ID RGAP1_MOUSE Reviewed; 628 AA.
AC Q9WVM1; Q3THR5; Q3TI41; Q3TM81;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=Rac GTPase-activating protein 1;
DE AltName: Full=Male germ cell RacGap;
DE Short=MgcRacGAP;
GN Name=Racgap1 {ECO:0000312|MGI:MGI:1349423}; Synonyms=Mgcracgap;
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] {ECO:0000305, ECO:0000312|EMBL:AAD40487.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Erythroleukemia {ECO:0000269|PubMed:10235109};
RX PubMed=10235109; DOI=10.1089/104454999315321;
RA Wooltorton E.J., Haliotis T., Mueller C.R.;
RT "Identification and characterization of a transcript for a novel Rac
RT GTPase-activating protein in terminally differentiating 3T3-L1
RT adipocytes.";
RL DNA Cell Biol. 18:265-273(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA90248.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10979956;
RA Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y.,
RA Nosaka T., Kitamura T.;
RT "MgcRacGAP is involved in the control of growth and differentiation of
RT hematopoietic cells.";
RL Blood 96:2116-2124(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG43539.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAG43539.1};
RX PubMed=11287179; DOI=10.1016/s0925-4773(01)00279-9;
RA Van de Putte T., Zwijsen A., Lonnoy O., Rybin V., Cozijnsen M., Francis A.,
RA Baekelandt V., Kozak C.A., Zerial M., Huylebroeck D.;
RT "Mice with a homozygous gene trap vector insertion in mgcRacGAP die during
RT pre-implantation development.";
RL Mech. Dev. 102:33-44(2001).
RN [4] {ECO:0000312|EMBL:BAE32931.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE40528.1},
RC DBA/2J {ECO:0000312|EMBL:BAE40131.1}, and
RC NOD {ECO:0000312|EMBL:BAE32931.1};
RC TISSUE=Heart {ECO:0000312|EMBL:BAE40528.1}, and
RC Lung {ECO:0000312|EMBL:BAE38446.1};
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 [5] {ECO:0000312|EMBL:AAH10715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10715.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH10715.1};
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 [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10493933; DOI=10.1042/bj3430225;
RA Arar C., Ott M.-O., Toure A., Gacon G.;
RT "Structure and expression of murine mgcRacGAP: its developmental regulation
RT suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis.";
RL Biochem. J. 343:225-230(1999).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=12590651; DOI=10.1042/bj20021652;
RA Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D.,
RA Chardin P., Gacon G.;
RT "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male
RT germ cells.";
RL Biochem. J. 372:105-112(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564; THR-577 AND THR-585, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: Component of the centralspindlin complex that serves as a
CC microtubule-dependent and Rho-mediated signaling required for the
CC myosin contractile ring formation during the cell cycle cytokinesis.
CC Required for proper attachment of the midbody to the cell membrane
CC during cytokinesis. Sequentially binds to ECT2 and RAB11FIP3 which
CC regulates cleavage furrow ingression and abscission during cytokinesis.
CC Plays key roles in controlling cell growth and differentiation of
CC hematopoietic cells through mechanisms other than regulating Rac GTPase
CC activity. Has a critical role in erythropoiesis (By similarity). Also
CC involved in the regulation of growth-related processes in adipocytes
CC and myoblasts. May be involved in regulating spermatogenesis and in the
CC RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase
CC activation) activity towards CDC42 and RAC1 and less towards RHOA.
CC Essential for the early stages of embryogenesis. May play a role in
CC regulating cortical activity through RHOA during cytokinesis. May
CC participate in the regulation of sulfate transport in male germ cells.
CC {ECO:0000250|UniProtKB:Q9H0H5, ECO:0000269|PubMed:10235109,
CC ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956,
CC ECO:0000269|PubMed:11287179}.
CC -!- SUBUNIT: Heterotetramer of two molecules each of RACGAP1 and KIF23.
CC Found in the centralspindlin complex. Associates with alpha-, beta- and
CC gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with
CC RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP
CC domain and basic region with PRC1. The interaction with PRC1 inhibits
CC its GAP activity towards CDC42 in vitro, which may be required for
CC maintaining normal spindle morphology. Interacts with SLC26A8 via its
CC N-terminus. Interacts with ECT2; the interaction is direct, occurs at
CC anaphase and during cytokinesis in a microtubule-dependent manner, is
CC enhanced by phosphorylation by PLK1 and phosphorylation at Ser-165
CC plays a major role in mediating binding. Interacts with RAB11FIP3; the
CC interaction occurs at late telophase. Interacts with KIF23; the
CC interaction is direct. {ECO:0000250|UniProtKB:Q9H0H5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12590651}. Cytoplasm
CC {ECO:0000269|PubMed:12590651}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:12590651}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:12590651}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q9H0H5}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q9H0H5}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H0H5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H0H5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H0H5}. Note=During interphase, localized to
CC the nucleus and cytoplasm along with microtubules, in anaphase, is
CC redistributed to the central spindle and, in telophase and cytokinesis,
CC to the midbody ring, also called Flemming body. Colocalizes with RHOA
CC at the myosin contractile ring during cytokinesis. Colocalizes with
CC ECT2 to the mitotic spindles during anaphase/metaphase, the cleavage
CC furrow during telophase and at the midbody at the end of cytokinesis.
