RABE2_MOUSE
ID RABE2_MOUSE Reviewed; 554 AA.
AC Q91WG2; Q3UMK8; Q99KN3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Rab GTPase-binding effector protein 2;
DE AltName: Full=Rabaptin-5beta;
GN Name=Rabep2; Synonyms=Rabpt5b;
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=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Plays a role in membrane trafficking and in homotypic early
CC endosome fusion. Participates in arteriogenesis by regulating vascular
CC endothelial growth factor receptor 2/VEGFR2 cell surface expression and
CC endosomal trafficking. By interacting with SDCCAG8, localizes to
CC centrosomes and plays a critical role in ciliogenesis.
CC {ECO:0000250|UniProtKB:Q9H5N1}.
CC -!- SUBUNIT: Heterodimer with RABGEF1. The dimer binds RAB5A that has been
CC activated by GTP-binding. Interacts with SDCCAG8; this interaction is
CC important for ciliogenesis regulation. Interacts with RAB4A; this
CC interaction may mediate VEGFR2 cell surface expression.
CC {ECO:0000250|UniProtKB:Q9H5N1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H5N1}. Early
CC endosome {ECO:0000250|UniProtKB:Q9H5N1}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9H5N1}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q9H5N1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q91WG2-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WG2-1; Sequence=VSP_010460;
CC Name=3;
CC IsoId=Q91WG2-2; Sequence=VSP_010461;
CC -!- SIMILARITY: Belongs to the rabaptin family. {ECO:0000305}.
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DR EMBL; AK144836; BAE26090.1; -; mRNA.
DR EMBL; BC004088; AAH04088.1; -; mRNA.
DR EMBL; BC015287; AAH15287.1; -; mRNA.
DR CCDS; CCDS21829.2; -. [Q91WG2-3]
DR RefSeq; NP_085043.2; NM_030566.2. [Q91WG2-3]
DR AlphaFoldDB; Q91WG2; -.
DR SMR; Q91WG2; -.
DR BioGRID; 213981; 9.
DR IntAct; Q91WG2; 5.
DR STRING; 10090.ENSMUSP00000102015; -.
DR iPTMnet; Q91WG2; -.
DR PhosphoSitePlus; Q91WG2; -.
DR EPD; Q91WG2; -.
DR MaxQB; Q91WG2; -.
DR PaxDb; Q91WG2; -.
DR PeptideAtlas; Q91WG2; -.
DR PRIDE; Q91WG2; -.
DR ProteomicsDB; 300384; -. [Q91WG2-3]
DR ProteomicsDB; 300385; -. [Q91WG2-1]
DR ProteomicsDB; 300386; -. [Q91WG2-2]
DR Antibodypedia; 26625; 134 antibodies from 26 providers.
DR Ensembl; ENSMUST00000106405; ENSMUSP00000102013; ENSMUSG00000030727. [Q91WG2-1]
DR Ensembl; ENSMUST00000106407; ENSMUSP00000102015; ENSMUSG00000030727. [Q91WG2-3]
DR GeneID; 70314; -.
DR KEGG; mmu:70314; -.
DR UCSC; uc009jrd.1; mouse. [Q91WG2-3]
DR CTD; 79874; -.
DR MGI; MGI:1917564; Rabep2.
DR VEuPathDB; HostDB:ENSMUSG00000030727; -.
DR eggNOG; KOG0993; Eukaryota.
DR GeneTree; ENSGT00530000063743; -.
DR HOGENOM; CLU_035043_0_0_1; -.
DR InParanoid; Q91WG2; -.
DR OMA; QCDEEIQ; -.
DR OrthoDB; 1369937at2759; -.
DR PhylomeDB; Q91WG2; -.
DR TreeFam; TF329365; -.
DR BioGRID-ORCS; 70314; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rabep2; mouse.
DR PRO; PR:Q91WG2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91WG2; protein.
DR Bgee; ENSMUSG00000030727; Expressed in lacrimal gland and 226 other tissues.
DR ExpressionAtlas; Q91WG2; baseline and differential.
DR Genevisible; Q91WG2; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1902017; P:regulation of cilium assembly; ISO:MGI.
DR InterPro; IPR003914; Rabaptin.
DR InterPro; IPR029882; Rabaptin-5beta.
DR InterPro; IPR018514; Rabaptin_coiled-coil.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR PANTHER; PTHR31179; PTHR31179; 1.
DR PANTHER; PTHR31179:SF6; PTHR31179:SF6; 1.
DR Pfam; PF09311; Rab5-bind; 2.
DR Pfam; PF03528; Rabaptin; 1.
DR PRINTS; PR01432; RABAPTIN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis; Endosome;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..554
FT /note="Rab GTPase-binding effector protein 2"
FT /id="PRO_0000187560"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..173
FT /evidence="ECO:0000255"
FT COILED 274..509
FT /evidence="ECO:0000255"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62835"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010460"
FT VAR_SEQ 483..554
FT /note="AQLTDLLSEQRAKTLRLQAELETSEQVQRDFVRLSQALQVRLERIRQAETLQ
FT QVRSILDEAPLRDIRDIKDS -> VSGAGGLA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010461"
SQ SEQUENCE 554 AA; 62132 MW; E94C2FB6A8A89130 CRC64;
MAAAPATLAL DPQPQEKQKD ASESSELSRL RAELAGALAE METMKAVAEV SESTKAEAVA
AVQRQCQEEV ASLQAILKDS ISSYETQIAA LKQERQQQQQ DFEEKDRELG HLKQLLARAH
PLDSLEKQME KAHEDSEKLR EIVLPMEQEI TELKGKLQRA EELIQEIQRR PRQPASLHGS
TELLPLSRNP SPPLEPLEEP SGDAGPAAEA FAHNCDDSAS ISSFSLGGAA GSASLRGPQG
LSPEQEETAS LVSTGTLVPE GIFLPPPGYQ LVPDSQWEQL QVEGRQLQKE LESVSRERDE
LQEGLRRSNE DCAKQMQVLL AQVQNSEQLL RTLQGTVSQA QERVQLQMAE LATSHKCLSQ
EVKRLNEENQ GLRAEQLPSS ALQGSEQRED QDEALPSSIQ ELHLLVQNTR QQARARQQAQ
EHEAERLRIE IVKLREALDE ETAAKASLER QLRVQREETD VLEASLCSLR IETERVQQEQ
RKAQLTDLLS EQRAKTLRLQ AELETSEQVQ RDFVRLSQAL QVRLERIRQA ETLQQVRSIL
DEAPLRDIRD IKDS
