ID   R3GEF_RAT               Reviewed;         377 AA.
AC   Q99NH3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Guanine nucleotide exchange factor for Rab-3A;
DE   AltName: Full=Rab-3A-interacting-like protein 1;
DE            Short=Rab3A-interacting-like protein 1;
DE   AltName: Full=Rabin3-like 1;
GN   Name=Rab3il1; Synonyms=Grab;
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], FUNCTION, INTERACTION WITH IHPK1 AND RAB3A,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11516400; DOI=10.1016/s0896-6273(01)00384-1;
RA   Luo H.R., Saiardi A., Nagata E., Ye K., Yu H., Jung T.S., Luo X., Jain S.,
RA   Sawa A., Snyder S.H.;
RT   "GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which
RT   interacts with inositol hexakisphosphate kinase.";
RL   Neuron 31:439-451(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 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: Guanine nucleotide exchange factor (GEF) which may activate
CC       RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes
CC       the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins
CC       into their active GTP-bound form. May also activate RAB8A and RAB8B (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:11516400}.
CC   -!- SUBUNIT: Interacts with RAB3A and IHPK1 through the coiled-coil domain.
CC       This interaction is competitive. IHPK1 kinase activity is not required
CC       for this interaction. {ECO:0000269|PubMed:11516400}.
CC   -!- TISSUE SPECIFICITY: Selectively localized to the brain (at protein
CC       level). {ECO:0000269|PubMed:11516400}.
CC   -!- DEVELOPMENTAL STAGE: Negligible levels at embryonic stages E9 and E15.
CC       RAB3IL1 levels increase progressively at postnatal ages P3, P7 and P13
CC       with maximal levels in adult brain. {ECO:0000269|PubMed:11516400}.
CC   -!- SIMILARITY: Belongs to the SEC2 family. {ECO:0000305}.
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DR   EMBL; AY026049; AAK07668.1; -; mRNA.
DR   RefSeq; NP_599238.1; NM_134411.1.
DR   AlphaFoldDB; Q99NH3; -.
DR   SMR; Q99NH3; -.
DR   STRING; 10116.ENSRNOP00000027611; -.
DR   iPTMnet; Q99NH3; -.
DR   PhosphoSitePlus; Q99NH3; -.
DR   PaxDb; Q99NH3; -.
DR   GeneID; 171452; -.
DR   KEGG; rno:171452; -.
DR   UCSC; RGD:619764; rat.
DR   CTD; 5866; -.
DR   RGD; 619764; Rab3il1.
DR   eggNOG; KOG4324; Eukaryota.
DR   InParanoid; Q99NH3; -.
DR   OrthoDB; 619794at2759; -.
DR   PhylomeDB; Q99NH3; -.
DR   Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q99NH3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0019900; F:kinase binding; IDA:RGD.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR   InterPro; IPR009449; Sec2_N.
DR   PANTHER; PTHR14430; PTHR14430; 1.
DR   Pfam; PF06428; Sec2p; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..377
FT                   /note="Guanine nucleotide exchange factor for Rab-3A"
FT                   /id="PRO_0000305297"
FT   REGION          23..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          77..128
FT                   /evidence="ECO:0000255"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   377 AA;  41908 MW;  0F76A1D1AB095B62 CRC64;
     MWSGPPQQDE GLPVGLSAIS VPWKNLGPSK GNRKSPGGLV EASASWEEAG GEEHPAAAPL
     DVSRLRSSSM EIREKGSEFL KEELYKAQKE LKLKDEECER LCKVRAQLEQ ELEELTASLF
     EEAHKMVREA NMKQAASEKQ LKEAWGKIDM LQAEVTALKT LVITSTPASP NRELHPQLLS
     PTKAGPRKGH SRQKSTSSLC PVVCPTAGHI PTPDKEGKEV DTTLFAEFQA WRASPTLDKN
     CPFLERVYRE DVGPCLDFTV QELSALVRTA VEDNTLTIEP VASQTLPNVE CNNTNTCALS
     GLARTCHHRI RLGDSDGHYY ISPSSRARIT AVCNFFTYVR YIQQGLVRQD AEPMFWEIMR
     LRKGMSLAKL GFFPQEA