GenomeNet

Database: UniProt
Entry: D3ZAS2_RAT
LinkDB: D3ZAS2_RAT
Original site: D3ZAS2_RAT 
ID   D3ZAS2_RAT              Unreviewed;      1096 AA.
AC   D3ZAS2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Small G protein signaling modulator 1 {ECO:0000313|Ensembl:ENSRNOP00000000898.7};
GN   Name=Sgsm1 {ECO:0000313|Ensembl:ENSRNOP00000000898.7,
GN   ECO:0000313|RGD:1308178};
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 {ECO:0000313|Ensembl:ENSRNOP00000000898.7, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000000898.7, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000898.7,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000000898.7}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000898.7};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the RUTBC family.
CC       {ECO:0000256|ARBA:ARBA00034124}.
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DR   RefSeq; XP_017453793.1; XM_017598304.1.
DR   AlphaFoldDB; D3ZAS2; -.
DR   STRING; 10116.ENSRNOP00000000898; -.
DR   iPTMnet; D3ZAS2; -.
DR   PhosphoSitePlus; D3ZAS2; -.
DR   PaxDb; 10116-ENSRNOP00000000898; -.
DR   Ensembl; ENSRNOT00000000898.8; ENSRNOP00000000898.7; ENSRNOG00000000708.8.
DR   GeneID; 288743; -.
DR   AGR; RGD:1308178; -.
DR   CTD; 129049; -.
DR   RGD; 1308178; Sgsm1.
DR   VEuPathDB; HostDB:ENSRNOG00000000708; -.
DR   eggNOG; KOG1648; Eukaryota.
DR   GeneTree; ENSGT00940000156871; -.
DR   HOGENOM; CLU_006235_0_0_1; -.
DR   InParanoid; D3ZAS2; -.
DR   OrthoDB; 164430at2759; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000000708; Expressed in frontal cortex and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   CDD; cd15784; PH_RUTBC; 1.
DR   CDD; cd17703; RUN_SGSM1; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 2.30.29.230; -; 1.
DR   Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like 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; IPR047344; RUN_SGSM1.
DR   InterPro; IPR037745; SGSM1/2.
DR   InterPro; IPR021935; SGSM1/2_RBD.
DR   PANTHER; PTHR22957:SF187; SMALL G PROTEIN SIGNALING MODULATOR 1; 1.
DR   PANTHER; PTHR22957; TBC1 DOMAIN FAMILY MEMBER GTPASE-ACTIVATING PROTEIN; 1.
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; RUN domain-like; 1.
DR   SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          36..190
FT                   /note="RUN"
FT                   /evidence="ECO:0000259|PROSITE:PS50826"
FT   DOMAIN          565..1029
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000259|PROSITE:PS50086"
FT   REGION          380..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          84..118
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        650..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..700
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..835
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  123829 MW;  23CAFEF9B696923D CRC64;
     MASVPAEAET RQRLLRTVKK EVKQIMEEAV TRKFVHEDSS HIISFCAAVE ACVLHGLRRR
     AAGFLRSNKI AALFMKVGKG FPPAEELSRK VQELEQLIES ARNQIQGLQE NVRKLPKLPN
     LSPLAIKHLW IRTALFERVL DKIVHYLVEN SSKYYEKEAL LMDPVDGPIL ASLLVGPCAL
     EYTKMKTADH FWTDPSADEL VQRHRIHSSH LRQDSPTKRP ALCVRWIQKR HSSGSMDDRP
     SISARDYVES LHQNSRATLL YGKNNVLVQP RDDMEAVPGY LSLHQTADVM TLKWTPNQLM
     NGSVGDLDYE KSVYWDYAVT IRLEEIVYLH CHQQVDSGGT VVLVSQDGIQ RPPFRFPKGG
     HLLQFLSCLE NGLLPHGQLD PPLWSQRGKG KVFPKLRKRS PQGSSESTSS DKEDDEATDY
     VFRIIYPGTQ SEFVPQDLMD VSMNNLPSLW QPSPRKSSCS SCSQSGSADG SSTNGCNHER
     APLKLLCDNM KYQILSRAFY GWLAYCRHLS TVRTHLSALV NHMIVSPDLP CDAGQGLTAS
     IWEQYIQDST TYPEQELLRL IYYGGVQPEI RRAVWPFLLG HYQFGMTEME RKEVDEQIHA
     CYAQTMSEWL GCEAIVRQRE RESHAAALAK CSSGASLDSH LHRMLHRDST ISNESSQSCS
     SGRQNLRLQS DSSSSTQVFE SVDEVEQTEA EGRSEEKHPK IPNGNPANGT CSPDSGHPSS
     HNFSSGLSEH SEPSLSTEDS VLDVQRSLPA VFRPGDSSVE DGQSSEATTS RDEAPREELA
     VQDSLESDLL ANESLEEFMS IPGSLDVALP EKDGAMMDGW PGEADKHGRA DSEDNLSEEP
     EMESLFPALA SLAVTSSANN ETSPVSSSGV TYSPELLDLY TVNLHRIEKD VQRCDRSYWY
     FTAANLEKLR NIMCSYIWQH IEIGYVQGMC DLLAPLLVIL DDEALAFSCF TELMKRMNQN
     FPHGGAMDTH FANMRSLIQI LDSELFELMH QNGDYTHFYF CYRWFLLDFK RELVYDDVFS
     VWETIWAAKH VSSAHYVLFI ALALVEVYRD IILENNMDFT DIIKFFNEMA ERHNAKQILQ
     LARDLVHKVQ ILIENK
//
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