SGSM1_MOUSE
ID SGSM1_MOUSE Reviewed; 1093 AA.
AC Q8BPQ7; Q3TJ12;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Small G protein signaling modulator 1;
DE AltName: Full=RUN and TBC1 domain-containing protein 2;
GN Name=Sgsm1; Synonyms=Rutbc2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Placenta;
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 SUBCELLULAR LOCATION, AND 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 254-425 IN COMPLEX WITH RAB9A,
RP INTERACTION WITH RAB9A AND RAB9B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LEU-256; LYS-260; ASN-261; ASN-262; TYR-277; ASN-294 AND MET-297.
RX PubMed=25220469; DOI=10.1016/j.str.2014.08.005;
RA Zhang Z., Wang S., Shen T., Chen J., Ding J.;
RT "Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular
RT basis for the binding specificity of Rab9A with RUTBC2.";
RL Structure 22:1408-1420(2014).
CC -!- FUNCTION: Interacts with numerous Rab family members, functioning as
CC Rab effector for some, and as GTPase activator for others. Promotes GTP
CC hydrolysis by RAB34 and RAB36. Probably functions as GTPase effector
CC with RAB9A and RAB9B; does not stimulate GTP hydrolysis with RAB9A and
CC RAB9B. {ECO:0000250|UniProtKB:Q2NKQ1}.
CC -!- SUBUNIT: Interacts with RAB9A (GTP-bound form) and RAB9B
CC (PubMed:25220469). Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A,
CC RAP1A, RAP1B, RAP2A and RAP2B. No interaction with RAB27A (By
CC similarity). {ECO:0000250|UniProtKB:Q2NKQ1,
CC ECO:0000269|PubMed:25220469}.
CC -!- INTERACTION:
CC Q8BPQ7-1; Q9R0M6: Rab9a; NbExp=8; IntAct=EBI-16121756, EBI-6552247;
CC Q8BPQ7-1; Q8BHH2: Rab9b; NbExp=3; IntAct=EBI-16121756, EBI-11568845;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:17509819}. Cytoplasm {ECO:0000269|PubMed:25220469}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25220469}; Peripheral
CC membrane protein {ECO:0000269|PubMed:25220469}. Note=Recruited to
CC cytoplasmic vesicle membranes via its interaction with Rab family
CC members, such as RAB9A. {ECO:0000269|PubMed:25220469}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BPQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPQ7-2; Sequence=VSP_024669, VSP_024670;
CC -!- TISSUE SPECIFICITY: Expressed only in brain.
CC {ECO:0000269|PubMed:17509819}.
CC -!- SIMILARITY: Belongs to the RUTBC family. {ECO:0000305}.
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DR EMBL; AK053555; BAC35428.1; -; mRNA.
DR EMBL; AK167632; BAE39683.1; -; mRNA.
DR CCDS; CCDS39218.1; -. [Q8BPQ7-1]
DR CCDS; CCDS84935.1; -. [Q8BPQ7-2]
DR RefSeq; NP_001156437.1; NM_001162965.1.
DR RefSeq; NP_001296457.1; NM_001309528.1. [Q8BPQ7-2]
DR RefSeq; NP_766306.2; NM_172718.3.
DR PDB; 4QXA; X-ray; 2.30 A; B=254-425.
DR PDBsum; 4QXA; -.
DR AlphaFoldDB; Q8BPQ7; -.
DR SMR; Q8BPQ7; -.
DR BioGRID; 206853; 2.
DR DIP; DIP-61070N; -.
DR IntAct; Q8BPQ7; 2.
DR STRING; 10090.ENSMUSP00000046544; -.
DR iPTMnet; Q8BPQ7; -.
DR PhosphoSitePlus; Q8BPQ7; -.
DR MaxQB; Q8BPQ7; -.
DR PaxDb; Q8BPQ7; -.
DR PeptideAtlas; Q8BPQ7; -.
DR PRIDE; Q8BPQ7; -.
DR ProteomicsDB; 256989; -. [Q8BPQ7-1]
DR ProteomicsDB; 256990; -. [Q8BPQ7-2]
DR Antibodypedia; 308; 92 antibodies from 28 providers.
DR DNASU; 52850; -.
DR Ensembl; ENSMUST00000057209; ENSMUSP00000084106; ENSMUSG00000042216. [Q8BPQ7-2]
DR GeneID; 52850; -.
DR KEGG; mmu:52850; -.
DR UCSC; uc008yuc.2; mouse. [Q8BPQ7-2]
DR CTD; 129049; -.
DR MGI; MGI:107320; Sgsm1.
DR VEuPathDB; HostDB:ENSMUSG00000042216; -.
DR eggNOG; KOG1648; Eukaryota.
DR GeneTree; ENSGT00940000156871; -.
DR HOGENOM; CLU_006235_0_1_1; -.
