ARGAL_MOUSE
ID ARGAL_MOUSE Reviewed; 1280 AA.
AC A2AWP8; A2AWP5; A2AWP9; A2AWQ0; A2AWQ1; Q6PCQ2; Q6ZPL3; Q8C1A1; Q8VDH5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Rho guanine nucleotide exchange factor 10-like protein;
DE AltName: Full=GrinchGEF;
GN Name=Arhgef10l; Synonyms=Kiaa1626;
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] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 561-1280 (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-152, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, and Pancreas;
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: Acts as guanine nucleotide exchange factor (GEF) for RHOA,
CC RHOB and RHOC. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RHOA, RHOB and RHOC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A2AWP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AWP8-2; Sequence=VSP_034428;
CC Name=3;
CC IsoId=A2AWP8-3; Sequence=VSP_034428, VSP_034431;
CC Name=4;
CC IsoId=A2AWP8-4; Sequence=VSP_034431;
CC Name=5;
CC IsoId=A2AWP8-5; Sequence=VSP_034427, VSP_034429, VSP_034430,
CC VSP_034431;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129408; BAC98218.1; ALT_INIT; mRNA.
DR EMBL; AK028648; BAC26047.1; -; mRNA.
DR EMBL; AL929073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX530090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021843; AAH21843.1; -; mRNA.
DR EMBL; BC059220; AAH59220.1; -; mRNA.
DR CCDS; CCDS51342.1; -. [A2AWP8-3]
DR CCDS; CCDS51343.1; -. [A2AWP8-2]
DR CCDS; CCDS51344.1; -. [A2AWP8-4]
DR CCDS; CCDS71507.1; -. [A2AWP8-1]
DR RefSeq; NP_001106193.1; NM_001112722.1. [A2AWP8-2]
DR RefSeq; NP_001106194.1; NM_001112723.1. [A2AWP8-3]
DR RefSeq; NP_001277732.1; NM_001290803.1. [A2AWP8-1]
DR RefSeq; NP_766003.3; NM_172415.3. [A2AWP8-4]
DR RefSeq; XP_006539264.1; XM_006539201.3. [A2AWP8-1]
DR RefSeq; XP_006539265.1; XM_006539202.1. [A2AWP8-1]
DR RefSeq; XP_011248639.1; XM_011250337.2. [A2AWP8-1]
DR RefSeq; XP_011248642.1; XM_011250340.2. [A2AWP8-3]
DR RefSeq; XP_017175885.1; XM_017320396.1. [A2AWP8-1]
DR AlphaFoldDB; A2AWP8; -.
DR SMR; A2AWP8; -.
DR IntAct; A2AWP8; 1.
DR STRING; 10090.ENSMUSP00000040531; -.
DR iPTMnet; A2AWP8; -.
DR PhosphoSitePlus; A2AWP8; -.
DR MaxQB; A2AWP8; -.
DR PaxDb; A2AWP8; -.
DR PeptideAtlas; A2AWP8; -.
DR PRIDE; A2AWP8; -.
DR ProteomicsDB; 277278; -. [A2AWP8-1]
DR ProteomicsDB; 277279; -. [A2AWP8-2]
DR ProteomicsDB; 277280; -. [A2AWP8-3]
DR ProteomicsDB; 277281; -. [A2AWP8-4]
DR ProteomicsDB; 277282; -. [A2AWP8-5]
DR Antibodypedia; 29390; 44 antibodies from 12 providers.
DR Ensembl; ENSMUST00000039204; ENSMUSP00000040531; ENSMUSG00000040964. [A2AWP8-4]
DR Ensembl; ENSMUST00000069623; ENSMUSP00000066249; ENSMUSG00000040964. [A2AWP8-2]
DR Ensembl; ENSMUST00000097820; ENSMUSP00000095431; ENSMUSG00000040964. [A2AWP8-3]
DR Ensembl; ENSMUST00000105797; ENSMUSP00000101423; ENSMUSG00000040964. [A2AWP8-5]
DR Ensembl; ENSMUST00000105799; ENSMUSP00000101425; ENSMUSG00000040964. [A2AWP8-1]
DR GeneID; 72754; -.
DR KEGG; mmu:72754; -.
DR UCSC; uc008vmw.2; mouse. [A2AWP8-4]
DR UCSC; uc008vmx.2; mouse. [A2AWP8-3]
DR UCSC; uc008vmy.2; mouse. [A2AWP8-2]
DR UCSC; uc056zye.1; mouse. [A2AWP8-1]
DR CTD; 55160; -.
DR MGI; MGI:1920004; Arhgef10l.
DR VEuPathDB; HostDB:ENSMUSG00000040964; -.
DR eggNOG; KOG3522; Eukaryota.
DR GeneTree; ENSGT00940000153798; -.
DR InParanoid; A2AWP8; -.
