ID   RIMS3_RAT               Reviewed;         307 AA.
AC   Q9JIR3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Regulating synaptic membrane exocytosis protein 3;
DE            Short=Nim3;
DE   AltName: Full=RIM3 gamma;
DE   AltName: Full=Rab-3-interacting molecule 3;
DE            Short=RIM 3;
GN   Name=Rims3; Synonyms=Nim3;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=10748113; DOI=10.1074/jbc.m909008199;
RA   Wang Y., Sugita S., Suedhof T.C.;
RT   "The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3
RT   and a new class of Src homology 3 domain proteins.";
RL   J. Biol. Chem. 275:20033-20044(2000).
RN   [2]
RP   INTERACTION WITH PPFIA3, AND TISSUE SPECIFICITY.
RX   PubMed=12620390; DOI=10.1016/s0888-7543(02)00024-1;
RA   Wang Y., Suedhof T.C.;
RT   "Genomic definition of RIM proteins: evolutionary amplification of a family
RT   of synaptic regulatory proteins.";
RL   Genomics 81:126-137(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, AND IDENTIFICATION BY
RP   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: Regulates synaptic membrane exocytosis.
CC       {ECO:0000269|PubMed:10748113}.
CC   -!- SUBUNIT: Binds PPFIA3. Does not bind RAB3.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in brain with significant
CC       levels in cortex, cerebellum and olfactory bulb. Detected at lower
CC       level in hippocampus. {ECO:0000269|PubMed:10748113,
CC       ECO:0000269|PubMed:12620390}.
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DR   EMBL; AF199334; AAF81656.1; -; mRNA.
DR   RefSeq; NP_075220.1; NM_022931.1.
DR   AlphaFoldDB; Q9JIR3; -.
DR   SMR; Q9JIR3; -.
DR   STRING; 10116.ENSRNOP00000015034; -.
DR   iPTMnet; Q9JIR3; -.
DR   PhosphoSitePlus; Q9JIR3; -.
DR   PaxDb; Q9JIR3; -.
DR   PRIDE; Q9JIR3; -.
DR   GeneID; 65025; -.
DR   KEGG; rno:65025; -.
DR   CTD; 9783; -.
DR   RGD; 628762; Rims3.
DR   eggNOG; KOG2060; Eukaryota.
DR   InParanoid; Q9JIR3; -.
DR   OrthoDB; 109268at2759; -.
DR   PhylomeDB; Q9JIR3; -.
DR   PRO; PR:Q9JIR3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR   GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:RGD.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:MGI.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR039032; Rim-like.
DR   PANTHER; PTHR12157; PTHR12157; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   Exocytosis; Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW   Synapse; Transport.
FT   CHAIN           1..307
FT                   /note="Regulating synaptic membrane exocytosis protein 3"
FT                   /id="PRO_0000190206"
FT   DOMAIN          155..273
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          86..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80U57"
SQ   SEQUENCE   307 AA;  32651 MW;  77E9D14F6A41C71A CRC64;
     MFNGEPGPAS AGASRNVVRS SSISGEICGS QQAGGGAGTT TAKKRRSSLG AKMVAIVGLT
     QWSKSTLQLP QPEGATKKLR SNIRRSTETG IAVEMRSRVT RQGSRESTDG STNSNSSEGT
     FIFPTRLGAE SQFSDFLDGL GPAQIVGRQT LATPPMGDVH IAIMDRSGQL EVEVIEARGL
     TPKPGSKSLP ATYIKAYLLE NGACVAKKKT KVAKKTCDPL YQQALLFDEG PQGKVLQVIV
     WGDYGRMDHK CFMGMAQIML DELDLSAVVT GWYKFFPTSS VADSTLGSLT RRLSQSSLES
     ATSPSCS