CNP_HELLU
ID CNP_HELLU Reviewed; 172 AA.
AC Q25077;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=HCS2 neuropeptides {ECO:0000305};
DE AltName: Full=CNP neuropeptides {ECO:0000305};
DE AltName: Full=Command neuron-specific peptides {ECO:0000303|PubMed:9622259};
DE Contains:
DE RecName: Full=Peptide CNP1 {ECO:0000303|PubMed:9622259};
DE AltName: Full=CNP1 {ECO:0000303|PubMed:9622259};
DE Contains:
DE RecName: Full=Peptide CNP2 {ECO:0000303|PubMed:9622259};
DE AltName: Full=CNP2 {ECO:0000303|PubMed:9622259};
DE AltName: Full=DYPRLamide {ECO:0000303|PubMed:11246168};
DE Contains:
DE RecName: Full=Peptide CNP3 {ECO:0000303|PubMed:9622259};
DE AltName: Full=CNP3 {ECO:0000303|PubMed:9622259};
DE Contains:
DE RecName: Full=Peptide CNP4 {ECO:0000303|PubMed:9622259};
DE AltName: Full=CNP4 {ECO:0000303|PubMed:9622259};
DE Flags: Precursor;
GN Name=HCS2 {ECO:0000303|PubMed:9622259};
OS Helix lucorum (Snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Helicidae; Helix.
OX NCBI_TaxID=31229 {ECO:0000312|EMBL:CAA63082.1};
RN [1] {ECO:0000312|EMBL:CAA63082.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF CNP1; CNP2; CNP3 AND CNP4,
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PROBABLE AMIDATION
RP AT LEU-31; ILE-48 AND VAL-88.
RC TISSUE=Neural ganglion {ECO:0000312|EMBL:CAA63082.1};
RX PubMed=9622259; DOI=10.1016/s0306-4522(97)00561-7;
RA Bogdanov Y.D., Balaban P.M., Poteryaev D.A., Zakharov I.S., Belyavsky A.V.;
RT "Putative neuropeptides and an EF-hand motif region are encoded by a novel
RT gene expressed in the four giant interneurons of the terrestrial snail.";
RL Neuroscience 85:637-647(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11246168; DOI=10.1016/s0306-4522(01)00004-5;
RA Balaban P.M., Poteryaev D.A., Zakharov I.S., Uvarov P., Malyshev A.,
RA Belyavsky A.V.;
RT "Up- and down-regulation of Helix command-specific 2 (HCS2) gene expression
RT in the nervous system of terrestrial snail Helix lucorum.";
RL Neuroscience 103:551-559(2001).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1023/B:MBIL.0000049866.40200.f9;
RA Ivanova J.L., Leonova O.G., Popenko V.I., Ierusalimskii V.N.,
RA Bogusalvskii D.V., Balaban P.M., Beliavskii A.V.;
RT "Immunocytochemical study of the distribution of hcs2 gene products in
RT Command Neurons of the Helix lucorum Snail.";
RL Mol. Biol. (Mosk.) 38:875-883(2004).
RN [4] {ECO:0000305}
RP FUNCTION (CNP4), TISSUE SPECIFICITY, AND SYNTHESIS OF CNP4.
RX PubMed=16465488; DOI=10.1007/s11055-006-0007-y;
RA Korshunova T.A., Malyshev A.Y., Zakharov I.S., Ierusalimskii V.N.,
RA Balaban P.M.;
RT "Functions of peptide CNP4, encoded by the HCS2 gene, in the nervous system
RT of Helix lucorum.";
RL Neurosci. Behav. Physiol. 36:253-260(2006).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16763780; DOI=10.1007/s10571-006-9025-0;
RA Ivanova J.L., Leonova O.G., Popenko V.I., Ierusalimsky V.N.,
RA Korshunova T.A., Boguslavsky D.V., Malyshev A.Y., Balaban P.M.,
RA Belyavsky A.V.;
RT "Intracellular localization of the HCS2 gene products in identified snail
RT neurons in vivo and in vitro.";
RL Cell. Mol. Neurobiol. 26:127-144(2006).
RN [6] {ECO:0000305}
RP FUNCTION (CNP2), TISSUE SPECIFICITY (CNP2), AND SYNTHESIS OF CNP2.
RX PubMed=20399241; DOI=10.1016/j.peptides.2010.04.006;
RA Aseyev N., Zakharov I.S., Balaban P.M.;
RT "Morphology of neuropeptide CNP2 modulation of heart activity in
RT terrestrial snail.";
RL Peptides 31:1301-1308(2010).
CC -!- FUNCTION: Neurotransmitter or neuromodulator peptides that mediate
CC withdrawal behavior such as pneumostome activity in the respiratory
CC system (PubMed:11246168, PubMed:9622259, Ref.3). Possibly regulates
CC calcium levels in command premotor interneurons (PubMed:11246168,
CC Ref.3). {ECO:0000269|PubMed:11246168, ECO:0000269|PubMed:9622259,
CC ECO:0000269|Ref.3}.
