RBF1_CAEEL
ID RBF1_CAEEL Reviewed; 1106 AA.
AC P41885; Q8MQ57; Q8WT49; Q8WT50; Q962V6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rabphilin-1;
GN Name=rbf-1; ORFNames=F37A4.7;
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), AND FUNCTION.
RX PubMed=11717359; DOI=10.1523/jneurosci.21-23-09255.2001;
RA Staunton J., Ganetzky B., Nonet M.L.;
RT "Rabphilin potentiates soluble N-ethylmaleimide sensitive factor attachment
RT protein receptor function independently of rab3.";
RL J. Neurosci. 21:9255-9264(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Rab-3 effector. {ECO:0000269|PubMed:11717359}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=d;
CC IsoId=P41885-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P41885-2; Sequence=VSP_011908;
CC Name=b;
CC IsoId=P41885-3; Sequence=VSP_011906;
CC Name=c;
CC IsoId=P41885-4; Sequence=VSP_011907;
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DR EMBL; AF399852; AAK84870.1; -; mRNA.
DR EMBL; FO081312; CCD70705.1; -; Genomic_DNA.
DR EMBL; FO081312; CCD70706.1; -; Genomic_DNA.
DR EMBL; FO081312; CCD70707.1; -; Genomic_DNA.
DR EMBL; FO081312; CCD70708.1; -; Genomic_DNA.
DR PIR; S44644; S44644.
DR RefSeq; NP_001022566.1; NM_001027395.3. [P41885-3]
DR RefSeq; NP_001022567.1; NM_001027396.3. [P41885-4]
DR RefSeq; NP_001022568.1; NM_001027397.2.
DR RefSeq; NP_498467.3; NM_066066.5. [P41885-2]
DR AlphaFoldDB; P41885; -.
DR SMR; P41885; -.
DR BioGRID; 41159; 1.
DR IntAct; P41885; 1.
DR STRING; 6239.F37A4.7d; -.
DR iPTMnet; P41885; -.
DR EPD; P41885; -.
DR PaxDb; P41885; -.
DR PeptideAtlas; P41885; -.
DR PRIDE; P41885; -.
DR EnsemblMetazoa; F37A4.7a.1; F37A4.7a.1; WBGene00004316. [P41885-2]
DR EnsemblMetazoa; F37A4.7a.2; F37A4.7a.2; WBGene00004316. [P41885-2]
DR EnsemblMetazoa; F37A4.7a.3; F37A4.7a.3; WBGene00004316. [P41885-2]
DR EnsemblMetazoa; F37A4.7b.1; F37A4.7b.1; WBGene00004316. [P41885-3]
DR EnsemblMetazoa; F37A4.7c.1; F37A4.7c.1; WBGene00004316. [P41885-4]
DR EnsemblMetazoa; F37A4.7d.1; F37A4.7d.1; WBGene00004316.
DR GeneID; 175943; -.
DR UCSC; F37A4.7d; c. elegans. [P41885-1]
DR CTD; 175943; -.
DR WormBase; F37A4.7a; CE29961; WBGene00004316; rbf-1. [P41885-2]
DR WormBase; F37A4.7b; CE29962; WBGene00004316; rbf-1. [P41885-3]
DR WormBase; F37A4.7c; CE29963; WBGene00004316; rbf-1. [P41885-4]
DR WormBase; F37A4.7d; CE30975; WBGene00004316; rbf-1. [P41885-1]
DR eggNOG; KOG1013; Eukaryota.
DR InParanoid; P41885; -.
DR OMA; TREIWLC; -.
DR OrthoDB; 374694at2759; -.
DR PRO; PR:P41885; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004316; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:1990504; P:dense core granule exocytosis; IMP:WormBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IBA:GO_Central.