DR InParanoid; Q8BPQ7; -.
DR OrthoDB; 171826at2759; -.
DR PhylomeDB; Q8BPQ7; -.
DR BioGRID-ORCS; 52850; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sgsm1; mouse.
DR PRO; PR:Q8BPQ7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BPQ7; protein.
DR Bgee; ENSMUSG00000042216; Expressed in superior cervical ganglion and 149 other tissues.
DR ExpressionAtlas; Q8BPQ7; baseline and differential.
DR Genevisible; Q8BPQ7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR CDD; cd15784; PH_RUTBC; 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; IPR037745; SGSM1/2.
DR InterPro; IPR021935; SGSM1/2_RBD.
DR Pfam; PF12068; PH_RBD; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; GTPase activation; Membrane; Reference proteome.
FT CHAIN 1..1093
FT /note="Small G protein signaling modulator 1"
FT /id="PRO_0000284834"
FT DOMAIN 36..190
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 562..1026
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 256..297
FT /note="Important for interaction with RAB9A and RAB9B"
FT /evidence="ECO:0000269|PubMed:25220469"
FT REGION 301..350
FT /note="Required for interaction with RAP family members"
FT /evidence="ECO:0000250"
FT REGION 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024669"
FT VAR_SEQ 288..308
FT /note="TLKWTPNQLMNGSVGDLDYEK -> MLGQVGLGDLWLPTVSLTSPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024670"
FT MUTAGEN 256
FT /note="L->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 260
FT /note="K->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 261
FT /note="N->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 262
FT /note="N->A: Mildly impaired interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 277
FT /note="Y->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 294
FT /note="N->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT MUTAGEN 297
FT /note="M->A: Abolishes interaction with RAB9A."
FT /evidence="ECO:0000269|PubMed:25220469"
FT CONFLICT 321
FT /note="E -> V (in Ref. 1; BAE39683)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="P -> T (in Ref. 1; BAC35428)"
FT /evidence="ECO:0000305"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4QXA"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4QXA"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:4QXA"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4QXA"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:4QXA"
SQ SEQUENCE 1093 AA; 123196 MW; 947E0CDB3220A6FA CRC64;
MASVPAEAET RQRLLRTVKK EVKQIMEEAV TRKFVHEDSS HIISFCAAVE ACVLHGLRRR
AAGFLRSNKI AALFMKVGKG FPPAEELSRK VQELEQLIES ARNQIQGLQE NVRKLPKLPN
LSPLAIKHLW IRTALFGRVL DKIVHYLVEN SSKYYEKEAL LMDPVDGPIL ASLLVGPCAL
EYTKMKTADH FWTDPSADEL VQRHRIHSSH LRQDSPTKRP ALCIQKRHSS GSMDDRPSIS
ARDYVESLHQ DSRATLLYGK NNVLVQPRDD MEAVPGYLSL HQTADVMTLK WTPNQLMNGS
VGDLDYEKSV YWDYAVTIRL EEIVYLHCHQ QVDSGGTVVL VSQDGIQRPP FRFPKGGHLL
QFLSCLENGL LPHGQLDPPL WSQRGKGKVF PKLRKRSPQG SSESTSSDKE DDEATDYVFR
IIYPGTQSEF VPQDLMDVSM NNLPPLWQPS PRKSSCSSCS QSGSADGGST NGCNHERAPL
KLLCDNMKYQ ILSRAFYGWL AYCRHLSTVR THLSALVNHM IVSPDLPCDA GQGLTASIWE
KYIQDSTTYP EQELLRLIYY GGVQPEIRRA VWPFLLGHYQ FGMTEMERKE VDEQIHACYA
QTMSEWLGCE AIVRQRERES HAAALAKCSS GASLDSHLHR MLHRDSTISN ESSQSCSSGR
QNLRLQSDSS SSTQVFESVD EVEQTEAEGR SEEKHPKIPN GNPANGTCSP DSGHPSSHNF
SSGLSEHSEP SLSTEDSVLD AQRSLPAVFR PGDSSVEDGQ SSEATTSRDE APREELAVQD
SLESDLLANE SLEEFMSIPG SLDVALPEKD GAVMDGWPGE ADKPSRADSE DNLSEEPEME
SLFPALASLA VTSSANNEAS PVSSSGVTYS PELLDLYTVN LHRIEKDVQR CDRSYWYFTA
ANLEKLRNIM CSYIWQHIEI GYVQGMCDLL APLLVILDDE ALAFSCFTEL MKRMNQNFPH
GGAMDTHFAN MRSLIQILDS ELFELMHQNG DYTHFYFCYR WFLLDFKREL VYDDVFSVWE
TIWAAKHVSS AHYVLFIALA LVEVYRDIIL ENNMDFTDII KFFNEMAERH NAKQILQLAR
DLVHKVQILI ENK
