RPGP2_MOUSE
ID RPGP2_MOUSE Reviewed; 712 AA.
AC Q5SVL6; Q3KNA3; Q3V3L0; Q80TL8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Rap1 GTPase-activating protein 2;
DE Short=Rap1GAP2;
DE AltName: Full=GTPase-activating Rap/Ran-GAP domain-like protein 4;
GN Name=Rap1gap2; Synonyms=Garnl4, Kiaa1039, Rap1ga2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-712.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-712.
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-488; SER-495; SER-593
RP AND SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SVL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SVL6-2; Sequence=VSP_029890, VSP_029952;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65706.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65706.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AL604065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107388; AAI07389.1; -; mRNA.
DR EMBL; AK038834; BAE20542.1; -; mRNA.
DR EMBL; AK122424; BAC65706.1; ALT_SEQ; mRNA.
DR CCDS; CCDS25032.1; -. [Q5SVL6-1]
DR RefSeq; NP_001015046.1; NM_001015046.2. [Q5SVL6-1]
DR AlphaFoldDB; Q5SVL6; -.
DR SMR; Q5SVL6; -.
DR BioGRID; 237610; 5.
DR STRING; 10090.ENSMUSP00000099580; -.
DR iPTMnet; Q5SVL6; -.
DR PhosphoSitePlus; Q5SVL6; -.
DR MaxQB; Q5SVL6; -.
DR PaxDb; Q5SVL6; -.
DR PeptideAtlas; Q5SVL6; -.
DR PRIDE; Q5SVL6; -.
DR ProteomicsDB; 260933; -. [Q5SVL6-1]
DR ProteomicsDB; 260934; -. [Q5SVL6-2]
DR Antibodypedia; 5443; 35 antibodies from 15 providers.
DR DNASU; 380711; -.
DR Ensembl; ENSMUST00000102521; ENSMUSP00000099580; ENSMUSG00000038807. [Q5SVL6-1]
DR GeneID; 380711; -.
DR KEGG; mmu:380711; -.
DR UCSC; uc007kbw.1; mouse. [Q5SVL6-2]
DR UCSC; uc007kbx.1; mouse. [Q5SVL6-1]
DR CTD; 23108; -.
DR MGI; MGI:3028623; Rap1gap2.
DR VEuPathDB; HostDB:ENSMUSG00000038807; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000160935; -.
DR HOGENOM; CLU_010739_2_2_1; -.
DR InParanoid; Q5SVL6; -.
DR OrthoDB; 845465at2759; -.
DR PhylomeDB; Q5SVL6; -.
DR TreeFam; TF318626; -.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR BioGRID-ORCS; 380711; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Rap1gap2; mouse.
DR PRO; PR:Q5SVL6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SVL6; protein.
DR Bgee; ENSMUSG00000038807; Expressed in dorsal pancreas and 194 other tissues.
DR ExpressionAtlas; Q5SVL6; baseline and differential.
DR Genevisible; Q5SVL6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0008361; P:regulation of cell size; 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; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..712
FT /note="Rap1 GTPase-activating protein 2"
FT /id="PRO_0000312717"
FT DOMAIN 229..445
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q684P5"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q684P5"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q684P5"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q684P5"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029890"
FT VAR_SEQ 195..206
FT /note="LSKLPSVPQIAK -> MVLDLCVFLPSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029952"
SQ SEQUENCE 712 AA; 78254 MW; 49FD87D1AF030A57 CRC64;
MLAGLKVKKQ ELANSSDVTL PDRPLSPPLT APPTMKSAEF FEMLEKMQGI KLEEQRPGPQ
KNKDDYIPYP SIDEVVEKGG PYPLIILPQF GGYWIEDPEN VGTPTSLGSS VYEEEEEDSL
SPNTFGYKLE CRGEARAYRR HFLGKDHLNF YCTGSSLGNL ILSIKCEEAE GMEYLRIILR
SKLKTVHERI PLAGLSKLPS VPQIAKAFCD DAVGLKFNPV LYPKASQMIV SYDEHDVNNT
FKFGVIYQKA RQTLEEELFG NNEESPAFKE FLDLLGDTIT LQDFKGFRGG LDVTHGQTGV
ESVYTTFRDR EIMFHVSTKL PFTDGDTQQL QRKRHIGNDI VAIIFQEENT PFVPDMIASN
FLHAYIVVQA DNPGTETPSY KVSVTAREDV PAFGPPLPSP PVFQKGAEFR EFLLTKLTNA
ENACCKSDKF AKLEDRTRAA LLDNLHDELH THTQVMLGMG PEEDKFENGG HGGFLESFKR
AIRVRSHSME TMVGSQRKLH GGNLPGSLSG GIVHNSMEVT KTTFSPPVAA ATAKNQSRSP
IKRRSGLFPR LHSGSEGQGD SRTRCDSASS TPKTPDGGHS SQEIKSETSS NPSSPEICPN
KEKPFIKLKE NGRANISRSS SSTSSFSSTA GEGEAMEECD SGSSQPSTTS PFKQEVFAYS
PSPSSESPSL GAAATPIIMS RSPTDAKSRN SPRSNLKFRF DKLSHASSSA GH