DR OMA; HKCDCKM; -.
DR OrthoDB; 67600at2759; -.
DR PhylomeDB; A2AWP8; -.
DR TreeFam; TF331430; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
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 BioGRID-ORCS; 72754; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Arhgef10l; mouse.
DR PRO; PR:A2AWP8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AWP8; protein.
DR Bgee; ENSMUSG00000040964; Expressed in right kidney and 125 other tissues.
DR ExpressionAtlas; A2AWP8; baseline and differential.
DR Genevisible; A2AWP8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0032933; P:SREBP signaling pathway; ISO:MGI.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039919; ARHGEF10/ARHGEF17.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12877; PTHR12877; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1280
FT /note="Rho guanine nucleotide exchange factor 10-like
FT protein"
FT /id="PRO_0000342362"
FT DOMAIN 314..501
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE6"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE6"
FT VAR_SEQ 1..215
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_034427"
FT VAR_SEQ 201..239
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034428"
FT VAR_SEQ 216..276
FT /note="TKRDILALRVGGRDMQELKLKCDCKMTQLMKAAKSGTRDGLEKTRMAVMRKV
FT SFLHRKDVL -> MLPSSSWGKRKPRSQRLGWVRCDARGNMWARQEGLRQPHPHPHALI
FT RCPSSSSSSVSCS (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_034429"
FT VAR_SEQ 399..468
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_034430"
FT VAR_SEQ 576..580
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_034431"
FT CONFLICT 280..281
FT /note="Missing (in Ref. 4; AAH59220)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="M -> V (in Ref. 2; BAC26047)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="V -> I (in Ref. 1; BAC98218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1280 AA; 139987 MW; 4A9C924B4D437252 CRC64;
MASSNPPPQP AIGAPLAPSA PGPSPEVEED SGEAFEFDDS DEEEDTSSGL VVPGLAPERD
TEPSLICFDT VPGSDLDPAA APPQTEAPTV VSNGDAVGAA ISGVRRSSWK RKSSRRIDRF
TFPALEEDVI YDDVPCESPD AHQPGAERGL VYEDVHRAGA PRETEDLGWS SSEFESYSED
SGEETKPEAE PTKHRGSFQP KLSPDLTRLK ERYVRTKRDI LALRVGGRDM QELKLKCDCK
MTQLMKAAKS GTRDGLEKTR MAVMRKVSFL HRKDVLGDSE EEDMGLLEVG VTDIKPPAPE
LGPMPDGLSP QQVVRRHILG SIVQSEGSYV ESLKRILQDY RNPLMEMEPK ALSARKCQVV
FFRVKEILHC HSMFQIALSS RVAEWDSTEK IGDLFVASFS KSMVLDVYSD YVNNFTNAMS
IIKKACLTKP AFLEFLKRRQ VCSTDRVTLY GLMVKPVQRF PQFILLLQDM LKNTPRGHPD
RLSLQLALTE LETLAEKLNE QKRLADQVAE IQQLTKSVSD RSSLNKLLTS GQRQLLLCET
LTETVYGDRG QLIKSKERRV FLLNDMLVCA NINFKPSNHR GQLEISSLVP LGPKYVVKWN
TALPQVQVVE VGQDGGTYDK DNLLIQHAGA KKATAAGQAQ NKVYLGPPRL FQELQDLQKD
LAVVEQITLL ISTLHGTYQN LNMTVAQDWC LALQRLMRVK EEEIHSANKC RLRLLLPGKP
DKSGRPISFM VVFITPNPLS KISWVNRLHL AKIGLREENQ PGWLCPDEDK KSKAPFWCPI
LACCVPAFSS RTLSLQLGGL VHSPVNSPLL GFSAVSTSLP QGYLWVGGGQ EGAGGQVEIF
SLNRPSPRTV KSFPVAAPVL CIEYIPDPEE EAEGAEESRA ATDPSVTVHP TVCLGLQDGS
ILLYGSVDTG TQCLATCKSP GPQPVLCLRH SPFYLLAGLQ DGTLAAYPRT SGDIPWDLES
PPMCITVGPG PIRTLLSLED AAWASCGPRV TVLDAATLQT QQSFEAHQDE AVSVTHMVKA
GSGVWMAFSS GSSIRLFHTE TLEHLQEINI ATRTTFLLPG QKHLCVTSLL ICQGLLWVGT
DQGVIVLLPV PRLEGIPKIT GKGMVSLNGH CGPVAFLAVA MSILAPDILR SDQEEAEGPQ
AEEDKPDGQA HETVPGPDSH TARELTRKKG ILLQYRLRST AHLPGPLLSV REPAPADGSA
LEHSEEDGSI YEMADDPDVW VRSRPCARDA HRKEICSVAI ISGGQGYRHF GGAPGGLSGR
AAPCSETDST LLIWQVPLAL
