CAPS_CAEEL
ID CAPS_CAEEL Reviewed; 1378 AA.
AC Q23658; C1P637; D3YT40; D3YT41; D3YT42; D3YT43;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 6.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calcium-dependent secretion activator;
DE AltName: Full=Uncoordinated protein 31;
GN Name=unc-31; ORFNames=ZK897.1;
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 [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).
RN [2]
RP PRELIMINARY FUNCTION.
RX PubMed=8325482; DOI=10.1093/genetics/134.2.455;
RA Avery L., Bargmann C.I., Horvitz H.R.;
RT "The Caenorhabditis elegans unc-31 gene affects multiple nervous system-
RT controlled functions.";
RL Genetics 134:455-464(1993).
RN [3]
RP PRELIMINARY FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10377425; DOI=10.1073/pnas.96.13.7394;
RA Ailion M., Inoue T., Weaver C.I., Holdcraft R.W., Thomas J.H.;
RT "Neurosecretory control of aging in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7394-7397(1999).
RN [4]
RP ERRATUM OF PUBMED:10377425.
RA Ailion M., Inoue T., Weaver C.I., Holdcraft R.W., Thomas J.H.;
RL Proc. Natl. Acad. Sci. U.S.A. 96:10944-10944(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16272411; DOI=10.1534/genetics.105.049577;
RA Charlie N.K., Schade M.A., Thomure A.M., Miller K.G.;
RT "Presynaptic UNC-31 (CAPS) is required to activate the G(alpha)s pathway of
RT the Caenorhabditis elegans synaptic signaling network.";
RL Genetics 172:943-961(2006).
RN [6]
RP FUNCTION.
RX PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA Liu T., Kim K., Li C., Barr M.M.;
RT "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT regulate male sexual turning behavior in Caenorhabditis elegans.";
RL J. Neurosci. 27:7174-7182(2007).
RN [7]
RP FUNCTION.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
RN [8]
RP FUNCTION.
RX PubMed=18316030; DOI=10.1016/j.cmet.2008.01.005;
RA You Y.J., Kim J., Raizen D.M., Avery L.;
RT "Insulin, cGMP, and TGF-beta signals regulate food intake and quiescence in
RT C. elegans: a model for satiety.";
RL Cell Metab. 7:249-257(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22124329; DOI=10.1038/emboj.2011.422;
RA Mills H., Wragg R., Hapiak V., Castelletto M., Zahratka J., Harris G.,
RA Summers P., Korchnak A., Law W., Bamber B., Komuniecki R.;
RT "Monoamines and neuropeptides interact to inhibit aversive behaviour in
RT Caenorhabditis elegans.";
RL EMBO J. 31:667-678(2012).
CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles
CC filled with neurotransmitters and neuropeptides. Probably acts upstream
CC of fusion in the biogenesis or maintenance of mature secretory
CC vesicles. May specifically mediate the Ca(2+)-dependent exocytosis of
CC large dense-core vesicles (DCVs) and other dense-core vesicles (By
CC similarity). Specifically required to activate the neuronal G-alpha
CC pathway. Functions with G-alpha proteins from the same motor neurons to
CC regulate locomotion (PubMed:16272411). Involved in regulating entry
CC into quiescence triggered by satiety (PubMed:18316030). Probably by
CC regulating neuronal transmission downstream of lin-3 and receptor lin-
CC 23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG
CC in ALA neurons, involved in the decrease in pharyngeal pumping during
CC the quiescent state that precedes each larval molt (PubMed:17891142).
CC Plays a role in octopamine signaling and specifically, the octopamine
CC inhibition of aversion responses in olfactory sensory neurons
CC (PubMed:22124329). Probably by controlling the secretion of FLP
CC neuropeptides, regulates the turning step of male mating behavior
CC (PubMed:17611271). {ECO:0000250|UniProtKB:Q62717,
CC ECO:0000269|PubMed:16272411, ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:17891142, ECO:0000269|PubMed:18316030,
CC ECO:0000269|PubMed:22124329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}.
CC Synapse {ECO:0000250}. Note=Membrane-associated to vesicles (By
CC similarity). Strongly enriched in synaptic fractions. Often
CC concentrated at or near active zones of motor neuron synapses.
