RABE2_BOVIN
ID RABE2_BOVIN Reviewed; 585 AA.
AC A4FUG8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Rab GTPase-binding effector protein 2;
GN Name=RABEP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 RAB4; 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; BC114873; AAI14874.1; -; mRNA.
DR RefSeq; NP_001076877.2; NM_001083408.2.
DR AlphaFoldDB; A4FUG8; -.
DR SMR; A4FUG8; -.
DR BioGRID; 168367; 2.
DR STRING; 9913.ENSBTAP00000008595; -.
DR PaxDb; A4FUG8; -.
DR PRIDE; A4FUG8; -.
DR Ensembl; ENSBTAT00000008595; ENSBTAP00000008595; ENSBTAG00000006542.
DR GeneID; 511736; -.
DR KEGG; bta:511736; -.
DR CTD; 79874; -.
DR VEuPathDB; HostDB:ENSBTAG00000006542; -.
DR VGNC; VGNC:33668; RABEP2.
DR eggNOG; KOG0993; Eukaryota.
DR GeneTree; ENSGT00530000063743; -.
DR HOGENOM; CLU_035043_0_0_1; -.
DR InParanoid; A4FUG8; -.
DR OMA; QCDEEIQ; -.
DR OrthoDB; 1369937at2759; -.
DR TreeFam; TF329365; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000006542; Expressed in retina and 105 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
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; 1.
DR Pfam; PF03528; Rabaptin; 1.
DR PRINTS; PR01432; RABAPTIN.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT CHAIN 2..585
FT /note="Rab GTPase-binding effector protein 2"
FT /id="PRO_0000346792"
FT REGION 178..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..183
FT /evidence="ECO:0000255"
FT COILED 288..540
FT /evidence="ECO:0000255"
FT COMPBIAS 248..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62835"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
SQ SEQUENCE 585 AA; 65602 MW; 47D90C9664C0BC40 CRC64;
MAAAAPAAAG EDGRRRLPGA ALDIQPQEGA KVEAESGELE RLRAELAGAL AEMETMKAVA
EVSESTKAEA VAAVQRQCQE EVASLQAILK DSISSYEAQI TSLKQERQQQ QQDCEEKERE
LGRLKQLLSR AHPLDSLEKQ MEKAHEDSEK LREIVLPMEQ EIEELKAKLL RAEELIQEIQ
RRPRHPPSLH GSTELLLSRD PSPPLEPLEE LSEDGGPAAE AFAHNCDDSA SISSFSLGGG
ASGRASLPRS RQGLSPEQEE TASLVSTGTL VPEGIYLPPP GYQLVPDNQW EQLQLEGRQL
QKDLESISRE RDELQEGLRR SNEDCAKQMQ VLLAQVQNSE QLLRTLQGTV SQAQERVQLQ
MAELANSHKC LSHEVKRLTE ENQGLRAEQP SSSVPRVLEQ DEGWEESLPS SLPELQQLVR
RTQQEARARQ QAQEHEAERL RIEIVTLREA LDEETAARAS LEGQLRVQRE ETEVLEASLC
SLRMEMERVQ EEQSKAKRQE VLRPSQGTGR TEEAQLTDLL SEQRAKMLRL QAELETSEQV
QRDFVRLSQA LQVRLERIRQ AGSLEQVRGI IDEAPLRDVR DIKDT
