RIMS1_MOUSE
ID RIMS1_MOUSE Reviewed; 1463 AA.
AC Q99NE5; Q5DU35; Q5J8K0; Q5J8K1; Q5J8K2; Q5J8K3; Q5J8K4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 1;
DE AltName: Full=Rab-3-interacting molecule 1;
DE Short=RIM 1;
DE AltName: Full=Rab-3-interacting protein 1;
GN Name=Rims1; Synonyms=Kiaa0340, Rab3ip1, Rim1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, MUTAGENESIS
RP OF ARG-33, AND INTERACTION WITH RAB3A; RAB3B AND RAB3D.
RC TISSUE=Brain;
RX PubMed=11431472; DOI=10.1074/jbc.m103337200;
RA Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially
RT related through N-terminal alpha-helix motifs.";
RL J. Biol. Chem. 276:32480-32488(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5 AND 6).
RA Wang X., Hu B., Kilimann M.W.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-1463 (ISOFORM 7).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RX PubMed=11797009; DOI=10.1038/415321a;
RA Schoch S., Castillo P.E., Jo T., Mukherjee K., Geppert M., Wang Y.,
RA Schmitz F., Malenka R.C., Suedhof T.C.;
RT "RIM1alpha forms a protein scaffold for regulating neurotransmitter release
RT at the active zone.";
RL Nature 415:321-326(2002).
RN [5]
RP INTERACTION WITH RAB3A; RAB3B; RAB3C; RAB3D; RAB10; RAB26 AND RAB37.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; SER-566; SER-716;
RP SER-866; SER-1023; SER-1027; SER-1110; SER-1111; SER-1113; SER-1448 AND
RP SER-1451, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 (ISOFORM 7),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Rab effector involved in exocytosis (PubMed:11797009). May
CC act as scaffold protein that regulates neurotransmitter release at the
CC active zone. Essential for maintaining normal probability of
CC neurotransmitter release and for regulating release during short-term
CC synaptic plasticity (PubMed:11797009). Plays a role in dendrite
CC formation by melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q86UR5, ECO:0000269|PubMed:11797009}.
CC -!- SUBUNIT: Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is
CC enhanced by calcium ions. Interaction with SNAP25 is weaker in the
CC presence of calcium ions. Interacts with TSPOAP1 and RIMBP2; interacts
CC with PPFIA3 and PPFIA4. Interacts with ERC1 (By similarity). Interacts
CC with RAB3A, RAB3B and RAB3D that have been activated by GTP-binding.
CC Interacts with RAB3C, RAB10, RAB26 AND RAB37. Binds UNC13A.
CC {ECO:0000250, ECO:0000269|PubMed:11431472,
CC ECO:0000269|PubMed:12578829}.
CC -!- INTERACTION:
CC Q99NE5; Q9CZV8: Fbxl20; NbExp=4; IntAct=EBI-775541, EBI-1551033;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q99NE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99NE5-2; Sequence=VSP_022231, VSP_022232;
CC Name=3;
CC IsoId=Q99NE5-3; Sequence=VSP_022235;
CC Name=4;
CC IsoId=Q99NE5-4; Sequence=VSP_022235, VSP_022236;
CC Name=5;
CC IsoId=Q99NE5-5; Sequence=VSP_022234;
CC Name=6;
CC IsoId=Q99NE5-6; Sequence=VSP_022233;
CC Name=7;
CC IsoId=Q99NE5-7; Sequence=VSP_022230, VSP_022233, VSP_022237,
CC VSP_022238;
CC -!- PTM: Phosphorylated by BRSK1. {ECO:0000250}.
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DR EMBL; AJ310531; CAC32041.1; -; mRNA.
DR EMBL; AY356534; AAR14797.1; -; mRNA.
DR EMBL; AY356535; AAR14798.1; -; mRNA.
DR EMBL; AY356536; AAR14799.1; -; mRNA.
DR EMBL; AY356537; AAR14800.1; -; mRNA.