CC {ECO:0000250, ECO:0000269|PubMed:16272411}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=c;
CC IsoId=Q23658-3; Sequence=Displayed;
CC Name=a;
CC IsoId=Q23658-1; Sequence=VSP_039776, VSP_039777;
CC Name=b;
CC IsoId=Q23658-2; Sequence=VSP_039777;
CC Name=d;
CC IsoId=Q23658-4; Sequence=VSP_039775, VSP_039777;
CC Name=e;
CC IsoId=Q23658-5; Sequence=VSP_039775;
CC Name=f;
CC IsoId=Q23658-6; Sequence=VSP_039774;
CC -!- TISSUE SPECIFICITY: Within the ventral, dorsal and sublateral nerve
CC cords, it is concentrated in cholinergic synapses. Within the ventral
CC and dorsal nerve cords, it is not concentrated at most non-cholinergic
CC synapses in the nerve cords, such as the GABAergic, glutamatergic, and
CC catecholaminergic synapses. However, within the nerve ring, which
CC contains a large number of interneuronal synapses in the head, it is
CC clearly concentrated in regions containing large numbers of non-
CC cholinergic synapses. {ECO:0000269|PubMed:16272411}.
CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC phospholipids. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms display increased adult life span and
CC constitutive dauer formation (PubMed:10377425). RNAi-mediated knockdown
CC in ADL sensory neurons results in reduced octopamine inhibition of the
CC aversive response when animals are exposed to 100% 1-octanol
CC (PubMed:22124329). {ECO:0000269|PubMed:10377425,
CC ECO:0000269|PubMed:22124329}.
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DR EMBL; Z69665; CAA93520.6; -; Genomic_DNA.
DR EMBL; Z69665; CAX65097.2; -; Genomic_DNA.
DR EMBL; Z69665; CBK19526.1; -; Genomic_DNA.
DR EMBL; Z69665; CBK19527.1; -; Genomic_DNA.
DR EMBL; Z69665; CBK19528.1; -; Genomic_DNA.
DR EMBL; Z69665; CBK19529.1; -; Genomic_DNA.
DR PIR; H88869; H88869.
DR PIR; T28087; T28087.
DR RefSeq; NP_001255664.1; NM_001268735.1. [Q23658-3]
DR RefSeq; NP_001255666.1; NM_001268737.1. [Q23658-1]
DR RefSeq; NP_001255667.1; NM_001268738.1. [Q23658-2]
DR RefSeq; NP_001255668.1; NM_001268739.1. [Q23658-5]
DR RefSeq; NP_001255669.1; NM_001268740.1. [Q23658-4]
DR RefSeq; NP_001255671.1; NM_001268742.1. [Q23658-6]
DR AlphaFoldDB; Q23658; -.
DR SMR; Q23658; -.
DR STRING; 6239.ZK897.1i; -.
DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR EPD; Q23658; -.
DR PaxDb; Q23658; -.
DR PeptideAtlas; Q23658; -.
DR EnsemblMetazoa; ZK897.1a.1; ZK897.1a.1; WBGene00006767. [Q23658-1]
DR EnsemblMetazoa; ZK897.1b.1; ZK897.1b.1; WBGene00006767. [Q23658-2]
DR EnsemblMetazoa; ZK897.1c.1; ZK897.1c.1; WBGene00006767. [Q23658-3]
DR EnsemblMetazoa; ZK897.1d.1; ZK897.1d.1; WBGene00006767. [Q23658-4]
DR EnsemblMetazoa; ZK897.1e.1; ZK897.1e.1; WBGene00006767. [Q23658-5]
DR EnsemblMetazoa; ZK897.1f.1; ZK897.1f.1; WBGene00006767. [Q23658-6]
DR GeneID; 178233; -.
DR UCSC; ZK897.1; c. elegans. [Q23658-3]
DR CTD; 178233; -.
DR WormBase; ZK897.1a; CE44675; WBGene00006767; unc-31. [Q23658-1]
DR WormBase; ZK897.1b; CE44637; WBGene00006767; unc-31. [Q23658-2]
DR WormBase; ZK897.1c; CE44563; WBGene00006767; unc-31. [Q23658-3]
DR WormBase; ZK897.1d; CE44694; WBGene00006767; unc-31. [Q23658-4]
DR WormBase; ZK897.1e; CE44651; WBGene00006767; unc-31. [Q23658-5]
DR WormBase; ZK897.1f; CE44601; WBGene00006767; unc-31. [Q23658-6]
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00590000083094; -.
DR InParanoid; Q23658; -.
DR PhylomeDB; Q23658; -.
DR PRO; PR:Q23658; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006767; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q23658; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031045; C:dense core granule; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:WormBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:WormBase.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:1902075; P:cellular response to salt; IMP:UniProtKB.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:1990504; P:dense core granule exocytosis; IMP:WormBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:1903745; P:negative regulation of pharyngeal pumping; IMP:UniProtKB.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IGI:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR GO; GO:0001820; P:serotonin secretion; IMP:WormBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro.