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; IPR010911; Rab_BD.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR030541; RBF-1.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF6; PTHR45729:SF6; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Exocytosis; Metal-binding;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1106
FT /note="Rabphilin-1"
FT /id="PRO_0000190231"
FT DOMAIN 198..324
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 827..950
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 967..1086
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 246..311
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 858
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 858
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 919
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 919
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 921
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 921
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 926
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 998
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 998
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1004
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1058
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1058
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1060
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1060
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1066
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:11717359"
FT /id="VSP_011908"
FT VAR_SEQ 1..152
FT /note="MTKSTKLRHCKQKKKKPEKTPKGNPPILITEKSIEDAATTTSTTDALLGSPE
FT GSRSKSRKLKLCCCTAQAATLSPLDPTSYGGIASTSAHNGMVGGLSRDSRAASRTSKRG
FT SSKSLNRPQIDADEPSTSGTNPDRRPSTHFVLDLPVVSTRY -> MFSRRTTPSPSITT
FT ASSSTFSISNLTNNNATSTSDLPASAISNIVPQIPPTPRRVPPKIGLLRHLSGFLESKK
FT D (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011906"
FT VAR_SEQ 1..152
FT /note="MTKSTKLRHCKQKKKKPEKTPKGNPPILITEKSIEDAATTTSTTDALLGSPE
FT GSRSKSRKLKLCCCTAQAATLSPLDPTSYGGIASTSAHNGMVGGLSRDSRAASRTSKRG
FT SSKSLNRPQIDADEPSTSGTNPDRRPSTHFVLDLPVVSTRY -> MYMNREDH (in
FT isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_011907"
SQ SEQUENCE 1106 AA; 120632 MW; 34F1C9D9E3AF495F CRC64;
MTKSTKLRHC KQKKKKPEKT PKGNPPILIT EKSIEDAATT TSTTDALLGS PEGSRSKSRK
LKLCCCTAQA ATLSPLDPTS YGGIASTSAH NGMVGGLSRD SRAASRTSKR GSSKSLNRPQ
IDADEPSTSG TNPDRRPSTH FVLDLPVVST RYLMNDWEIG GTQNKWVCPS DRHLHLRAQL
KSGWSVRTAT ARSPTNSKAQ TGSITAAEQE HIQKVLAKAE ESKSKEQQRI GKMVDRLEKM
RRRATGNGVT HCLLCHTEFG LLASKSYAAM CVDCRKYVCQ RNCGVETTDV NQTTGKVETV
FLCKICSEAR EVLWKKSGAW FYKEMPEFQR PDDRLPYYVP VTTNGTLPNA SSAATPLSGT
PGGAGPQPMT MPSTSSCQMT TPKWASPGVC NSPGLQMNGG PTSPLPNGTR RNTGHGGIEF
PSSSRPSICS VLQAIEPLDR SKSPRPRIQP RWVNEKVMSS MSVDDEEKAA SSSDGESFVQ
SGVPRRALNN KTPVGSTSAT TSPAPPPTST TPTSRREANM ERFSRHTHAH ANRLYSTDDD
DDSSPESRPS TRSTSPRHSL ATPSSYAHDT CHDTSLPDAD TRSIDSGVVQ SDHSNPQQSG
LTCSSSSLTP LQQQASHDHH SGGGTPRRIS NPDRTTSRVA QSASGTSLVT PPPPISSRTS
PDNCNSSPLN VMEHKSSSAS TASSGGNRRV GSAEPVLNNH HAMHNNQNHN DINKKLISQT
SRAESPLAAS SSFLSSPDDD TKQKNRRRDG VGRVNSLQLR TSLDDVAPPV APISKMNGHI
VSSEPTSSTT SNQNHTSVPI PTVPVVPEEE EEKAITASTE SASEPGSLGS ITLTLTYHSA
DKKLKMHLIR AKNLKAMDSN GFSDPYVKFH LLPGNTKATK LTSKTIEKTL NPEWNEEMSY
YGITEDDKEK KILRVTVLDR DRIGSDFLGE TRIALKKLND NEMKKFNLYL ESALPVPQQT
KEEENEDRGK INVGLQYNIQ QGSLFININR CVELVGMDST GFSDPYCKVS LTPITSKAHR
AKTSTKKRTL NPEWNEQLQF VVPFKDLPKK TLQIGVYDHD LGKHDDYIGG ILLSTSAKDE
RGRQWIKCIE NPGTLVEAWH RLELDS
