ARHGG_MOUSE
ID ARHGG_MOUSE Reviewed; 713 AA.
AC Q3U5C8; B1ASH6; Q501M8; Q8VCE8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Rho guanine nucleotide exchange factor 16;
DE AltName: Full=Ephexin-4;
GN Name=Arhgef16;
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=Thymus;
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 GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 [4]
RP IDENTIFICATION.
RX PubMed=15848799; DOI=10.1016/j.neuron.2005.01.030;
RA Sahin M., Greer P.L., Lin M.Z., Poucher H., Eberhart J., Schmidt S.,
RA Wright T.M., Shamah S.M., O'connell S., Cowan C.W., Hu L., Goldberg J.L.,
RA Debant A., Corfas G., Krull C.E., Greenberg M.E.;
RT "Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth cone
RT collapse.";
RL Neuron 46:191-204(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-212; THR-230;
RP SER-231 AND SER-234, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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: Guanyl-nucleotide exchange factor of the RHOG GTPase
CC stimulating the exchange of RHOG-associated GDP for GTP. May play a
CC role in chemotactic cell migration by mediating the activation of RAC1
CC by EPHA2. May also activate CDC42 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ELMO2, EPHA2, RAC1 and RHOG; mediates
CC activation of RAC1 by EPHA2. Interacts with TAX1BP3 (via PDZ domain)
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with TAX1BP3.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32151.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK153708; BAE32151.1; ALT_INIT; mRNA.
DR EMBL; AL627123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137847; AAI37848.1; -; mRNA.
DR EMBL; BC144970; AAI44971.1; -; mRNA.
DR EMBL; BC020030; AAH20030.1; -; mRNA.
DR EMBL; BC095966; AAH95966.1; -; mRNA.
DR CCDS; CCDS51399.1; -.
DR RefSeq; NP_001106215.1; NM_001112744.1.
DR RefSeq; XP_006538892.1; XM_006538829.3.
DR RefSeq; XP_011248544.1; XM_011250242.2.
DR PDB; 7CSO; X-ray; 2.39 A; A/B/C/D=261-713.
DR PDB; 7CSP; X-ray; 3.00 A; A/B=209-713.
DR PDB; 7CSR; X-ray; 3.00 A; A/B/C=261-713.
DR PDBsum; 7CSO; -.
DR PDBsum; 7CSP; -.
DR PDBsum; 7CSR; -.
DR AlphaFoldDB; Q3U5C8; -.
DR SMR; Q3U5C8; -.
DR STRING; 10090.ENSMUSP00000030898; -.
DR iPTMnet; Q3U5C8; -.
DR PhosphoSitePlus; Q3U5C8; -.
DR MaxQB; Q3U5C8; -.
DR PaxDb; Q3U5C8; -.
DR PeptideAtlas; Q3U5C8; -.
DR PRIDE; Q3U5C8; -.
DR ProteomicsDB; 273932; -.
DR Antibodypedia; 1622; 129 antibodies from 26 providers.
DR Ensembl; ENSMUST00000030898; ENSMUSP00000030898; ENSMUSG00000029032.
DR Ensembl; ENSMUST00000169623; ENSMUSP00000126296; ENSMUSG00000029032.
DR GeneID; 230972; -.
DR KEGG; mmu:230972; -.
DR UCSC; uc008wbr.2; mouse.
DR CTD; 27237; -.
DR MGI; MGI:2446219; Arhgef16.
DR VEuPathDB; HostDB:ENSMUSG00000029032; -.
DR eggNOG; KOG3523; Eukaryota.
DR GeneTree; ENSGT01030000234571; -.
DR HOGENOM; CLU_012820_2_1_1; -.
DR InParanoid; Q3U5C8; -.
DR OMA; FHPYVVY; -.
DR OrthoDB; 1176939at2759; -.
DR PhylomeDB; Q3U5C8; -.
DR TreeFam; TF316357; -.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 230972; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q3U5C8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3U5C8; protein.
DR Bgee; ENSMUSG00000029032; Expressed in intestinal villus and 136 other tissues.
DR ExpressionAtlas; Q3U5C8; baseline and differential.
DR Genevisible; Q3U5C8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11938; SH3_ARHGEF16_26; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035797; ARHGEF16/ARHGEF26_SH3.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..713
FT /note="Rho guanine nucleotide exchange factor 16"
FT /id="PRO_0000233691"
FT DOMAIN 288..472
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 505..624
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 633..693
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..485
FT /note="Required for RHOG activation and mediates
FT interaction with EPHA2"
FT /evidence="ECO:0000250"
FT MOTIF 711..713
FT /note="PDZ-binding motif"
FT COMPBIAS 54..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VV41"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VV41"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 538
FT /note="V -> L (in Ref. 1; BAE32151)"
FT /evidence="ECO:0000305"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:7CSP"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7CSP"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 284..313
FT /evidence="ECO:0007829|PDB:7CSO"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 336..356
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 400..411
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 426..443
FT /evidence="ECO:0007829|PDB:7CSO"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 449..488
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:7CSR"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7CSP"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 529..546
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 549..557
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 584..594
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 609..619
FT /evidence="ECO:0007829|PDB:7CSO"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 625..630
FT /evidence="ECO:0007829|PDB:7CSP"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:7CSO"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:7CSO"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:7CSO"
FT HELIX 694..707
FT /evidence="ECO:0007829|PDB:7CSO"
SQ SEQUENCE 713 AA; 80381 MW; 823AC537814C80F7 CRC64;
MSQRHSDSSL DEKLLEYRFH AELRLDANGN PIPGLPMVRS SLKARANAAF EPDASEPLPP
PPSPEDEEPP RPIVLSTQSP AALKMGTQQL IPKSLAVASK AKTKSPARHQ SFGAAVLSKE
AARRNPQLFS APSFSLDDMD MDMVTTGNLR RNLRNQSYRA AMKGPGPPSS KGDSVQLGPK
LQALAEEAAQ PPSRYPAKNK KTLGRKRAHK GSFKDDPQLY QEIRERGLNT SHESDDDILD
EPSGPVGTQR ADTTIVVKSY RPAQLTWSQL PEVLESGVLD TLSTEERKRQ EAIFEILTSE
FSYLHSLSIL VTEFLQSREL RATMTQTEHH HLFSNILDVM SASQKFFEAL EQRHKAQVCV
EDISDILEDH AQHHFHPYIA YCSNEVYQQR TLQKLSNSNA AFRDVLKEIE KRPACGGLPM
ISFLILPMQR VTRLPLLTDT LCLKTQGHPE RYKAASQALK AISKLVKQCN EGAHKMERTE
QIYTLNMQLD FGKVKSLPLI SASRWLLKRG ELFLLEESSI FRKIASRPTC YLFLFNDVLV
VTKKKSEESY LVQDYAQLDH VQVRKLEPSE PLLPGGSSRS SSVPYPFQVN LLHNSEGRQE
QILLSSDSAS DRARWITALT YKERQWQGIT NKGELPQVEV TKAYFAKQAD EITLQQADIV
LVLQEEDGWL HGERLRDGET GWFPESFAHS ITSRVAVEGN VRRMERLRVE TDV
