SGSM3_RAT
ID SGSM3_RAT Reviewed; 749 AA.
AC Q6P6R7; Q76KK4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Small G protein signaling modulator 3;
DE AltName: Full=BDIF-1;
DE AltName: Full=RUN and TBC1 domain-containing protein 3;
GN Name=Sgsm3 {ECO:0000250|UniProtKB:Q96HU1};
GN Synonyms=Bdif1, Rutbc3 {ECO:0000312|EMBL:AAH62060.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH GJA1.
RC TISSUE=Astrocyte;
RX PubMed=21453730; DOI=10.1016/j.neures.2011.03.008;
RA Ito T., Ueki T., Furukawa H., Sato K.;
RT "The identification of novel protein, brain-derived integrating factor-1
RT (BDIF1), which interacts with astrocytic gap junctional protein.";
RL Neurosci. Res. 70:330-333(2011).
RN [2] {ECO:0000312|EMBL:AAH62060.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH62060.1};
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a cooperative role in NF2-mediated growth
CC suppression of cells. May act as a modulator of small G protein
CC RAB- and RAP-mediated neuronal signal transduction and vesicular
CC transportation pathways (By similarity).
CC {ECO:0000250|UniProtKB:Q96HU1}.
CC -!- SUBUNIT: Interacts with GJA1. Interaction with GJA1 induces its
CC degradation. Interacts (via RUN domain) with NF2 (via C-terminus).
CC Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A, RAP1A, RAP1B, RAP2A,
CC RAP2B and PDCD6I. No interaction with RAB27A. No interaction with GJB1
CC or GJD2. {ECO:0000269|PubMed:21453730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VCZ6}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, kidney and testis.
CC Moderately expressed in heart, very weakly in lung and muscle. Not
CC expressed in spleen. {ECO:0000269|PubMed:21453730}.
CC -!- SIMILARITY: Belongs to the small G protein signaling modulator family.
CC {ECO:0000305}.
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DR EMBL; AB091009; BAC82539.2; -; mRNA.
DR EMBL; BC062060; AAH62060.1; -; mRNA.
DR RefSeq; NP_942082.2; NM_198787.2.
DR AlphaFoldDB; Q6P6R7; -.
DR BMRB; Q6P6R7; -.
DR SMR; Q6P6R7; -.
DR STRING; 10116.ENSRNOP00000025381; -.
DR iPTMnet; Q6P6R7; -.
DR PhosphoSitePlus; Q6P6R7; -.
DR jPOST; Q6P6R7; -.
DR PaxDb; Q6P6R7; -.
DR GeneID; 362963; -.
DR KEGG; rno:362963; -.
DR UCSC; RGD:735113; rat.
DR CTD; 27352; -.
DR RGD; 735113; Sgsm3.
DR eggNOG; KOG2222; Eukaryota.
DR InParanoid; Q6P6R7; -.
DR PhylomeDB; Q6P6R7; -.
DR PRO; PR:Q6P6R7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005921; C:gap junction; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
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:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
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 Cell cycle; Coiled coil; Cytoplasm; Growth arrest; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..749
FT /note="Small G protein signaling modulator 3"
FT /id="PRO_0000307812"
FT DOMAIN 113..304
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 479..538
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 554..717
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT COILED 414..438
FT /evidence="ECO:0000255"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 20
FT /note="I -> V (in Ref. 1; BAC82539)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> V (in Ref. 1; BAC82539)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="Q -> R (in Ref. 1; BAC82539)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="D -> G (in Ref. 1; BAC82539)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="N -> D (in Ref. 1; BAC82539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 85188 MW; D72A3C27CDA88466 CRC64;
MSGNHTPSAS GPFSALTPSI WPQEILAKSS QKEDSSEPEI CYDEFGFRVD KEGSEPGCSQ
MAGTPLVEDP PQRLRWQAHL EFTHNHDVGD LTWDKIAVSL PRSEKLRSLV LAGIPHGMRP
QLWMRLSGAL QKKKNSELSY REIVKNSSND ETIAAKQIEK DLLRTMPSNA CFANVNSIGV
PRLRRVLRAL AWLYPEIGYC QGTGMVAACL LLFLEEEDAF WMMCAIIEDL LPASYFSTTL
LGVQTDQRVL RHLIVQYLPR LDKLLQEHDI ELSLITLHWF LTAFASVVHI RLLLRIWDLF
FYEGSLVLFQ TTLGMLRLKE EELIQSENSA SIFNTLSDIP AQMDDAELLL GEAMQLAGSL
TDVAVETQRR KHLAYLIADQ GQTLGTSTTT SLSQVVRRRT QRRKSGITSL LFGEDDLEAL
KAKNIKQTEL VADLREAILR VARHFQCTDP KNCSVELTPD YSMESHQRDH ENYVACLRSH
RRRAKALLDF ERHDDDELGF RKNDIITIIS QKDEHCWVGE LNGLRGWFPA KFVEVLDERS
KEYSIAGDDS VTEGVTDLVR GTLCPALKAL FEHGLKKPSL LGGACHPWLF IEEAAGREVE
RDFDSVYSRL VLCKTYRLDE DGKVLTPEEL LYRAVQSVNV THDAAHAQMD VKLRSLICVG
LNEQVLHLWL EVLCSSLPTV EKWYQPWSFL RSPGWVQIKC ELRVLCCFAF SLSQDWELPA
KREEEKQPLK EGVQDMLVKH HLFSWDIDG