DR GO; GO:0007419; P:ventral cord development; IGI:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR033227; CAPS.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12166; PTHR12166; 1.
DR Pfam; PF06292; MUN; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasmic vesicle;
KW Exocytosis; Lipid-binding; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..1378
FT /note="Calcium-dependent secretion activator"
FT /id="PRO_0000053871"
FT DOMAIN 430..547
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 569..675
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 964..1095
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..184
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1361
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_039774"
FT VAR_SEQ 1..448
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_039775"
FT VAR_SEQ 78
FT /note="S -> SPMRMNAPSPMPQ (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_039776"
FT VAR_SEQ 1337..1378
FT /note="AAINGSAQGSVFPTSLGNATAAVSNMSSMVEGAGAKMFSLFK -> GIRKH
FT (in isoform a, isoform b and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_039777"
SQ SEQUENCE 1378 AA; 156188 MW; 3FDC1CDED2BD3AE7 CRC64;
MLGASSSEEE DDDFQEDHDS LPIAQVKKRS LLSGAMTPRS SSPAPSDSVS QTNSLKRNNS
SSQGRRKDSV QSQTPARSAR IMSNVSKPIM QNSQEFDGDE EEGEEGSTTV VGSGDECGGP
ALSKEEQERM KAEREEEDHK KNLQMYMFLA RCIAYPFNGQ QTGDMARRQM KVNKQELARI
RERFTLFLKG ETNIAADEAF TKAIQSYFEV FLKSERVQKV VHAGGFSQHD FREVFRLNIE
KRVRSLPDIE GLSKDTVLNS WLAKFDAIIK GDETDQNRNA RGRSRNPQNA MSADAVLGKE
QLYDVFQQIL GVKKFEHQII FNALQLDNPD EQAAAIRREF ATREEALKDP IKMKRLTPKF
VVKDMETLYM DEVRMSINTL IGNLETVPVT TRGATVGKRK DKSRSRSIED LSLFNSLKRR
TSSGSLNKGD SEDGDVTLTK SDVSLALSME VVVMEVQGLK SVQPSKIVYC TMEVDGHKLQ
TDHAEASKPK WDTQGDFSTK NPLPVVKVKL YTEVKSMIAF EDKELGKVII QPTPNCARSP
EWYTMTLPKS SQDQNLKIRI AIRVEKPPNL KYCGYCYCIG RNAWKKWKKR FFCLVQVSQY
AFAVCSFRQK KADPTEFIQL DGFTIDYMPE SDPELSAQGG KHFFTAIKEG DELKFATDDE
NERHLWVQAL YRATGQAYKP VPPKQSTIAP KAQGFQDKAS KHGMDAMIQA DSINFDHDHF
YSDVQRLTLD FRINEPICSL GWFSPGQAFV LEEYSARYMV RGCFRHVTLL SNLLDKADDG
LLIDPALIHY SFAFCASHVH GNRCMPDRQG PEGVGTVTLE EKEKFQEIKE RLRVLLEKQI
TNFRYCFPFG RPEGALKGTL GLLERVLMKD VVSPVPPEEV RAVIRKCLED AALVNYTRIC
NEAKIEQRMG IDVSPAQRIE DMIRVTEFCI DLLKENEEHH GEAFAWFSDL LSDHSEIFWS
LYSVDLDSAL EVQPHDSWDS FPLFQMLNDF LLSESSLKGG IFHNKIVQQF QPLVVRYIDL
MEHSIAQAID KGFSKEKWES RKEGCATSED IYWKLDALHT FVIDLNWPEE DFRKYLQTKM
KSLTSDMISK VSDCTFTAFD SWMQRAKKST DYMLPSEVCV QINVMFSSKS RAVRVTVDSG
EYKYQSKLDE TLETMLKTME SCIQEKLHGV LESVLSRLAR YDEGNPIGAI LNIAPKPASI
FNKLKTMAGD TSAQATTTAR QPLTAQQSSG QIGNSYVTFF HGCTELLRQV IIDEIWVNGL
FEHWYDNQMK SINEWLTERL QQSLSATQYI SLSTIVKKVY QDFSLQGIDE ERLNSKTYQS
ISRRLQLEES NSHIQEAAIN GSAQGSVFPT SLGNATAAVS NMSSMVEGAG AKMFSLFK
