SGSM2_MOUSE
ID SGSM2_MOUSE Reviewed; 1005 AA.
AC Q80U12; Q5SWE0; Q5SWE1; Q6PAP8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Small G protein signaling modulator 2;
DE AltName: Full=RUN and TBC1 domain-containing protein 1;
GN Name=Sgsm2; Synonyms=Kiaa0397, Rutbc1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-444 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP 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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26620560; DOI=10.1074/jbc.m115.684043;
RA Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
RT "RUTBC1 functions as a GTPase-activating protein for Rab32/38 and regulates
RT melanogenic enzyme trafficking in melanocytes.";
RL J. Biol. Chem. 291:1427-1440(2016).
CC -!- FUNCTION: Possesses GTPase activator activity towards RAB32, RAB33B and
CC RAB38. Regulates the trafficking of melanogenic enzymes TYR, TYRP1 and
CC DCT/TYRP2 to melanosomes in melanocytes by inactivating RAB32 and
CC RAB38. Inhibits RAB32 and RAB38 activation both directly by promoting
CC their GTPase activity and indirectly by disrupting the RAB9A-HPS4
CC interaction which is required for RAB32/38 activation
CC (PubMed:26620560). {ECO:0000269|PubMed:26620560}.
CC -!- SUBUNIT: Interacts with RAB4A, RAB11A, RAP1A, RAP1B, RAP2A and RAP2B.
CC No interaction with RAB27A. Interacts with RAB9A (By similarity).
CC {ECO:0000250|UniProtKB:O43147}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43147}.
CC Melanosome {ECO:0000269|PubMed:26620560}. Note=Melanosomal localization
CC is mediated by RAB9A. {ECO:0000250|UniProtKB:O43147}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80U12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U12-2; Sequence=VSP_024599;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17509819}.
CC -!- DOMAIN: The Rab-GAP TBC domain possesses GTPase activator activity.
CC {ECO:0000250|UniProtKB:O43147}.
CC -!- SIMILARITY: Belongs to the RUTBC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58414.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH60163.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122273; BAC65555.1; ALT_INIT; mRNA.
DR EMBL; AL604066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058414; AAH58414.1; ALT_FRAME; mRNA.
DR EMBL; BC060163; AAH60163.1; ALT_FRAME; mRNA.
DR CCDS; CCDS36224.1; -. [Q80U12-1]
DR CCDS; CCDS88189.1; -. [Q80U12-2]
DR RefSeq; NP_922934.2; NM_197943.2. [Q80U12-1]
DR RefSeq; XP_006534644.1; XM_006534581.3.
DR AlphaFoldDB; Q80U12; -.
DR SMR; Q80U12; -.
DR BioGRID; 220852; 3.
DR DIP; DIP-61071N; -.
DR IntAct; Q80U12; 2.
DR STRING; 10090.ENSMUSP00000050496; -.
DR iPTMnet; Q80U12; -.
DR PhosphoSitePlus; Q80U12; -.
DR MaxQB; Q80U12; -.
DR PaxDb; Q80U12; -.
DR PeptideAtlas; Q80U12; -.
DR PRIDE; Q80U12; -.
DR ProteomicsDB; 256991; -. [Q80U12-1]
DR ProteomicsDB; 256992; -. [Q80U12-2]
DR Antibodypedia; 10736; 82 antibodies from 22 providers.
DR DNASU; 97761; -.
DR Ensembl; ENSMUST00000057631; ENSMUSP00000050496; ENSMUSG00000038351. [Q80U12-1]
DR Ensembl; ENSMUST00000081799; ENSMUSP00000080489; ENSMUSG00000038351. [Q80U12-2]
DR GeneID; 97761; -.
DR KEGG; mmu:97761; -.
DR UCSC; uc007kck.1; mouse. [Q80U12-1]
DR CTD; 9905; -.
DR MGI; MGI:2144695; Sgsm2.
DR VEuPathDB; HostDB:ENSMUSG00000038351; -.
DR eggNOG; KOG1648; Eukaryota.
DR GeneTree; ENSGT00940000159315; -.
DR HOGENOM; CLU_006235_0_0_1; -.
DR InParanoid; Q80U12; -.
DR OMA; CHRSHCH; -.
DR OrthoDB; 171826at2759; -.
DR PhylomeDB; Q80U12; -.
DR TreeFam; TF318216; -.
DR BioGRID-ORCS; 97761; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Sgsm2; mouse.
DR PRO; PR:Q80U12; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80U12; protein.
DR Bgee; ENSMUSG00000038351; Expressed in dentate gyrus of hippocampal formation granule cell and 172 other tissues.
DR Genevisible; Q80U12; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0034499; P:late endosome to Golgi transport; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO: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 Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1005
FT /note="Small G protein signaling modulator 2"
FT /id="PRO_0000284663"
FT DOMAIN 34..191
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 566..938
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 95..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 430
FT /note="N -> ITINYHHLAASRAASVDDDEEEEDKLHAMLSMICSRNLTAPNPMKD
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024599"
FT MOD_RES Q80U12-2:444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1005 AA; 113076 MW; 5902EC20348D031F CRC64;
MGSAEDAVKE KLLWNVKKEV KQIMEEAVTR KFVHEDSSHI IALCGAVEAC LLHQLRRRAA
GFLRSDKMAA LFTKVGKTCP VAEDICHKVQ ELQQQAEGRK PSGGSQEALR KQGSTGGKAP
ALSPQALKHI WVRTALMEKV LDRVVQYLAE NCSKYYEKEA LLADPVFGPI LACLLVGPCA
LEYTKLKTAD HYWTDPSADE LVQRHRIRGP PNRQDSPAKR PALGIRKRHS SGSASEDRLA
ACAREYVESL HQNSRTRLLY GKNNVLVQPK EDMEAVPGYL SLHQSAENLT LKWTPNQLMN
GTLGDSELEK SVYWDYALVV PFSQIVCIHC HQQKSGGTLV LVSQDGIQRP PLHFPQGGHL
LSFLSCLENG LLPRGQLEPP LWTQQGKGKV FPKLRKRSSI RSIDVEELGV GRATDYVFRI
IYPGHRHEHN AGDMIEMQGF GPSLTAWHLE PLCSQGSSCL SCSSSSSPYA TPSHCSCIPD
RLPLRLLCES MKRQIVSRAF YGWLAYCRHL STVRTHLSAL VHHNIIPPDR PPGASGGLTK
DVWSKYQKDE KNYKELELLR QVYYGGVEHE IRKDVWPFLL GHYKFGMSKK EMEQVDTAVA
ARYQQVLAEW KACEVVVRQR EREAHPATLT KFSSGSSIDS HVQRLVHRDS TISNDVFISV
DDLEPSGPQD LEDSKPKREQ EPGAGTPGIA AAEQQSVEFD SPDSGLPSSR NYSVASGIQS
SLDEAQSVGF EDDGAGEDGS EGPATAAHTF PGPHDPGQET LAPASELEAG QELAAVCAAA
YTIELLDTVA LNLHRIDKDV QRCDRNYWYF TTSNLERLRD IMCSYVWEHL DMGYVQGMCD
LLAPLLVILD NDQLAYSCFS HLMKRMGQNF PSGGAMDSHF ANMRSLIQIL DSELFELMHQ
NGDYTHFYFC YRWFLLDFKR ELLYEDVFAV WEVIWAARRI SSEHFVLFIA LALVEAYREI
IRDNNMDFTD IIKFFNERAE RHDAQEILRI ARDLVHKVQM LIDNK
