RP1BL_HUMAN
ID RP1BL_HUMAN Reviewed; 184 AA.
AC A6NIZ1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ras-related protein Rap-1b-like protein;
DE Flags: Precursor;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- ACTIVITY REGULATION: Activated by guanine nucleotide-exchange factor
CC (GEF) EPAC2 in a cAMP-dependent manner. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SGSM1, SGSM2 and SGSM3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Note=May shuttle between plasma membrane and cytosol.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; CR611640; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC113404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95773.1; -; Genomic_DNA.
DR AlphaFoldDB; A6NIZ1; -.
DR SMR; A6NIZ1; -.
DR IntAct; A6NIZ1; 6.
DR MINT; A6NIZ1; -.
DR iPTMnet; A6NIZ1; -.
DR MetOSite; A6NIZ1; -.
DR PhosphoSitePlus; A6NIZ1; -.
DR SwissPalm; A6NIZ1; -.
DR BioMuta; -; -.
DR jPOST; A6NIZ1; -.
DR MassIVE; A6NIZ1; -.
DR MaxQB; A6NIZ1; -.
DR PeptideAtlas; A6NIZ1; -.
DR PRIDE; A6NIZ1; -.
DR neXtProt; NX_A6NIZ1; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR PhylomeDB; A6NIZ1; -.
DR PathwayCommons; A6NIZ1; -.
DR Pharos; A6NIZ1; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NIZ1; protein.
DR Genevisible; A6NIZ1; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0071320; P:cellular response to cAMP; IBA:GO_Central.
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 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 ADP-ribosylation; Cell membrane; Cytoplasm; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..181
FT /note="Ras-related protein Rap-1b-like protein"
FT /id="PRO_0000343734"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000343735"
FT MOTIF 32..40
FT /note="Effector region"
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 39
FT /note="ADP-ribosylserine; by botulinum toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="Phosphoserine; by PKA"
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"
SQ SEQUENCE 184 AA; 20925 MW; DF8D6225E43C5499 CRC64;
MREYKLVVLG SRGVGKSALT VQFVQGIFVE KYDPTIEDSY REQVEVDAQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS
CQLL
