ID   CAPS_CAEBR              Reviewed;        1354 AA.
AC   Q60PC0; A8Y216;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Calcium-dependent secretion activator;
DE   AltName: Full=Uncoordinated protein 31;
GN   Name=unc-31; ORFNames=CBG22310;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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.
CC       Specifically required to activate the neuronal G-alpha pathway.
CC       Functions with G-alpha proteins from the same motor neurons to regulate
CC       locomotion. Involved in regulating entry into quiescence triggered by
CC       satiety. Probably by regulating neuronal transmission downstream of
CC       lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of
CC       innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in
CC       pharyngeal pumping during the quiescent state that precedes each larval
CC       molt. Plays a role in octopamine signaling and specifically, the
CC       octopamine inhibition of aversion responses in olfactory sensory
CC       neurons. Probably by controlling the secretion of FLP neuropeptides,
CC       regulates the turning step of male mating behavior.
CC       {ECO:0000250|UniProtKB:Q23658, ECO:0000250|UniProtKB:Q62717}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}.
CC       Synapse {ECO:0000250}. Note=Membrane-associated to vesicles. Strongly
CC       enriched in synaptic fractions. {ECO:0000250}.
CC   -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC       phospholipids. {ECO:0000250}.
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DR   EMBL; HE601241; CAP38936.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q60PC0; -.
DR   SMR; Q60PC0; -.
DR   STRING; 6238.CBG22310; -.
DR   PRIDE; Q60PC0; -.
DR   WormBase; CBG22310a; CBP40444; WBGene00040906; Cbr-unc-31.
DR   eggNOG; KOG3543; Eukaryota.
DR   HOGENOM; CLU_007068_0_0_1; -.
DR   InParanoid; Q60PC0; -.
DR   OMA; RWEIKGN; -.
DR   OrthoDB; 138870at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro.
DR   Gene3D; 2.30.29.30; -; 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   3: Inferred from homology;
KW   Calcium; Cytoplasmic vesicle; Exocytosis; Lipid-binding; Membrane;
KW   Metal-binding; Protein transport; Reference proteome; Synapse; Transport.
FT   CHAIN           1..1354
FT                   /note="Calcium-dependent secretion activator"
FT                   /id="PRO_0000053870"
FT   DOMAIN          441..558
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          580..686
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          975..1106
FT                   /note="MHD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT   REGION          1..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1354 AA;  154108 MW;  2F279BE33DC3C157 CRC64;
     MLGASSSEEE DDDFQDDHES QLPIAQVKKR SLLSGAMTPR SSSPAPSDSV SQTNSLKRNN
     SSSQARRKDS VHSQTPARSP MKMNSPSPMP QARTMSNVTR PVLQNSQELD GEEIEETEGS
     GTMVASDDGG PSLSKEEQER IKAEKEEEEH KKNLQMYVFI ARCVAYPFNG QQTGDMARRQ
     MKVNKPELAR IRERFAQFLR GETNIAADEA FTKAIQSYTE VFLKSERVQK VVHAGGFSQH
     DFREVFRLII EKRVRSLPDI EGLSKDTVLN SWLAKFDAII KGDETDQNRN ARGRSRNPNS
     AMSADAVLGK EQLYDVFQQI LGVKKFEHQI IFNSLQLDNP DEQAAAIRRE FATREEALKD
     PMKMKRLTPK FVVKDMETLY MDEVRMSINT LIGNLETVPV TTRGQTVGKR KDKSRSRSIE
     DLSLFNSLKR RTSSGSLNKG DSDDGDVTLT KSDVSLALSM EVVVMEVQGL KSIQPNKIVY
     CVMDVDGHKL ATDHAEASKP KWDTQGDFTT KTPLPTVKVK LYTEVKSLVS FDDKELGKIM
     ITPTPNCSRN PEWYTMTLPK NSQDSSLKIR IAIRIEKPPN LKYSGHCWCI GRNSWKKWKK
     RFFCLVQVSQ YAFAVCSFRE KKADPTEFIQ LDGFTIDYMP ESDPELSAQG GKHFFTAIKE
     GDELKFATDD ENERHLWVQA LYRATGQAYK PVPPKQSTIA PKAQGFQDKA SKHGMDALIQ
     ADSINFDHDH LYSDIQRLTL DFRINEPICS LGWFSPGQAF VLEEYSARYM VRGCFRHVTL
     LSNLLDKADD GLLIDPALIH YSFAFCASHV HGNRCMPDRQ GPEGVGTVTL EEKEKFQEIK
     ERLRVLLEKQ ITNFRYCFPF GRPEGALKGT LGLLERVLMK DVVSPVPPEE VRAVIRKCLE
     DAALVNYTRI CNEAKIEQRM GNDVSPAQRI EDMIRVTEFC IDLLKENEEH HGEAFSWFSD
     LLSDHSEIFW SLYSVDLDSA LEVQPHDSWD SFPLFQMLND FLLSEPNLKG GIFHNKLVQQ
     FQPLVVRYID LMEHSIAQAI DKGFLKEKWE SRKEGCATSE DIYWKMDALH TFVIDLNWPE
     EDFRKYLQTK MKTLTSDLIS KVSDCTFTAF DSWMQKAKKS TDYMLPSEVC VQINVMFSSK
     SRAVRVTVDS GEYKYQSKLD ETLETMLKTM ESCIQEKLLG VLESVLSRLA RYDEGNPIGA
     ILNIAPKPAS IFNKLKTMAG DTSVQSSSST RQPLTAQQSS GQIGNSYVTF FHGCTELLRQ
     VIIDEIWVNG LFEHWYDNQM KAINDWLTER LQQSLSATQF ISLSNIVKKV YQDFAMQGID
     EERLNSKTYQ SISRRLQLEE SNSHIQEGIR RLKT