DR EMBL; AY356538; AAR14801.1; -; mRNA.
DR EMBL; AK220335; BAD90402.1; -; mRNA.
DR RefSeq; NP_001012641.1; NM_001012623.1.
DR RefSeq; NP_001012642.1; NM_001012624.1.
DR RefSeq; NP_001012643.1; NM_001012625.1.
DR RefSeq; NP_444500.1; NM_053270.1.
DR RefSeq; NP_898839.2; NM_183018.2.
DR AlphaFoldDB; Q99NE5; -.
DR SMR; Q99NE5; -.
DR BioGRID; 228025; 12.
DR IntAct; Q99NE5; 4.
DR MINT; Q99NE5; -.
DR STRING; 10090.ENSMUSP00000095420; -.
DR iPTMnet; Q99NE5; -.
DR PhosphoSitePlus; Q99NE5; -.
DR MaxQB; Q99NE5; -.
DR PeptideAtlas; Q99NE5; -.
DR PRIDE; Q99NE5; -.
DR ProteomicsDB; 255141; -. [Q99NE5-1]
DR ProteomicsDB; 255142; -. [Q99NE5-2]
DR ProteomicsDB; 255143; -. [Q99NE5-3]
DR ProteomicsDB; 255144; -. [Q99NE5-4]
DR ProteomicsDB; 255145; -. [Q99NE5-5]
DR ProteomicsDB; 255146; -. [Q99NE5-6]
DR ProteomicsDB; 255147; -. [Q99NE5-7]
DR DNASU; 116837; -.
DR GeneID; 116837; -.
DR KEGG; mmu:116837; -.
DR UCSC; uc029qni.1; mouse. [Q99NE5-1]
DR UCSC; uc029qnj.1; mouse. [Q99NE5-3]
DR UCSC; uc029qnk.1; mouse. [Q99NE5-4]
DR UCSC; uc029qnm.1; mouse. [Q99NE5-6]
DR CTD; 22999; -.
DR MGI; MGI:2152971; Rims1.
DR eggNOG; KOG2060; Eukaryota.
DR InParanoid; Q99NE5; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q99NE5; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 116837; 4 hits in 20 CRISPR screens.
DR ChiTaRS; Rims1; mouse.
DR PRO; PR:Q99NE5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99NE5; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IMP:SynGO-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:MGI.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:MGI.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0010808; P:positive regulation of synaptic vesicle priming; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IGI:ParkinsonsUK-UCL.
DR GO; GO:0016081; P:synaptic vesicle docking; IDA:SynGO.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; PTHR12157; 2.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Differentiation;
KW Exocytosis; Membrane; Metal-binding; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..1463
FT /note="Regulating synaptic membrane exocytosis protein 1"
FT /id="PRO_0000190199"
FT DOMAIN 22..205
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 440..526
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 577..700
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1309..1427
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 133..193
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1025
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR4"
FT MOD_RES 1448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UR5"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UR5"
FT VAR_SEQ 369
FT /note="K -> KEEEYQTRYRSDPNLARYPVKAPLEEQQMRMHARVSRARHERRHSDV
FT ALPHTEAAAAVSAETTAGKRAQTTARVSPPESPRARAPAAQPPAEHGPPPPRPAPGPAE
FT PPEPRVPEPLRKQGRLDPGSAVLLRKAKREKAESMLRNDSLSSDQSESVRPSPPKPHRP
FT KRGGKRRQMSVSSS (in isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_022230"
FT VAR_SEQ 373..388
FT /note="GVSTPEYTSCEDVELE -> YQTRYRSDPNLARYPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11431472"
FT /id="VSP_022231"
FT VAR_SEQ 389..1463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11431472"
FT /id="VSP_022232"
FT VAR_SEQ 853..1016
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_022233"
FT VAR_SEQ 904..1016
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022234"
FT VAR_SEQ 904..931
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022235"
FT VAR_SEQ 956..1016
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022236"
FT VAR_SEQ 1150..1170
FT /note="FTPKMQGRRMGTSGRAIIKST -> LTLVLLMMALPYKFVQKSRLF (in
FT isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_022237"
FT VAR_SEQ 1171..1463
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_022238"
FT MUTAGEN 33
FT /note="R->G: Abolishes interaction with RAB3A."
