
|Gene3D||1.10.555.10. 1 hit. |
|InterPro||IPR002219. Prot_Kinase_C-like_PE/DAG-bd. |
|Pfam||PF00130. C1_1. 1 hit. |
PF00620. RhoGAP. 1 hit.
|SMART||SM00109. C1. 1 hit. |
SM00324. RhoGAP. 1 hit.
|SUPFAM||SSF48350. Rho_GAP. 1 hit. |
|PROSITE||PS50238. RHOGAP. 1 hit. |
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
|ChiTaRS||RACGAP1. mouse. |
|Accession||Primary (citable) accession number: Q9WVM1|
Secondary accession number(s): Q3THR5, Q3TI41, Q3TM81
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|