RHG08_MOUSE
ID RHG08_MOUSE Reviewed; 425 AA.
AC Q9CXP4; Q99JY7;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Rho GTPase-activating protein 8;
DE AltName: Full=Rho-type GTPase-activating protein 8;
GN Name=Arhgap8;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Lung;
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].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 TISSUE SPECIFICITY.
RX PubMed=15225876; DOI=10.1016/j.gene.2004.01.025;
RA Johnstone C.N., Castellvi-Bel S., Chang L.M., Bessa X., Nakagawa H.,
RA Harada H., Sung R.K., Pique J.M., Castells A., Rustgi A.K.;
RT "ARHGAP8 is a novel member of the RHOGAP family related to
RT ARHGAP1/CDC42GAP/p50RHOGAP: mutation and expression analyses in colorectal
RT and breast cancers.";
RL Gene 336:59-71(2004).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, lung and
CC testis, and at lower levels in kidney, stomach and colon. Not detected
CC in heart, liver, spleen, breast, brain, neonatal head or pancreas.
CC {ECO:0000269|PubMed:15225876}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10306.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014171; BAB29190.1; -; mRNA.
DR EMBL; AK086816; BAC39750.1; -; mRNA.
DR EMBL; BC005563; AAH05563.1; -; mRNA.
DR EMBL; BC010306; AAH10306.2; ALT_INIT; mRNA.
DR CCDS; CCDS27712.1; -.
DR RefSeq; NP_001158099.1; NM_001164627.1.
DR RefSeq; NP_001158100.1; NM_001164628.1.
DR RefSeq; NP_001192263.1; NM_001205334.1.
DR RefSeq; NP_082731.2; NM_028455.4.
DR RefSeq; XP_006521533.1; XM_006521470.3.
DR RefSeq; XP_006521534.1; XM_006521471.3.
DR AlphaFoldDB; Q9CXP4; -.
DR SMR; Q9CXP4; -.
DR BioGRID; 215811; 9.
DR IntAct; Q9CXP4; 5.
DR STRING; 10090.ENSMUSP00000132008; -.
DR iPTMnet; Q9CXP4; -.
DR PhosphoSitePlus; Q9CXP4; -.
DR MaxQB; Q9CXP4; -.
DR PaxDb; Q9CXP4; -.
DR PRIDE; Q9CXP4; -.
DR ProteomicsDB; 255258; -.
DR DNASU; 73167; -.
DR Ensembl; ENSMUST00000006029; ENSMUSP00000006029; ENSMUSG00000078954.
DR Ensembl; ENSMUST00000168811; ENSMUSP00000130977; ENSMUSG00000078954.
DR Ensembl; ENSMUST00000172307; ENSMUSP00000132008; ENSMUSG00000078954.
DR GeneID; 73167; -.
DR KEGG; mmu:73167; -.
DR UCSC; uc007xci.2; mouse.
DR CTD; 23779; -.
DR MGI; MGI:1920417; Arhgap8.
DR VEuPathDB; HostDB:ENSMUSG00000078954; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00940000160758; -.
DR HOGENOM; CLU_030214_1_0_1; -.
DR InParanoid; Q9CXP4; -.
DR OMA; ESLPEHH; -.
DR OrthoDB; 1511935at2759; -.
DR PhylomeDB; Q9CXP4; -.
DR TreeFam; TF324164; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 73167; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Prr5; mouse.
DR PRO; PR:Q9CXP4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CXP4; protein.
DR Bgee; ENSMUSG00000078954; Expressed in seminal vesicle and 104 other tissues.
DR Genevisible; Q9CXP4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:2001136; P:negative regulation of endocytic recycling; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW GTPase activation; Reference proteome.
FT CHAIN 1..425
FT /note="Rho GTPase-activating protein 8"
FT /id="PRO_0000056711"
FT DOMAIN 13..168
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 195..381
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 62
FT /note="L -> P (in Ref. 1; BAB29190)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="QP -> HT (in Ref. 1; BAB29190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48972 MW; 4CC08499D7A81F43 CRC64;
MAGLDPTLST SHPFYDVARH GILQVAGDDR QGRRIFTFSC CRLPPLHQLN HQRLLEYLKY
TLDQHVENDY TIVYFHYGLS SQNKPSLGWL QNTYKEFDRK YKKNLKALYV VHPTSLIKAL
WNIFKPLISH KFGKKVTYCS NLRELREHLQ CDQLLIPPEV VRYDEKLQNL HKGQPPPPTK
TPPPRPPLPT QQFGVSLQYL RDKNQGELIP PVLRWTVTYL REKGLRTEGL FRRSASAQTV
RQVQRLYDQG KPVNFDDYGD MHLPAVILKT FLRELPQPLL TFQAYEQILG ITSVESSLRV
THCRLILRSL PEHNYAVLRY LMGFLHEVSL ESISNKMNSS NLACVFGLNL IWPSQGVASL
SALVPLNLFT ELLIEYYDKV FSCQEAPGEH TRDTVEVQQA GPVTKEFMKT GTPRASPYLS
RLRIS