FT /evidence="ECO:0000269|PubMed:11431472"
FT MOD_RES Q99NE5-7:413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1463 AA; 163161 MW; 1E0BE5D522924738 CRC64;
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MAKPAACKTP RNAESQPHQP PLNIFRCVCV PRKPSSEEGG PDRNWRLHQQ FESYKEQVRK
IGEEARRYQG EHKDDAPTCG ICHKTKFADG CGHLCSYCRT KFCARCGGRV SLRSNNEDKV
VMWVCNLCRK QQEILTKSGA WFFGSGPQQP SQDGTLSDTA TGAGSEVPRE KKARLQERSR
SQTPLSTAAV SSQDTASHGA PLDRNKGAEP SQQALGPEQK QASRSRSEPP RERKKAPGLS
EQNGKGGQKS ERKRVPKSVV QPGEGTADER ERKERRETRR LEKGRSQDYP DRLEKREDGR
VAEDEKQRKE EEGVSTPEYT SCEDVELESE SVSEKGDLDY WLDPATWHSR ETSPISSHPV
TWQPSKEGDR LIGRVILNKR TTMPKESGAL LGLKVVGGKM TDLGRLGAFI TKVKKGSLAD
VVGHLRAGDE VLEWNGKPLP GATNEEVYNI ILESKSEPQV EIIVSRPIGD IPRIPESSHP
PLESSSSSFE SQKMERPSIS VISPTSPGAL KDAPQVLPGQ LSVKLWYDKV GHQLIVNVLQ
ATDLPPRVDG RPRNPYVKMY FLPDRSDKSK RRTKTVKKLL EPKWNQTFVY SHVHRRDFRE
RMLEITVWDQ PRVQDEESEF LGEILIELET ALLDDEPHWY KLQTHDESSL PLPQPSPFMP
RRHIHGESSS KKLQRSQRIS DSDISDYEVD DGIGVVPPVG YRASARESKA TTLTVPEQQR
TTHHRSRSVS PHRGDDQGRP RSRLPNVPLQ RSLDEIHPTR RSRSPTRHHD ASRSLADHRS
RHAESQYSSE PDSELLMLPR AKRGRSAECL HMTSELQPSL DRARSASTNC LRPDTSLHSP
ERERGRWSPS LARRRPASPR IQIQHASPEN DRHSRKSERS SIQKQSRKGT ASDADRVLPP
CLSRRGYAIP RATDQPVIRG KHTTRSRSSE HSSIRTLCSM HHLAPGGSAP PSPLLTRTHR
QGSPTQSPPA DTSFGSRRGR QLPQVPVRSG SIEQASLVVE ERTRQMKMKV HRFKQTTGSG
SSQELDHEQY SKYNIHKDQY RSCDNASAKS SDSDVSDVSA ISRASSTSRL SSTSFMSEQS
ERPRGRISSF TPKMQGRRMG TSGRAIIKST SVSGEIYTLE HNDGSQSDTA VGTVGAGGKK
RRSSLSAKVV AIVSRRSRST SQLSQTESGH KKLKSTIQRS TETGMAAEMR KMVRQPSRES
TDGSINSYSS EGNLIFPGVR VGPDSQFSDF LDGLGPAQLV GRQTLATPAM GDIQIGMEDK
KGQLEVEVIR ARSLTQKPGS KSTPAPYVKV YLLENGACIA KKKTRIARKT LDPLYQQSLV
FDESPQGKVL QVIVWGDYGR MDHKCFMGVA QILLEELDLS SMVIGWYKLF PPSSLVDPTL
TPLTRRASQS SLESSSGPPC IRS
