RPGP1_MOUSE
ID RPGP1_MOUSE Reviewed; 663 AA.
AC A2ALS5; E9PZZ8; Q6A063; Q80VZ8; Q8K2L6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Rap1 GTPase-activating protein 1;
DE Short=Rap1GAP;
DE Short=Rap1GAP1;
DE AltName: Full=ARPP-90;
GN Name=Rap1gap; Synonyms=Kiaa0474, Rap1ga1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 241-663 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
RN [4]
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-499.
RX PubMed=19218462; DOI=10.1073/pnas.0813263106;
RA McAvoy T., Zhou M.M., Greengard P., Nairn A.C.;
RT "Phosphorylation of Rap1GAP, a striatally enriched protein, by protein
RT kinase A controls Rap1 activity and dendritic spine morphology.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3531-3536(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-484; SER-499;
RP SER-541 AND SER-542, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND
RP THR-9 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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 -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-
CC bound state. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and heterodimer with RAP1B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2ALS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ALS5-2; Sequence=VSP_053560;
CC Name=3;
CC IsoId=A2ALS5-3; Sequence=VSP_053561;
CC Name=4;
CC IsoId=A2ALS5-4; Sequence=VSP_053562;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and striatum (at protein
CC level). Detected in brain cortex and striatum.
CC {ECO:0000269|PubMed:19218462}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52065.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32233.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172955; BAD32233.1; ALT_INIT; mRNA.
DR EMBL; AL805954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030891; AAH30891.1; -; mRNA.
DR EMBL; BC052065; AAH52065.1; ALT_INIT; mRNA.
DR CCDS; CCDS38925.1; -. [A2ALS5-2]
DR CCDS; CCDS84809.1; -. [A2ALS5-3]
DR RefSeq; NP_001074624.1; NM_001081155.3. [A2ALS5-2]
DR RefSeq; NP_001318144.1; NM_001331215.1. [A2ALS5-3]
DR RefSeq; NP_083839.1; NM_029563.2. [A2ALS5-1]
DR AlphaFoldDB; A2ALS5; -.
DR SMR; A2ALS5; -.
DR BioGRID; 225521; 9.
DR IntAct; A2ALS5; 2.
DR STRING; 10090.ENSMUSP00000101461; -.
DR iPTMnet; A2ALS5; -.
DR PhosphoSitePlus; A2ALS5; -.
DR MaxQB; A2ALS5; -.
DR PaxDb; A2ALS5; -.
DR PeptideAtlas; A2ALS5; -.
DR PRIDE; A2ALS5; -.
DR ProteomicsDB; 260929; -. [A2ALS5-1]
DR ProteomicsDB; 260930; -. [A2ALS5-2]
DR ProteomicsDB; 260931; -. [A2ALS5-3]
DR ProteomicsDB; 260932; -. [A2ALS5-4]
DR Antibodypedia; 1096; 248 antibodies from 30 providers.
DR DNASU; 110351; -.
DR Ensembl; ENSMUST00000047243; ENSMUSP00000042473; ENSMUSG00000041351. [A2ALS5-2]
DR Ensembl; ENSMUST00000097837; ENSMUSP00000095448; ENSMUSG00000041351. [A2ALS5-3]
DR GeneID; 110351; -.
DR KEGG; mmu:110351; -.
DR UCSC; uc008vjm.2; mouse. [A2ALS5-1]
DR UCSC; uc008vjn.2; mouse. [A2ALS5-2]
DR CTD; 5909; -.
DR MGI; MGI:109338; Rap1gap.
DR VEuPathDB; HostDB:ENSMUSG00000041351; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000156138; -.
DR HOGENOM; CLU_010739_2_1_1; -.
DR OMA; ESISCVT; -.
DR OrthoDB; 845465at2759; -.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 110351; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rap1gap; mouse.
DR PRO; PR:A2ALS5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2ALS5; protein.
DR Bgee; ENSMUSG00000041351; Expressed in superior frontal gyrus and 204 other tissues.
DR ExpressionAtlas; A2ALS5; baseline and differential.
DR Genevisible; A2ALS5; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:1990792; P:cellular response to glial cell derived neurotrophic factor; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:1904425; P:negative regulation of GTP binding; ISO:MGI.
DR GO; GO:1903697; P:negative regulation of microvillus assembly; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:1904442; P:negative regulation of thyroid gland epithelial cell proliferation; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR Pfam; PF02188; GoLoco; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SMART; SM00390; GoLoco; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..663
FT /note="Rap1 GTPase-activating protein 1"
FT /id="PRO_0000424956"
FT DOMAIN 1..17
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 181..397
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19218462,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47736"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1
FT /note="M -> MSGRKRSFTFGAYGGVDKSFSLRQSVWRSDGQKQSFPQALNLLLVDS
FT VPSHPASPYPKNTDLFEM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053560"
FT VAR_SEQ 1
FT /note="M -> MAQPRPPAPHGRPRRGSLPAGAGWQNTDLFEM (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053561"
FT VAR_SEQ 593..663
FT /note="ESVSSSGTPHKRDSFLYSTWLDDSVSTTSGGSSPGLTRSPHPDVGKSGDPAC
FT PEIKIQLETSEQHTPQMGC -> HMAGRQREHHERGQLPSEVAPSCPPSQASHGHPTQT
FT SASRGTLRVPRSRSNWKHLSSTHPRWAASCHLISRRD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053562"
FT CONFLICT 413
FT /note="G -> S (in Ref. 1; BAD32233)"
FT /evidence="ECO:0000305"
FT MOD_RES A2ALS5-2:7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES A2ALS5-2:9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES A2ALS5-3:17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 663 AA; 73433 MW; E3C8B54957C30C71 CRC64;
MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ FGGYWIEGTN
HEISSLPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF NYYSLDTALG HLVFSLKYDV
IGDQEHLRLL LRTKCRTHHD VIPISCLTEF PNVVQMAKLV CEDVNVDRFY PVLYPKASRL
IVTFDEHVIS NNFKFGVIYQ KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR
GGLDVTHGQT GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE
NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP DPAVFRKGPE
FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE LHIHSQSMMG LGGDDDKMEN
GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK KPNTVSTSHS GSFTPNNPDL AKAAGISLIV
PGKSPTRKKS GPFGSRRSSA IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ
SSPEMPTTKN RVESAAQRTE VLQGFSRSSS SASSFTSVVE ETEGVDGDDT GLESVSSSGT
PHKRDSFLYS TWLDDSVSTT SGGSSPGLTR SPHPDVGKSG DPACPEIKIQ LETSEQHTPQ
MGC