CC Colocalizes with Cdc42 to spindle microtubules from prometaphase to
CC telophase (By similarity). Colocalizes with RND2 in Golgi-derived
CC proacrosomal vesicles and the acrosome. {ECO:0000250|UniProtKB:Q9H0H5}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, thymus and spleen and
CC weakly expressed in brain, heart, skeletal muscle and kidney. In
CC testis, expression is restricted to germ cells with the highest levels
CC of expression found in spermatocytes. Not detected in adult liver. Also
CC expressed in fetal liver and in several hematopoietic cell lines.
CC {ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956,
CC ECO:0000269|PubMed:11287179}.
CC -!- DEVELOPMENTAL STAGE: At 6.5 dpc expressed in primitive endoderm,
CC embryonic ectoderm, extraembryonic ectoderm and the ectoplacental cone.
CC By 7.5 dpc, a widespread expression was observed in all intra- and
CC extraembryonic tissues and also in the giant cells lining the inner
CC boundary of the deciduum. At 9.5 dpc, expression was elevated in the
CC neuroepithelium of the brain ventricles and the neural tube. By 12.5
CC dpc, expression remains widespread and in the brain higher levels were
CC observed in the ventricular zone of the two telencephalic lobes, and in
CC the mesencephalon and diencephalon, with the exception of the median
CC sulcus. In adult brain, highest levels of expression were detected in
CC cerebellum, specifically the Purkinje cell layer extending into the
CC molecular layer. {ECO:0000269|PubMed:11287179}.
CC -!- INDUCTION: Expression is down-regulated during macrophage
CC differentiation of M1 cells. {ECO:0000269|PubMed:10979956}.
CC -!- DOMAIN: The coiled coil region is indispensible for localization to the
CC midbody during cytokinesis. {ECO:0000250|UniProtKB:Q9P2W2}.
CC -!- DOMAIN: The phorbol-ester/DAG-type zinc finger domain mediates
CC interaction with membranes enriched in phosphatidylinositol 3,4,5-
CC trisphosphate and is required during mitotic cytokinesis for normal
CC attachment of the midbody to the cell membrane. {ECO:0000250}.
CC -!- PTM: Phosphorylated at multiple sites in the midbody during cytokinesis
CC (By similarity). Phosphorylation by AURKB on Ser-388 at the midbody is,
CC at least in part, responsible for exerting its latent GAP activity
CC towards RhoA (By similarity). Phosphorylation on multiple serine
CC residues by PLK1 enhances its association with ECT2 and is critical for
CC cleavage furrow formation (By similarity). Phosphorylation on Ser-165
CC plays a major role in mediating interaction with ECT2 (By similarity).
CC Phosphorylation on Ser-158 does not appear to contribute to binding to
CC ECT2 (By similarity). {ECO:0000250|UniProtKB:Q9H0H5}.
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DR EMBL; AF079974; AAD40487.1; -; mRNA.
DR EMBL; AB030252; BAA90248.1; -; mRNA.
DR EMBL; AF212320; AAG43539.1; -; mRNA.
DR EMBL; AF212321; AAG43540.1; -; mRNA.
DR EMBL; AK144608; BAE25967.1; -; mRNA.
DR EMBL; AK154929; BAE32931.1; -; mRNA.
DR EMBL; AK165897; BAE38446.1; -; mRNA.
DR EMBL; AK166084; BAE38561.1; -; mRNA.
DR EMBL; AK168020; BAE40005.1; -; mRNA.
DR EMBL; AK168025; BAE40010.1; -; mRNA.
DR EMBL; AK168170; BAE40131.1; -; mRNA.
DR EMBL; AK168679; BAE40528.1; -; mRNA.
DR EMBL; BC010715; AAH10715.1; -; mRNA.
DR CCDS; CCDS27825.1; -.
DR RefSeq; NP_001240737.1; NM_001253808.1.
DR RefSeq; NP_001240738.1; NM_001253809.1.
DR RefSeq; NP_036155.1; NM_012025.7.
DR RefSeq; XP_011243948.1; XM_011245646.1.
DR AlphaFoldDB; Q9WVM1; -.
DR SMR; Q9WVM1; -.
DR BioGRID; 205072; 48.
DR DIP; DIP-42340N; -.
DR IntAct; Q9WVM1; 46.
DR MINT; Q9WVM1; -.
