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   27-MAR-2024, entry version 156.
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}, Rutbc3
GN   {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}, Mammary tumor
RC   {ECO:0000312|EMBL:AAH25561.1}, and Salivary gland
RC   {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   BioGRID; 222930; 1.
DR   IntAct; Q8VCZ6; 1.
DR   STRING; 10090.ENSMUSP00000122543; -.
DR   iPTMnet; Q8VCZ6; -.
DR   PhosphoSitePlus; Q8VCZ6; -.
DR   MaxQB; Q8VCZ6; -.
DR   PaxDb; 10090-ENSMUSP00000043311; -.
DR   ProteomicsDB; 261015; -.
DR   Pumba; Q8VCZ6; -.
DR   Antibodypedia; 45865; 144 antibodies from 30 providers.
DR   DNASU; 105835; -.
DR   Ensembl; ENSMUST00000139517.9; ENSMUSP00000122543.2; ENSMUSG00000042303.20.
DR   GeneID; 105835; -.
DR   KEGG; mmu:105835; -.
DR   AGR; MGI:1916329; -.
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; QKWYQPW; -.
DR   OrthoDB; 12479at2759; -.
DR   PhylomeDB; Q8VCZ6; -.
DR   BioGRID-ORCS; 105835; 0 hits in 77 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 176 other cell types or tissues.
DR   ExpressionAtlas; Q8VCZ6; baseline and differential.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0048227; P:plasma membrane to endosome transport; 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:0051726; P:regulation of cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0032483; P:regulation of Rab protein signal transduction; ISS:UniProtKB.
DR   CDD; cd17688; RUN_SGSM3; 1.
DR   CDD; cd11813; SH3_SGSM3; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR   InterPro; IPR000195; Rab-GAP-TBC_dom.
DR   InterPro; IPR035969; Rab-GAP_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   PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1.
DR   PANTHER; PTHR47219:SF19; RUN AND TBC1 DOMAIN-CONTAINING PROTEIN 3; 1.
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; RUN domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
DR   Genevisible; Q8VCZ6; MM.
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
//