ID SGSM3_MOUSE Reviewed; 750 AA. AC Q8VCZ6; Q3TCB6; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 16-JUN-2009, entry version 55. DE RecName: Full=Small G protein signaling modulator 3; DE AltName: Full=RUN and TBC1 domain-containing protein 3; GN Name=Sgsm3; Synonyms=Cip85, Rutbc3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GJA1. RC TISSUE=Embryo; RX PubMed=15709751; DOI=10.1021/bi048306w; RA Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.; RT "Novel rab GAP-like protein, CIP85, interacts with connexin43 and RT induces its degradation."; RL Biochemistry 44:2385-2396(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Dendritic cell; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver, Mammary tumor, and Salivary 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY. RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013; RA Yang H., Sasaki T., Minoshima S., Shimizu N.; RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate RT small G protein (RAP and RAB)-mediated signaling pathway."; RL Genomics 90:249-260(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASS RP SPECTROMETRY. 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 STRUCTURE BY NMR OF 483-549. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of mouse RUN and TBC1 domain RT containing 3."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: May play a cooperative role in NF2-mediated growth CC suppression of cells (By similarity). CC -!- SUBUNIT: Interacts with GJA1. Interaction with GJA1 induces its CC degradation. Interacts via its RUN domain with the C-terminal CC region of NF2. Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A, CC RAP1A, RAP1B, RAP2A, RAP2B and PDCD6I. No interaction with RAB27A CC (By similarity). CC -!- INTERACTION: CC P08050:Gja1 (xeno); NbExp=1; IntAct=EBI-525155, EBI-476947; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the small G protein signaling modulator CC family. CC -!- SIMILARITY: Contains 1 Rab-GAP TBC domain. CC -!- SIMILARITY: Contains 1 RUN domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY382616; AAR89983.1; -; mRNA. DR EMBL; AK170806; BAE42041.1; ALT_INIT; mRNA. DR EMBL; BC018197; AAH18197.1; -; mRNA. DR EMBL; BC024122; AAH24122.1; -; mRNA. DR EMBL; BC025561; AAH25561.1; -; mRNA. DR IPI; IPI00311375; -. DR UniGene; Mm.274943; -. DR PDB; 2YUO; NMR; -; A=483-547. DR PDBsum; 2YUO; -. DR IntAct; Q8VCZ6; 1. DR PhosphoSite; Q8VCZ6; -. DR PRIDE; Q8VCZ6; -. DR Ensembl; ENSMUSG00000042303; Mus musculus. DR KEGG; mmu:105835; -. DR NMPDR; fig|10090.3.peg.30296; -. DR MGI; MGI:1916329; Sgsm3. DR HOVERGEN; Q8VCZ6; -. DR NextBio; 357910; -. DR ArrayExpress; Q8VCZ6; -. DR Bgee; Q8VCZ6; -. DR CleanEx; MM_SGSM3; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005921; C:gap junction; IDA:UniProtKB. DR GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro. DR GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW. DR GO; GO:0045732; P:positive regulation of protein catabolic pr...; IDA:UniProtKB. DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB. DR GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro. DR InterPro; IPR000195; RabGAP_TBC. DR InterPro; IPR004012; Run. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF02759; RUN; 1. DR Pfam; PF00018; SH3_1; 1. DR Pfam; PF00566; TBC; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00593; RUN; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00164; TBC; 1. DR PROSITE; PS50826; RUN; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50086; TBC_RABGAP; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Coiled coil; Cytoplasm; Growth arrest; KW Phosphoprotein; SH3 domain. FT CHAIN 1 750 Small G protein signaling modulator 3. FT /FTId=PRO_0000307811. FT DOMAIN 114 305 Rab-GAP TBC. FT DOMAIN 480 539 SH3. FT DOMAIN 555 718 RUN. FT COILED 415 439 Potential. FT MOD_RES 410 410 Phosphoserine. FT CONFLICT 622 622 D -> G (in Ref. 2; BAE42041). FT STRAND 483 489 FT STRAND 506 511 FT STRAND 514 522 FT STRAND 525 530 FT HELIX 531 533 FT STRAND 534 537 SQ SEQUENCE 750 AA; 85490 MW; C0306BE346808B07 CRC64; MSGNHTPSAS GPFSALTPSI WPQEILAKYS QKEESSEQPE LCYDEFGFRV DKEGSEPGCS QMTGSPLVED PPQRLRWQAH LEFTHNHDVG DLTWDKIAVS LPRSEKLRSL VLAGIPHGMR PQLWMRLSGA LQKKKNSELS YREIIKNSSN DETIAAKQIE KDLLRTMPSN ACFANVNSIG VPRLRRVLRA LAWLYPEIGY CQGTGMVAAC LLLFLEEEDA FWMMCAIIED LLPASYFSTT LLGVQTDQRV LRHLIVQYLP RLDKLLQEHD IELSLITLHW FLTAFASVVH IRLLLRIWDL FFYEGSLVLF QTTLGMLRLK EEELIQSENS ASIFNTLSDI PAQMDDAELL LGEAMRLAGS LTDVAVETQR RKHLAYLIAD QGQTLGTGTT TNLSQVVRRR TQRRKSGITS LLFGEDDLEA LKAKNIKQTE LVADLREAIL RVARHFQCTD PKNCSVELTP DYSMESHQRD HENYVACLRS HRRRAKALLD FERHDDDELG FRKNDIITII SQKDEHCWVG ELNGLRGWFP AKFVEVLDER SKEYSIAGDD SVTEGVTDLV RGTLCPALKA LFEHGLKKPS LLGGACHPWL FIEEAAGREV ERDFDSVYSR LVLCKTYRLD EDGKVLTPEE LLYRAVQSVN VTHDAAHAQM DVKLRSLICV GLNEQVLHLW LEVLCSSLPT VEKWYQPWSF LRSPGWVQIK CELRVLCCFA FSLSQDWELP ARREEEKQPL KEGVQDMLVK HHLFSWDIDG //