RIM_CAEEL
ID RIM_CAEEL Reviewed; 1563 AA.
AC Q22366; Q22367; Q8MPX5; Q95WX9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Rab-3-interacting molecule unc-10;
DE Short=Rim;
DE AltName: Full=Uncoordinated protein 10;
GN Name=unc-10 {ECO:0000312|WormBase:T10A3.1a};
GN ORFNames=T10A3.1 {ECO:0000312|WormBase:T10A3.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11559854; DOI=10.1038/nn732;
RA Koushika S.P., Richmond J.E., Hadwiger G., Weimer R.M., Jorgensen E.M.,
RA Nonet M.L.;
RT "A post-docking role for active zone protein Rim.";
RL Nat. Neurosci. 4:997-1005(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=30460068; DOI=10.1080/19768354.2017.1325779;
RA Kim S.M., Hwang S.Y.;
RT "CFL-1, a novel F-box protein with leucine-rich repeat may interact with
RT UNC-10 for the regulation of defecation and daumone response in
RT Caenorhabditis elegans.";
RL Anim. Cells Syst. (Seoul) 21:185-189(2017).
CC -!- FUNCTION: Regulates the efficiency of a post-docking step of the
CC release pathway. Acts after vesicle docking likely via regulating
CC priming. May regulate the conformational changes in syntaxin. Binding
CC of vesicles via rab-3[GTP] to Rim may signal the presence of a docked
CC synaptic vesicle. Rim may then signal to unc-13 to change the
CC conformation of syntaxin from the closed to the open state. Syntaxin
CC could then engage synaptobrevin on the docked vesicle to form SNARE
CC complexes and to prime the vesicle for release. Not required for the
CC development or the structural organization of synapses. May play a role
CC in regulating entry into the dauer state (PubMed:30460068).
CC {ECO:0000269|PubMed:11559854, ECO:0000269|PubMed:30460068}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T10A3.1a};
CC IsoId=Q22366-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T10A3.1b};
CC IsoId=Q22366-2; Sequence=VSP_009139, VSP_009140, VSP_009141;
CC -!- TISSUE SPECIFICITY: Restricted to discrete puncta in synapse-rich
CC regions of the nervous system including the nerve ring, the ventral
CC nerve cord and the dorsal nerve cord. Localized expression was found in
CC the head. {ECO:0000269|PubMed:11559854}.
CC -!- DEVELOPMENTAL STAGE: Observed in all larval stages.
CC {ECO:0000269|PubMed:11559854}.
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DR EMBL; AF257062; AAK49331.1; -; mRNA.
DR EMBL; BX284606; CCD71364.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD71365.1; -; Genomic_DNA.
DR PIR; T29736; T29736.
DR RefSeq; NP_001024901.1; NM_001029730.3. [Q22366-2]
DR RefSeq; NP_741831.1; NM_171720.3. [Q22366-1]
DR AlphaFoldDB; Q22366; -.
DR SMR; Q22366; -.
DR BioGRID; 45915; 4.
DR IntAct; Q22366; 7.
DR MINT; Q22366; -.
DR STRING; 6239.T10A3.1a; -.
DR iPTMnet; Q22366; -.
DR EPD; Q22366; -.
DR PaxDb; Q22366; -.
DR PeptideAtlas; Q22366; -.
DR PRIDE; Q22366; -.
DR EnsemblMetazoa; T10A3.1a.1; T10A3.1a.1; WBGene00006750. [Q22366-1]
DR EnsemblMetazoa; T10A3.1b.1; T10A3.1b.1; WBGene00006750. [Q22366-2]
DR GeneID; 180990; -.
DR UCSC; T10A3.1b; c. elegans. [Q22366-1]
DR CTD; 180990; -.
DR WormBase; T10A3.1a; CE30169; WBGene00006750; unc-10. [Q22366-1]
DR WormBase; T10A3.1b; CE31234; WBGene00006750; unc-10. [Q22366-2]
DR eggNOG; KOG2060; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR eggNOG; KOG3799; Eukaryota.
DR GeneTree; ENSGT00940000168297; -.
DR HOGENOM; CLU_001061_3_1_1; -.
DR InParanoid; Q22366; -.
DR OMA; NATYEQV; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q22366; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR PRO; PR:Q22366; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006750; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q22366; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IDA:WormBase.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IDA:WormBase.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:1905909; P:regulation of dauer entry; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:WormBase.
