RABE2_PONAB
ID RABE2_PONAB Reviewed; 569 AA.
AC Q5RCR6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Rab GTPase-binding effector protein 2;
GN Name=RABEP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- SEQUENCE CAUTION:
CC Sequence=CAH90441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CR858203; CAH90441.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001127288.1; NM_001133816.1.
DR AlphaFoldDB; Q5RCR6; -.
DR SMR; Q5RCR6; -.
DR STRING; 9601.ENSPPYP00000008167; -.
DR GeneID; 100174345; -.
DR KEGG; pon:100174345; -.
DR CTD; 79874; -.
DR eggNOG; KOG0993; Eukaryota.
DR InParanoid; Q5RCR6; -.
DR OrthoDB; 1369937at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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 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 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..569
FT /note="Rab GTPase-binding effector protein 2"
FT /id="PRO_0000346793"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..184
FT /evidence="ECO:0000255"
FT COILED 292..391
FT /evidence="ECO:0000255"
FT COILED 423..523
FT /evidence="ECO:0000255"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..267
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 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62835"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5N1"
SQ SEQUENCE 569 AA; 63609 MW; 130E37ABA005C3E6 CRC64;
MAAAAPVAAD DDERRRRPGA ALEDSRPQEG ANGEAELGEL SRLRAELAGA LAEMETMKAV
AEVSESTKAE AVAAVQRQCQ EEVASLQAIL KDSISSYEAQ ITALKQERQQ QQQDCEEKER
ELGRLKQLLS RAHPLDSLEK QMEKAHEDSE KLREIVLPME KEIEELKAKL LRAEELIQEI
QRRPQHVPSL HGSTELLPLS RDPSPPLEPL EELSGDGGPA AEAFAHNCDD SASISSFSLG
GGVGSSSSLP RSRQGLSPEQ EETASLVSTG TLVPEGIYLP PPGYQLVPDT QWEQLQMEGR
QLQKDLESVS RERDELQEGL RRSNEDCAKQ MQVLLAQVQN AEQLLRTLQG TVSQAQERVQ
LQMAELVTTH KCLHHEVKRL NEENQGLRAE QLPSSAPQGP QQEQGEEESL PSSVPELQQL
LCRTRQEARA QLQAQEHGAE RLRIEIVTLR EALEEETAAR ASLEGQLRVQ REETEVLEAS
LCSLRTEMER VQQEQSKPQL PDLLSEQRAK VLRLQAELET SEQVQRDFVR LSQALQVRLE
RIRQAETLEQ VHSIMDEAPL TDVRDIKDT
