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RAP1B_DANRE
ID   RAP1B_DANRE             Reviewed;         184 AA.
AC   Q6TEN1; Q5RGV9; Q803B8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Ras-related protein Rap-1b;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
DE   Flags: Precursor;
GN   Name=rap1b; ORFNames=si:dkey-31f5.4;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable GTP-binding protein that possesses GTPase activity.
CC       May play a role in endothelial cell polarity and endothelial barrier
CC       function (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P61224};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}. Cell junction {ECO:0000250}. Note=May shuttle between
CC       plasma membrane and cytosol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AY423018; AAQ97994.1; -; mRNA.
DR   EMBL; BX649534; CAI21142.1; -; Genomic_DNA.
DR   EMBL; BC044548; AAH44548.1; -; mRNA.
DR   RefSeq; NP_955827.1; NM_199533.1.
DR   AlphaFoldDB; Q6TEN1; -.
DR   SMR; Q6TEN1; -.
DR   STRING; 7955.ENSDARP00000114387; -.
DR   PaxDb; Q6TEN1; -.
DR   Ensembl; ENSDART00000042250; ENSDARP00000042249; ENSDARG00000008867.
DR   GeneID; 321107; -.
DR   KEGG; dre:321107; -.
DR   CTD; 5908; -.
DR   ZFIN; ZDB-GENE-030131-9662; rap1b.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000154429; -.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; Q6TEN1; -.
DR   OrthoDB; 1353024at2759; -.
DR   PhylomeDB; Q6TEN1; -.
DR   TreeFam; TF313014; -.
DR   Reactome; R-DRE-354192; Integrin signaling.
DR   Reactome; R-DRE-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-DRE-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-DRE-392517; Rap1 signalling.
DR   Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-8875555; MET activates RAP1 and RAC1.
DR   PRO; PR:Q6TEN1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 4.
DR   Bgee; ENSDARG00000008867; Expressed in spleen and 60 other tissues.
DR   ExpressionAtlas; Q6TEN1; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IMP:ZFIN.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IGI:ZFIN.
DR   GO; GO:0060536; P:cartilage morphogenesis; IGI:ZFIN.
DR   GO; GO:0071320; P:cellular response to cAMP; IBA:GO_Central.
DR   GO; GO:0003428; P:chondrocyte intercalation involved in growth plate cartilage morphogenesis; IGI:ZFIN.
DR   GO; GO:0060026; P:convergent extension; IMP:ZFIN.
DR   GO; GO:0007507; P:heart development; IGI:ZFIN.
DR   GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0032486; P:Rap protein signal transduction; IBA:GO_Central.
DR   GO; GO:0032525; P:somite rostral/caudal axis specification; IGI:ZFIN.
DR   GO; GO:0001756; P:somitogenesis; IGI:ZFIN.
DR   CDD; cd04175; Rap1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038851; Rap1.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Cytoplasm; GTP-binding; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome.
FT   CHAIN           1..181
FT                   /note="Ras-related protein Rap-1b"
FT                   /id="PRO_0000366913"
FT   PROPEP          182..184
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000366914"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         181
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           181
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        43..44
FT                   /note="QV -> AM (in Ref. 2; CAI21142)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="D -> G (in Ref. 3; AAH44548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   184 AA;  20828 MW;  CDC75A0BFF187D03 CRC64;
     MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG
     TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
     EDERVVGKEQ GQNLARQWNS CAFLESSAKS KINVNEIFYD LVRQINRKTP VTGKPRKKST
     CQLL
 
 
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