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 2: Evidence at transcript level;
KW Alternative splicing; Exocytosis; Metal-binding; Reference proteome;
KW Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1563
FT /note="Rab-3-interacting molecule unc-10"
FT /id="PRO_0000190210"
FT DOMAIN 7..133
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 643..733
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 840..962
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1417..1536
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 66..121
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT VAR_SEQ 976..991
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009139"
FT VAR_SEQ 1386..1387
FT /note="WL -> AR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009140"
FT VAR_SEQ 1388..1563
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009141"
SQ SEQUENCE 1563 AA; 175479 MW; 77EE93619C24E899 CRC64;
MDDPSMMPDL SHLSAEEREI IENVFKRQKD EEAKETQISQ KASEELSELD KQITERKETS
KKLVGTQDDA ICQICQKTKF ADGIGHKCFY CQLRSCARCG GRAQSKNKAI WACSLCQKRQ
QILAKTGKWF QPEEQPQPKI SGSEPSPSPQ PLTDDNVPEP QQRRAEPPDK MNTPNYQNNQ
QPRGMGMQPN HNQTQQNFMN QNQNSNQHPN QNHNQNQMQN PHQNQNHVQN NHQGANNHQQ
NNRRAMQQQP MSQNQANQIN QMNQNQNQQQ SHNQNMTQNQ RNQTGPQNQQ RTNDSRTMKQ
TPQQQPSQYQ NNVGAAHQHH NQHGQQEQHH QQMNEQRTDN NRMRENTNGQ GGMFNRQPSL
EQTTPMNKYN HVEDDGMNQR PTFYTGNSEN DQRQFDGQMQ QGSQQNNQNQ NQNNRNLRKN
TVSRVTEEDY ASSSNFESKK QRNNSSQSQS NTQGVRACPS TDDHLNRVKN RLHRQLRSMS
SSEEDIIAGG GGNTLKMSTS AVVASGGKTA FHDDMGASNV QRLSEECNSE KDLLRYIYGD
HKNSDSSSLG AGVGGSGGGG VLSGNSVLKS KSHALLKGSY QGGLDMQANR RRDKSLSLSP
SRNDHFGTGS ISGGDLLASR IRTFLSHPVT WQPSADQKKL IGHMILHRTE NSAANGDLGL
KIVGGRRTDT GKLGAFITQV KPGSVADTIG RLRPGDEVVE WNGQSLQNAT YEQVYDSIAA
SRYDTSVELI VSRSAIIPGG DDFLNLTPSQ MSSSAYSRVP SAYPSQFQRQ LPNPDLFLDI
HPALQQLSLP HSQSAVFPHN NTLTSRNRST SSYYYSDVPD LGVPSNREMQ ESQAFGTGHI
FGRIEVSFVY SHHDRQLSVA LVRGFDLPPR SDGTPRNPYV KIFLLPDRSE KSRRQSAVIA
ETLMPVWDEV FYYNGLTEPM LLQRVLELTV WDYDKFGTNS FLGETLIDLA SVPLDGEHSL
MCILVDMDDD NPLRTVISIF KFHVIILTFL QRLKLRKASY NAPTRRPQSE LNYYDHSSNY
YDHISQNIDK QPHHHHLAPN DEENDEYIDD DELENDIDLA TGGGARKSRT YRREKGMHGG
HGYADWTQNH QRQSGYTSDH GYGRQNMIGR AYNRRQQRRP RSATALSQME REDMYDPTRK
HRDDNEYSMR ESVRHGSQYY LGDQPLYEDG RYKISQGQMT PKQHNQQHQP HPLSQAHQQQ
QTAGVQPQHH QGFQQQQHPQ QPNQQMQQMQ PPMPNQGYYS DGSETLSVHS TNSMPTTMTT
VNRRNMNANN TSNDNTSFAE TPTANTNRVP IKETKQNSLA SSSSVAGGGS AANNVMKERK
KSLMTRFIPG RGAEGKRTGF ARSEEVGIPG NLSSDRLTEP TPPFLKQASK ESTDSAHSDK
FARQCWLPVL ADGPLGTFVD NLGPGQVVGR QVLASPVLGE IQIALMAGRS GIDVEIIKAK
NLVVKPGVKV CPAPYVKVYL MEGKQCIAKA KTNAATKTTS PLFQQHLIFN DSPKKKTLQV
TVLGDYGRME RKVFMGISQI RLEDLELGSQ PLIGWYKLFH SSSLAGTGPV RKDSDVSVGG
AQQ
