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RAB37_MOUSE
ID   RAB37_MOUSE             Reviewed;         223 AA.
AC   Q9JKM7; Q8C7E1;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Ras-related protein Rab-37;
DE   Flags: Precursor;
GN   Name=Rab37;
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 [MRNA].
RX   PubMed=10722846; DOI=10.1016/s0014-5793(00)01288-6;
RA   Masuda E.S., Luo Y., Young C., Shen M., Rossi A.B., Huang B.C., Yu S.,
RA   Bennett M.K., Payan D.G., Scheller R.H.;
RT   "Rab37 is a novel mast cell specific GTPase localized to secretory
RT   granules.";
RL   FEBS Lett. 470:61-64(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
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   [3]
RP   PROTEIN SEQUENCE OF 71-91, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH RIMS1.
RX   PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA   Fukuda M.;
RT   "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT   Identification of a critical determinant of Rab3A/Rab27A recognition by
RT   Rim2.";
RL   J. Biol. Chem. 278:15373-15380(2003).
RN   [5]
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).
CC   -!- SUBUNIT: Interacts with RIMS1. {ECO:0000269|PubMed:12578829}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Secretory granules.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the bone marrow mast
CC       cells.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AF233582; AAF67162.1; -; mRNA.
DR   EMBL; AK050483; BAC34282.1; -; mRNA.
DR   CCDS; CCDS25620.1; -.
DR   RefSeq; NP_067386.3; NM_021411.4.
DR   AlphaFoldDB; Q9JKM7; -.
DR   SMR; Q9JKM7; -.
DR   BioGRID; 208399; 2.
DR   IntAct; Q9JKM7; 4.
DR   STRING; 10090.ENSMUSP00000021076; -.
DR   iPTMnet; Q9JKM7; -.
DR   PhosphoSitePlus; Q9JKM7; -.
DR   EPD; Q9JKM7; -.
DR   jPOST; Q9JKM7; -.
DR   MaxQB; Q9JKM7; -.
DR   PaxDb; Q9JKM7; -.
DR   PRIDE; Q9JKM7; -.
DR   ProteomicsDB; 253145; -.
DR   DNASU; 58222; -.
DR   GeneID; 58222; -.
DR   KEGG; mmu:58222; -.
DR   CTD; 326624; -.
DR   MGI; MGI:1929945; Rab37.
DR   eggNOG; KOG0083; Eukaryota.
DR   InParanoid; Q9JKM7; -.
DR   OrthoDB; 1018397at2759; -.
DR   PhylomeDB; Q9JKM7; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 58222; 2 hits in 75 CRISPR screens.
DR   ChiTaRS; Rab37; mouse.
DR   PRO; PR:Q9JKM7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9JKM7; protein.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; ISS:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasmic vesicle; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AX2"
FT   CHAIN           2..220
FT                   /note="Ras-related protein Rab-37"
FT                   /id="PRO_0000121250"
FT   PROPEP          221..223
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370829"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..67
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AX2"
FT   MOD_RES         220
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           219
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           220
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        67
FT                   /note="S -> F (in Ref. 1; AAF67162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  24656 MW;  8C500ED4CE854C24 CRC64;
     MTGTPGAATA GDGEAPERSP PFSPNYDLTG KVMLLGDSGV GKTCFLIQFK DGAFLSGTFI
     ATVGIDSRNK VVTVDGARVK LQIWDTAGQE RFRSVTHAYY RDAQALLLLY DITNQSSFDN
     IRAWLTEIHE YAQRDVVIML LGNKADVSSE RVIRSEDGET LAREYGVPFM ETSAKTGMNV
     ELAFLAIAKE LKYRAGRQPD EPSFQIRDYV ESQKKRSSCC SFV
 
 
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