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REM2_MOUSE
ID   REM2_MOUSE              Reviewed;         341 AA.
AC   Q8VEL9; Q8BPB1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=GTP-binding protein REM 2;
DE   AltName: Full=Rad and Gem-like GTP-binding protein 2;
GN   Name=Rem2;
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=Pituitary, and Spinal cord;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Binds GTP saturably and exhibits a low intrinsic rate of GTP
CC       hydrolysis. {ECO:0000250|UniProtKB:Q9WTY2}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WTY2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VEL9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VEL9-2; Sequence=VSP_038749;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC36746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK077317; BAC36746.1; ALT_INIT; mRNA.
DR   EMBL; AK090165; BAC41120.1; -; mRNA.
DR   EMBL; BC018219; AAH18219.1; ALT_INIT; mRNA.
DR   CCDS; CCDS27090.2; -. [Q8VEL9-1]
DR   RefSeq; NP_542764.2; NM_080726.3.
DR   PDB; 3Q85; X-ray; 1.76 A; A/B=114-282.
DR   PDBsum; 3Q85; -.
DR   AlphaFoldDB; Q8VEL9; -.
DR   SMR; Q8VEL9; -.
DR   IntAct; Q8VEL9; 1.
DR   MINT; Q8VEL9; -.
DR   STRING; 10090.ENSMUSP00000127199; -.
DR   iPTMnet; Q8VEL9; -.
DR   PhosphoSitePlus; Q8VEL9; -.
DR   MaxQB; Q8VEL9; -.
DR   PaxDb; Q8VEL9; -.
DR   PRIDE; Q8VEL9; -.
DR   ProteomicsDB; 253218; -. [Q8VEL9-1]
DR   ProteomicsDB; 253219; -. [Q8VEL9-2]
DR   ABCD; Q8VEL9; 1 sequenced antibody.
DR   DNASU; 140743; -.
DR   GeneID; 140743; -.
DR   KEGG; mmu:140743; -.
DR   CTD; 161253; -.
DR   MGI; MGI:2155260; Rem2.
DR   eggNOG; KOG0395; Eukaryota.
DR   InParanoid; Q8VEL9; -.
DR   OrthoDB; 679855at2759; -.
DR   PhylomeDB; Q8VEL9; -.
DR   BioGRID-ORCS; 140743; 0 hits in 72 CRISPR screens.
DR   EvolutionaryTrace; Q8VEL9; -.
DR   PRO; PR:Q8VEL9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8VEL9; protein.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; ISO:MGI.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   DisProt; DP02573; -.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; GTP-binding; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..341
FT                   /note="GTP-binding protein REM 2"
FT                   /id="PRO_0000122484"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT   BINDING         230..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT   BINDING         261..262
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTY2"
FT   MOD_RES         296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTY2"
FT   VAR_SEQ         1..69
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_038749"
FT   CONFLICT        13..15
FT                   /note="TET -> IEI (in Ref. 2; AAH18219)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203
FT                   /note="G -> S (in Ref. 2; AAH18219)"
FT                   /evidence="ECO:0000305"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           184..188
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   STRAND          190..197
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           201..205
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           207..217
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           242..251
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   TURN            261..264
FT                   /evidence="ECO:0007829|PDB:3Q85"
FT   HELIX           267..280
FT                   /evidence="ECO:0007829|PDB:3Q85"
SQ   SEQUENCE   341 AA;  37367 MW;  D7F415A9ABC86125 CRC64;
     MHTDLDTDMD MDTETVALCS SSSRQASPLG TPTPEADTTL LKQKPEKLLA ELDLSGPPPA
     PGVPRRRGSM PVPYKHQLRR AQAVDELDWP PQASPSGSSD SLGSGEAALT QKDGVFKVML
     VGESGVGKST LAGTFGGLQG DHAHEMENSE DTYERRIMVD KEEVTLIVYD IWEQGDAGGW
     LQDHCLQTGD AFLIVFSVTD RRGFSKVPET LLRLRAGRPH HDLPVILVGN KSDLARSREV
     SLEEGRHLAG TLSCKHIETS AALHHNTREL FEGAVRQIRL RRGRGHAGGQ RPEPSSPDGP
     APPTRRESLT KKAKRFLANL VPRNAKFFKQ RSRSCHDLSV L
 
 
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