ID   RABE1_RAT               Reviewed;         862 AA.
AC   O35550; P70609;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Rab GTPase-binding effector protein 1;
DE   AltName: Full=Rabaptin-5;
DE   AltName: Full=Rabaptin-5alpha;
GN   Name=Rabep1; Synonyms=Rabpt5, Rabpt5a;
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=Sprague-Dawley; TISSUE=Brain;
RA   Fujimoto H., Uyeda A., Nishimune H., Taguchi T.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wang Y., Suedhof T.C.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 60-75; 301-311 AND 587-602, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH KCNH1.
RX   PubMed=22841712; DOI=10.1016/j.febslet.2012.07.055;
RA   Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.;
RT   "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion
RT   channel trafficking.";
RL   FEBS Lett. 586:3077-3084(2012).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, 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: Rab effector protein acting as linker between gamma-adaptin,
CC       RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane
CC       trafficking of recycling endosomes. Involved in KCNH1 channels
CC       trafficking to and from the cell membrane. Stimulates RABGEF1 mediated
CC       nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex
CC       from the endoplasmic reticulum through the Golgi to the cilium.
CC       {ECO:0000250|UniProtKB:O35551, ECO:0000250|UniProtKB:Q15276}.
CC   -!- SUBUNIT: Heterodimer with RABGEF1. The heterodimer binds RAB4A and
CC       RAB5A that have been activated by GTP-binding. Interacts with TSC2 (By
CC       similarity). Interacts with GGA1 (via GAE domain), GGA2 (via GAE
CC       domain) and GGA3 (via GAE domain) (By similarity). Interacts with AP1G1
CC       (via GAE domain) (By similarity). Interacts with AP1G2 (via GAE domain)
CC       (By similarity). Interacts with ECPAS (By similarity). Interacts with
CC       KCNH1 (By similarity). Interacts with PKD1 (via C-terminal domain) and
CC       GGA1; the interactions recruit PKD1:PKD2 complex to GGA1 and ARL3 at
CC       trans-Golgi network (By similarity). Interacts with KCNH1
CC       (PubMed:22841712). {ECO:0000250|UniProtKB:O35551,
CC       ECO:0000250|UniProtKB:Q15276, ECO:0000269|PubMed:22841712}.
CC   -!- INTERACTION:
CC       O35550; Q63472: Kcnh1; NbExp=2; IntAct=EBI-7991542, EBI-7991592;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC       {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle
CC       {ECO:0000250}.
CC   -!- PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of
CC       endosome fusion activity. {ECO:0000250}.
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; D85844; BAA21782.1; -; mRNA.
DR   EMBL; U70777; AAB47746.1; -; mRNA.
DR   RefSeq; NP_061997.1; NM_019124.1.
DR   AlphaFoldDB; O35550; -.
DR   SMR; O35550; -.
DR   BioGRID; 248445; 2.
DR   ELM; O35550; -.
DR   IntAct; O35550; 2.
DR   MINT; O35550; -.
DR   STRING; 10116.ENSRNOP00000050017; -.
DR   iPTMnet; O35550; -.
DR   PhosphoSitePlus; O35550; -.
DR   PaxDb; O35550; -.
DR   PRIDE; O35550; -.
DR   GeneID; 54190; -.
DR   KEGG; rno:54190; -.
DR   UCSC; RGD:708568; rat.
DR   CTD; 9135; -.
DR   RGD; 708568; Rabep1.
DR   eggNOG; KOG0993; Eukaryota.
DR   InParanoid; O35550; -.
DR   OrthoDB; 1369937at2759; -.
DR   PhylomeDB; O35550; -.
DR   PRO; PR:O35550; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0055037; C:recycling endosome; 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:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR   GO; GO:1903441; P:protein localization to ciliary membrane; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR   InterPro; IPR003914; Rabaptin.
DR   InterPro; IPR029880; Rabaptin-5.
DR   InterPro; IPR018514; Rabaptin_coiled-coil.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR   PANTHER; PTHR31179; PTHR31179; 1.
DR   PANTHER; PTHR31179:SF5; PTHR31179:SF5; 1.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF03528; Rabaptin; 1.
DR   PRINTS; PR01432; RABAPTIN.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endocytosis; Endosome; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   CHAIN           2..862
FT                   /note="Rab GTPase-binding effector protein 1"
FT                   /id="PRO_0000187558"
FT   REGION          315..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..328
FT                   /evidence="ECO:0000255"
FT   COILED          534..816
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        360..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   MOD_RES         282
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         408
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15276"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        79
FT                   /note="W -> S (in Ref. 2; AAB47746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="E -> D (in Ref. 2; AAB47746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="G -> E (in Ref. 2; AAB47746)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   862 AA;  99428 MW;  9C93CD967EF3202D CRC64;
     MAQPGPAPQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ
     NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAV
     MKETVRDYEH QFHLRLEQER AQWAQYRESA DREIADLRRR LSEGQEEENL ENEMKKAQED
     AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV
     LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
     MEIVLTSEQL RQVEELKKKD QEEDEQQRIN KGKDNKKIDT EEEVKIPVVC ALTQEESSTP
     LSNEEEHLDS THGSVHSLDA DLLLPSGDPF SKSDNDMFKE GLRRAQSTDS LGTSSSLQSK
     ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTVSLGSL QMPSGFMLTK DQERAIKAMT
     PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE
     KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKEKQE LEDFLRQSAE DSSHQISALV
     LRAQASEVLL EELQQSFSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV
     SLQLAEDFIL PDTVQVLREL VLKYRENIVH VRTAADHMEE KLKAEILFLK EQIQAEQCLK
     ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQLES TLREKSQQLE SLQEIKVNLE
     EQLKKETAAK ATVEQLMFEE KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS
     LERIRAILND TKLTDINQLP ET