RHG19_MOUSE
ID RHG19_MOUSE Reviewed; 494 AA.
AC Q8BRH3; B9EI55; Q0VGS7; Q5DU53; Q9D468;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Rho GTPase-activating protein 19;
DE AltName: Full=Rho-type GTPase-activating protein 19;
GN Name=Arhgap19;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-494 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BRH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRH3-2; Sequence=VSP_023702;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK016763; BAB30415.1; -; mRNA.
DR EMBL; AK044841; BAC32114.1; -; mRNA.
DR EMBL; BC086680; AAH86680.1; ALT_INIT; mRNA.
DR EMBL; BC139195; AAI39196.1; -; mRNA.
DR EMBL; AK220317; BAD90233.1; -; mRNA.
DR CCDS; CCDS37989.1; -. [Q8BRH3-1]
DR RefSeq; NP_001156967.1; NM_001163495.1.
DR RefSeq; NP_081943.2; NM_027667.3. [Q8BRH3-1]
DR AlphaFoldDB; Q8BRH3; -.
DR SMR; Q8BRH3; -.
DR BioGRID; 214464; 10.
DR STRING; 10090.ENSMUSP00000026150; -.
DR iPTMnet; Q8BRH3; -.
DR PhosphoSitePlus; Q8BRH3; -.
DR EPD; Q8BRH3; -.
DR jPOST; Q8BRH3; -.
DR MaxQB; Q8BRH3; -.
DR PaxDb; Q8BRH3; -.
DR PRIDE; Q8BRH3; -.
DR ProteomicsDB; 254874; -. [Q8BRH3-1]
DR ProteomicsDB; 254875; -. [Q8BRH3-2]
DR DNASU; 71085; -.
DR Ensembl; ENSMUST00000026150; ENSMUSP00000026150; ENSMUSG00000025154. [Q8BRH3-1]
DR Ensembl; ENSMUST00000177495; ENSMUSP00000135293; ENSMUSG00000025154. [Q8BRH3-2]
DR GeneID; 71085; -.
DR KEGG; mmu:71085; -.
DR UCSC; uc008hmh.2; mouse. [Q8BRH3-1]
DR UCSC; uc012blt.1; mouse. [Q8BRH3-2]
DR CTD; 84986; -.
DR MGI; MGI:1918335; Arhgap19.
DR VEuPathDB; HostDB:ENSMUSG00000025154; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00940000157331; -.
DR HOGENOM; CLU_046228_0_0_1; -.
DR InParanoid; Q8BRH3; -.
DR OMA; CQSPANQ; -.
DR OrthoDB; 878646at2759; -.
DR PhylomeDB; Q8BRH3; -.
DR TreeFam; TF326309; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 71085; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Arhgap19; mouse.
DR PRO; PR:Q8BRH3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BRH3; protein.
DR Bgee; ENSMUSG00000025154; Expressed in otolith organ and 168 other tissues.
DR ExpressionAtlas; Q8BRH3; baseline and differential.
DR Genevisible; Q8BRH3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT CHAIN 2..494
FT /note="Rho GTPase-activating protein 19"
FT /id="PRO_0000280466"
FT DOMAIN 102..308
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 399..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14CB8"
FT VAR_SEQ 332..346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023702"
FT CONFLICT 490
FT /note="R -> G (in Ref. 1; BAC32114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55734 MW; 37F366BF042343AC CRC64;
MAAEAPSGGE APVCDSGRSD AICNFVICND SPLRGQPIIF NPDFFVEKLR HEKPEVFTEL
VVSNITRLID LPGTELAQLM GEVDLKLPGG AGPAAGFFRS LMSLKRKEKG VVFGSPLTEE
GIAQIYQLIE YLHKNLRVEG LFRVPGNSVR QQLLRDALNN GTDIDLDSGE FHSNDVATLL
KMFLGELPEP LLTHKHFHVH LKIADLMQFD DKGNKTNIPD KERQIEALQL LFLILPPANR
NLLKLLLDLL YQTAKKQDKN KMSAHNLALM FAPHVLWPKN VTANDLQENI IKLNTGMAFM
IKHSQKLFKA PAYIRECARL YYLGSRTQMS KDDLDLTTSC HNMSFQLARC QRQNRVDPSS
QQEETQQHTE EALRELFQHV HNWPDSAKKK QLLRQFHKQS LTQTPGREPS TPRVQKRARS
RSFSGLIKRK VLGSQMTSEK KNSSPAPESV AMGELKKASK ENMNLFFSGS PAGTVTPTRL
KWSEAKREGR KGFF
