SGSM3_MOUSE
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 03-AUG-2022, entry version 147.
DE RecName: Full=Small G protein signaling modulator 3;
DE AltName: Full=RUN and TBC1 domain-containing protein 3;
GN Name=Sgsm3 {ECO:0000250|UniProtKB:Q96HU1};
GN Synonyms=Cip85 {ECO:0000312|EMBL:AAR89983.1},
GN Rutbc3 {ECO:0000312|EMBL:AAH18197.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAR89983.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GJA1.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR89983.1};
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 induces
RT its degradation.";
RL Biochemistry 44:2385-2396(2005).
RN [2] {ECO:0000312|EMBL:BAE42041.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD {ECO:0000312|EMBL:BAE42041.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE42041.1};
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] {ECO:0000312|EMBL:AAH18197.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH18197.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH24122.1},
RC Mammary tumor {ECO:0000312|EMBL:AAH25561.1}, and
RC Salivary gland {ECO:0000312|EMBL:AAH18197.1};
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] {ECO:0000305}
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 small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
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-406, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [7]
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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GJA1. Interaction with GJA1 induces its
CC degradation. Interacts via its RUN domain with the C-terminal region of
CC NF2. Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A, RAP1A, RAP1B,
CC RAP2A, RAP2B and PDCD6I. No interaction with RAB27A (By similarity).
CC {ECO:0000250|UniProtKB:Q96HU1, ECO:0000269|PubMed:15709751}.
CC -!- INTERACTION:
CC Q8VCZ6; P08050: Gja1; Xeno; NbExp=4; IntAct=EBI-525155, EBI-476947;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96HU1}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}.
CC -!- SIMILARITY: Belongs to the small G protein signaling modulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE42041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 CCDS; CCDS49673.2; -.
DR RefSeq; NP_598852.3; NM_134091.2.
DR PDB; 2YUO; NMR; -; A=483-547.
DR PDBsum; 2YUO; -.
DR AlphaFoldDB; Q8VCZ6; -.
DR BMRB; Q8VCZ6; -.
DR SMR; Q8VCZ6; -.
DR IntAct; Q8VCZ6; 1.
DR STRING; 10090.ENSMUSP00000043311; -.
DR iPTMnet; Q8VCZ6; -.
DR PhosphoSitePlus; Q8VCZ6; -.
DR MaxQB; Q8VCZ6; -.
DR PaxDb; Q8VCZ6; -.
DR PRIDE; Q8VCZ6; -.
DR ProteomicsDB; 261015; -.
DR Antibodypedia; 45865; 126 antibodies from 30 providers.
DR DNASU; 105835; -.
DR Ensembl; ENSMUST00000139517; ENSMUSP00000122543; ENSMUSG00000042303.
DR GeneID; 105835; -.
DR KEGG; mmu:105835; -.
DR CTD; 27352; -.
DR MGI; MGI:1916329; Sgsm3.
DR VEuPathDB; HostDB:ENSMUSG00000042303; -.
DR eggNOG; KOG2222; Eukaryota.
DR GeneTree; ENSGT00940000157282; -.
DR HOGENOM; CLU_020721_0_0_1; -.
DR InParanoid; Q8VCZ6; -.
DR OMA; NSPGWVQ; -.
DR OrthoDB; 1162786at2759; -.
DR PhylomeDB; Q8VCZ6; -.
DR BioGRID-ORCS; 105835; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Sgsm3; mouse.
DR EvolutionaryTrace; Q8VCZ6; -.
DR PRO; PR:Q8VCZ6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VCZ6; protein.
DR Bgee; ENSMUSG00000042303; Expressed in spermatid and 173 other tissues.
DR ExpressionAtlas; Q8VCZ6; baseline and differential.
DR Genevisible; Q8VCZ6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; NAS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; ISS:UniProtKB.
DR CDD; cd11813; SH3_SGSM3; 1.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR035833; SGSM3_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF50044; SSF50044; 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; Reference proteome; SH3 domain.
FT CHAIN 1..750
FT /note="Small G protein signaling modulator 3"
FT /id="PRO_0000307811"
FT DOMAIN 114..305
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 480..539
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 555..718
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT COILED 415..439
FT /evidence="ECO:0000255"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 622
FT /note="D -> G (in Ref. 2; BAE42041)"
FT /evidence="ECO:0000305"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:2YUO"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:2YUO"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:2YUO"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:2YUO"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:2YUO"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:2YUO"
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