DR STRING; 10090.ENSMUSP00000126417; -.
DR iPTMnet; Q9WVM1; -.
DR PhosphoSitePlus; Q9WVM1; -.
DR EPD; Q9WVM1; -.
DR jPOST; Q9WVM1; -.
DR MaxQB; Q9WVM1; -.
DR PaxDb; 10090-ENSMUSP00000023756; -.
DR PeptideAtlas; Q9WVM1; -.
DR ProteomicsDB; 253121; -.
DR Pumba; Q9WVM1; -.
DR Antibodypedia; 14118; 666 antibodies from 41 providers.
DR DNASU; 26934; -.
DR Ensembl; ENSMUST00000023756.12; ENSMUSP00000023756.6; ENSMUSG00000023015.15.
DR Ensembl; ENSMUST00000171702.8; ENSMUSP00000126417.2; ENSMUSG00000023015.15.
DR GeneID; 26934; -.
DR KEGG; mmu:26934; -.
DR UCSC; uc007xpx.2; mouse.
DR AGR; MGI:1349423; -.
DR CTD; 29127; -.
DR MGI; MGI:1349423; Racgap1.
DR VEuPathDB; HostDB:ENSMUSG00000023015; -.
DR eggNOG; KOG3564; Eukaryota.
DR GeneTree; ENSGT00940000154610; -.
DR HOGENOM; CLU_026187_1_0_1; -.
DR InParanoid; Q9WVM1; -.
DR OMA; ECKMPIS; -.
DR OrthoDB; 22770at2759; -.
DR PhylomeDB; Q9WVM1; -.
DR TreeFam; TF318102; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 26934; 25 hits in 84 CRISPR screens.
DR ChiTaRS; Racgap1; mouse.
DR PRO; PR:Q9WVM1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9WVM1; Protein.
DR Bgee; ENSMUSG00000023015; Expressed in ventricular zone and 234 other cell types or tissues.
DR ExpressionAtlas; Q9WVM1; baseline and differential.
DR Genevisible; Q9WVM1; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0097149; C:centralspindlin complex; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; ISS:UniProtKB.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007405; P:neuroblast proliferation; IEP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0008272; P:sulfate transport; ISO:MGI.
DR CDD; cd20821; C1_MgcRacGAP; 1.
DR CDD; cd04382; RhoGAP_MgcRacGAP; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR46199; RAC GTPASE-ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR46199:SF1; RAC GTPASE-ACTIVATING PROTEIN 1; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cell membrane; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
KW Differentiation; GTPase activation; Ion transport; Isopeptide bond;
KW Lipid-binding; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Transport; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..628
FT /note="Rac GTPase-activating protein 1"
FT /id="PRO_0000228809"
FT DOMAIN 350..540
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 287..336
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 107..286
FT /note="Interaction with SLC26A8"
FT /evidence="ECO:0000250"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..110
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 150
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 158
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 165
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 171
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 388
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 411
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H0H5"
FT CONFLICT 29..31
FT /note="IEF -> MES (in Ref. 4; BAE38561)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Q -> E (in Ref. 4; BAE40131/BAE40010)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="K -> E (in Ref. 4; BAE40005)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="P -> T (in Ref. 4; BAE40005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 70158 MW; 8D1B9DEC3CE057BE CRC64;
MDTTMVNLWT LFEQLVRRME IINEGNESIE FIQVVKDFED FRKKYQRTNQ ELEKFKDLLL
KAETGRSALD VKLKHARNQV DVEIKRRQRA EAECAKLEQQ IQLIRDILMC DTSGSIQLSE
EQKSALAFLN RGQASSGHAG NNRLSTIDES GSILSDISFD KTDESLDWDS SLVKNFKMKK
REKRRSNSRQ FIDGPPGPVK KTCSIGSTVD QANESIVAKT TVTVPSDGGP IEAVSTIETL
PSWTRSRGKS GPLQPVNSDS ALNSRPLEPR TDTDNLGTPQ NTGGMRLHDF VSKTVIKPES
CVPCGKRIKF GKLSLKCRDC RLVSHPECRD RCPLPCIPPL VGTPVKIGEG MLADFVSQAS
PMIPAIVVSC VNEIEQRGLT EAGLYRISGC DRTVKELKEK FLKVKTVPLL SKVDDIHVIC
SLLKDFLRNL KEPLLTFWLS KAFMEAAEIT DEDNSTAAMY QAVSELPQAN RDTLAFLMIH
LQRVSQSPDT KMDIANLAKV FGPTIVAHTV PNPDPVTMFQ DIKRQLKVVE RLLSLPLEYW
NQFMMVDQEN IDSQRGNGNS TPRTPDVKVS LLGPVTTPEF QLVKTPLSSS LSQRLYNLSK
STPRFGNKSK SATNLGQQGK FFPAPYLK
//
