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RB22A_MOUSE
ID   RB22A_MOUSE             Reviewed;         194 AA.
AC   P35285; Q3UCA7; Q91VD4;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Ras-related protein Rab-22A;
DE            Short=Rab-22;
DE   AltName: Full=Rab-14;
GN   Name=Rab22a; Synonyms=Rab22;
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].
RA   Kussmann S., Worch S., Hansmann I., Schlote D.;
RT   "Mapping and characterization of mouse Rab22a gene.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [MRNA] OF 17-65.
RC   TISSUE=Kidney;
RX   PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT   by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=8126105; DOI=10.1242/jcs.106.4.1249;
RA   Olkkonen V.M., Dupree P., Killisch I., Luetcke A., Simons K., Zerial M.;
RT   "Molecular cloning and subcellular localization of three GTP-binding
RT   proteins of the rab subfamily.";
RL   J. Cell Sci. 106:1249-1261(1993).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RABGEF1.
RX   PubMed=19759177; DOI=10.1091/mbc.e09-06-0453;
RA   Zhu H., Liang Z., Li G.;
RT   "Rabex-5 is a Rab22 effector and mediates a Rab22-Rab5 signaling cascade in
RT   endocytosis.";
RL   Mol. Biol. Cell 20:4720-4729(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-64.
RX   PubMed=27718357; DOI=10.7554/elife.20417;
RA   Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT   "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT   recycling via recruiting RabGAP1L to early endosomes.";
RL   Elife 5:0-0(2016).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-169 IN COMPLEX WITH GTP ANALOG
RP   AND ZFYVE20, AND INTERACTION WITH ZFYVE20.
RX   PubMed=16034420; DOI=10.1038/nature03798;
RA   Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT   "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL   Nature 436:415-419(2005).
CC   -!- FUNCTION: Plays a role in endocytosis and intracellular protein
CC       transport (PubMed:19759177, PubMed:27718357). Mediates trafficking of
CC       TF from early endosomes to recycling endosomes. Required for NGF-
CC       mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds
CC       GTP and GDP and has low GTPase activity. Alternates between a GTP-bound
CC       active form and a GDP-bound inactive form (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:19759177,
CC       ECO:0000269|PubMed:27718357}.
CC   -!- SUBUNIT: Binds EEA1 (By similarity). Interacts (in its GTP-bound form)
CC       with RINL (By similarity). Interacts directly with ZFYVE20
CC       (PubMed:16034420). Interacts (in its GTP-bound form) with RABGEF1
CC       (PubMed:19759177). {ECO:0000250|UniProtKB:P51154,
CC       ECO:0000250|UniProtKB:Q9UL26, ECO:0000269|PubMed:16034420,
CC       ECO:0000269|PubMed:19759177}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:27718357};
CC       Lipid-anchor {ECO:0000305}. Cell membrane
CC       {ECO:0000250|UniProtKB:P51154}; Lipid-anchor {ECO:0000305}. Early
CC       endosome {ECO:0000269|PubMed:19759177, ECO:0000269|PubMed:27718357}.
CC       Late endosome {ECO:0000250|UniProtKB:P51154}. Cell projection, ruffle
CC       {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:27718357}. Cytoplasmic vesicle, phagosome
CC       {ECO:0000250|UniProtKB:Q9UL26}. Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}. Note=Recruited to phagosomes containing S.aureus or
CC       M.tuberculosis. {ECO:0000250|UniProtKB:Q9UL26}.
CC   -!- TISSUE SPECIFICITY: Detected in brain and heart, and at lower levels in
CC       lung and spleen. {ECO:0000269|PubMed:8126105}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AJ311124; CAC41378.1; -; mRNA.
DR   EMBL; AK031667; BAC27501.1; -; mRNA.
DR   EMBL; AK146594; BAE27289.1; -; mRNA.
DR   EMBL; AK150617; BAE29707.1; -; mRNA.
DR   EMBL; BC006596; AAH06596.1; -; mRNA.
DR   EMBL; M79304; AAK14828.1; -; mRNA.
DR   CCDS; CCDS38352.1; -.
DR   PIR; JH0644; JH0644.
DR   RefSeq; NP_077756.2; NM_024436.3.
DR   PDB; 1YVD; X-ray; 1.93 A; A=3-169.
DR   PDB; 1Z0J; X-ray; 1.32 A; A=2-169.
DR   PDBsum; 1YVD; -.
DR   PDBsum; 1Z0J; -.
DR   AlphaFoldDB; P35285; -.
DR   SMR; P35285; -.
DR   BioGRID; 202539; 1.
DR   DIP; DIP-60516N; -.
DR   IntAct; P35285; 33.
DR   STRING; 10090.ENSMUSP00000029024; -.
DR   iPTMnet; P35285; -.
DR   PhosphoSitePlus; P35285; -.
DR   EPD; P35285; -.
DR   PaxDb; P35285; -.
DR   PeptideAtlas; P35285; -.
DR   PRIDE; P35285; -.
DR   ProteomicsDB; 300246; -.
DR   Antibodypedia; 29093; 160 antibodies from 30 providers.
DR   DNASU; 19334; -.
DR   Ensembl; ENSMUST00000029024; ENSMUSP00000029024; ENSMUSG00000027519.
DR   GeneID; 19334; -.
DR   KEGG; mmu:19334; -.
DR   UCSC; uc008oed.1; mouse.
DR   CTD; 57403; -.
DR   MGI; MGI:105072; Rab22a.
DR   VEuPathDB; HostDB:ENSMUSG00000027519; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000157009; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P35285; -.
DR   OMA; SESHRTC; -.
DR   OrthoDB; 1340129at2759; -.
DR   PhylomeDB; P35285; -.
DR   TreeFam; TF331262; -.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 19334; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Rab22a; mouse.
DR   EvolutionaryTrace; P35285; -.
DR   PRO; PR:P35285; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P35285; protein.
DR   Bgee; ENSMUSG00000027519; Expressed in humerus cartilage element and 251 other tissues.
DR   ExpressionAtlas; P35285; baseline and differential.
DR   Genevisible; P35285; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; ISO:MGI.
DR   GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0097494; P:regulation of vesicle size; ISO:MGI.
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   3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW   Endocytosis; Endosome; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..194
FT                   /note="Ras-related protein Rab-22A"
FT                   /id="PRO_0000121210"
FT   REGION          170..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         60..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   BINDING         148..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   LIPID           193
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           194
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         64
FT                   /note="Q->L: Constitutively active. Disrupts general
FT                   recycling of receptors in embryonic fibroblasts."
FT                   /evidence="ECO:0000269|PubMed:27718357"
FT   CONFLICT        54
FT                   /note="H -> R (in Ref. 4; AAK14828)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   STRAND          39..49
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   STRAND          52..61
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           65..71
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   STRAND          79..86
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           90..106
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   STRAND          111..118
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           130..139
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   TURN            149..152
FT                   /evidence="ECO:0007829|PDB:1Z0J"
FT   HELIX           155..165
FT                   /evidence="ECO:0007829|PDB:1Z0J"
SQ   SEQUENCE   194 AA;  21802 MW;  1799B676CA9091F7 CRC64;
     MALRELKVCL LGDTGVGKSS IVWRFVEDSF DPNINPTIGA SFMTKTVQYQ NELHKFLIWD
     TAGQERFRAL APMYYRGSAA AIIVYDITKE ETFSTLKNWV RELRQHGPPS IVVAIAGNKC
     DLTDVREVME RDAKDYADSI HAIFVETSAK NAININELFI EISRRIPSTD ANPASGGKGF
     KLRRQPSEPK RSCC
 
 
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