RABE2_RAT
ID RABE2_RAT Reviewed; 554 AA.
AC Q62835;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Rab GTPase-binding effector protein 2;
DE AltName: Full=MP13 protein;
DE AltName: Full=Rabaptin-5beta;
GN Name=Rabep2; Synonyms=Rabpt5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344; TISSUE=Hippocampus;
RX PubMed=11108998; DOI=10.1016/s0304-3940(00)01641-4;
RA Feng Z., Hong J., Qi Q., Han Y., Wilson B., Iadarola M., Tiao N., Bing G.;
RT "Cloning and expression of MP13 gene from rat hippocampus, a new factor
RT related to guanosine triphosphate regulation.";
RL Neurosci. Lett. 296:129-132(2000).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the rabaptin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U34932; AAA79137.1; -; mRNA.
DR RefSeq; NP_085074.1; NM_030585.1.
DR AlphaFoldDB; Q62835; -.
DR SMR; Q62835; -.
DR BioGRID; 249480; 2.
DR STRING; 10116.ENSRNOP00000025043; -.
DR iPTMnet; Q62835; -.
DR PhosphoSitePlus; Q62835; -.
DR jPOST; Q62835; -.
DR PaxDb; Q62835; -.
DR PRIDE; Q62835; -.
DR GeneID; 80754; -.
DR KEGG; rno:80754; -.
DR CTD; 79874; -.
DR RGD; 621416; Rabep2.
DR eggNOG; KOG0993; Eukaryota.
DR InParanoid; Q62835; -.
DR OrthoDB; 1369937at2759; -.
DR PhylomeDB; Q62835; -.
DR PRO; PR:Q62835; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:RGD.
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 Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..554
FT /note="Rab GTPase-binding effector protein 2"
FT /id="PRO_0000187561"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..173
FT /evidence="ECO:0000255"
FT COILED 274..512
FT /evidence="ECO:0000255"
FT COMPBIAS 376..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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"
SQ SEQUENCE 554 AA; 61973 MW; 39448FAF2B41A004 CRC64;
MAAAPAALAL DPQPQEEQKD ASESSELSRL RAELAGALAE METMKAVAEV SESTKAEAVA
AVQRQCQEEV ASLQAILKDS ISSYETQIAA LKQERQQQQQ DSEEKERELG HLKQLLARAH
PLDSLEKQME KAHEDSEKLR EIVLPMEQEI AELKVKLLRA EELIQEIQRR PRQPASLHGS
TELLPLSRNP SPPLEPSEEP SGDAGPAAEA FAHNCDDSAS ISSFSLGGAA GSVSLRGPQG
LSPEQEETAS LVSTGTLVPE GIYLPPPGYQ LVPDSQWEQL QVEGRQLQKE LESVRRERDE
LQEGLSRSNE DCAKQMQVLL AQVQNSEQLL RTLQGTVSQA QERVQRQMAE LATSHKCLSQ
EVKRLNEENR GLRAEQLPSS ALQGSEQQED QDEALPSSIQ ELHQLVRHTR QQARARQQAQ
EHEAERLRIE IVKLREALDE ETAAKASLEG QLRVQREETD VLEASLCSLR IETERVQQEH
HKAQLTDLLS EQRAKALRLQ AELETSEQVQ RDFVRLSQAL QVRLEQIRQA DTLEQVRSIL
DEAPLRDIKD IKDS