CC -!- FUNCTION: [Peptide CNP2]: Involved in neural modulation of the
CC cardiovascular system, in addition to or as part of, the peptide's role
CC in mediating withdrawal behavior (PubMed:9622259, PubMed:20399241).
CC Appears to have a function in both the ventricle and auricle chambers
CC of the heart; the effects are both positively inotrophic, by affecting
CC the magnitude of ventricle contractions, and positively chronotropic,
CC by affecting the frequency of auricle contractions (PubMed:20399241).
CC In vitro modulates the spontaneous activity rate of parietal command
CC neurons on motoneurons from the visceral ganglions that control
CC pneumostome closure (PubMed:9622259). {ECO:0000269|PubMed:20399241,
CC ECO:0000269|PubMed:9622259}.
CC -!- FUNCTION: [Peptide CNP3]: Likely to function as a neurotransmitter or
CC neuromodulator that mediates withdrawal behavior. In vitro modulates
CC the spontaneous activity rate of parietal command neurons on
CC motoneurons from the visceral ganglion that control pneumostome
CC closure. {ECO:0000269|PubMed:9622259}.
CC -!- FUNCTION: [Peptide CNP4]: Involved in neural modulation that mediates
CC pneumostome movements in the respiratory system as part of the
CC withdrawal response (PubMed:16465488, PubMed:9622259). In vitro elicits
CC an increase in the rhythmic activity of pneumostome motoneurons, and
CC increases the frequency and intensity of pneumostome movements
CC (PubMed:16465488, PubMed:9622259). This suggests that this peptide, and
CC possibly other HCS2 peptides, may be responsible for the 'delayed
CC effect' influence of the command interneurons which consists of an
CC intensification of respiratory movements (PubMed:16465488,
CC PubMed:9622259). Also promotes the growth of neuron processes in
CC cultured cells extracted from the pleural ganglia, and may therefore
CC have a role in development and/or rearrangements of the defensive
CC neural network (PubMed:16465488). {ECO:0000269|PubMed:16465488,
CC ECO:0000269|PubMed:9622259}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16763780,
CC ECO:0000269|Ref.3}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:16763780, ECO:0000269|Ref.3}. Perikaryon
CC {ECO:0000269|Ref.3}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:16763780}. Note=Occurs mainly on the granule
CC surface (Ref.3). Present in the perikaryon of command neurons in the
CC cytoplasm surrounding giant nuclei (Ref.3). {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: [Peptide CNP3]: Cytoplasm {ECO:0000269|Ref.3}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:16763780,
CC ECO:0000269|Ref.3}. Perikaryon {ECO:0000269|Ref.3}. Note=Occurs mainly
CC within the granule. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: [Peptide CNP4]: Cytoplasm {ECO:0000269|Ref.3}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|Ref.3}. Perikaryon
CC {ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed in regions of the central nervous system
CC that are known to control withdrawal behavior (PubMed:9622259,
CC PubMed:11246168, PubMed:16465488, PubMed:16763780, Ref.3). Detected in
CC the cell bodies and processes of the command interneurons (at protein
CC level) (PubMed:16465488, PubMed:16763780, Ref.3). Predominately
CC expressed in the LPa3/RPa3 and LW/RPa2 giant interneurons that are
CC located in the parietal ganglia, as well as in other unidentified
CC neurons in the pedal, pleural and cerebral ganglia (PubMed:9622259,
CC PubMed:16763780, PubMed:11246168). Peptide CNP2: Detected in neural
CC fibers that pass along the cardiorenal complex in the pericardium and
CC arborize in adjacent connective tissue to innervate both the auricle,
CC near the exit of the pulmonary vein, and the ventricle near the aorta
CC (at protein level) (PubMed:20399241). The inner surface of the heart,
CC ventricle neck region and aorta, are richly innervated with these
CC neural fibers (at protein level) (PubMed:20399241). Also detected in
CC large varicosities in the heart trabeculae and in the
CC auriculoventricular region at the fiber terminals (at protein level)
CC (PubMed:20399241). In the parieto-visceral ganglionic complex of the
CC CNS, detected in a soma on the ventral caudal surface of the visceral
CC ganglion and a soma located in the right parietal ganglion (at protein
CC level) (PubMed:20399241). Peptide CNP3: Detected in the command
CC interneurons (at protein level) (PubMed:16763780, Ref.3). Peptide CNP4:
CC Detected in the cell bodies and processes of the command interneurons
CC (at protein level) (PubMed:16465488, Ref.3).
CC {ECO:0000269|PubMed:11246168, ECO:0000269|PubMed:16465488,
CC ECO:0000269|PubMed:16763780, ECO:0000269|PubMed:20399241,
CC ECO:0000269|PubMed:9622259, ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: In embryos, not detected until 3 days before
CC hatching when it is significantly expressed in the right but not in the
CC left parietal giant interneurons. In juveniles under a month old,
CC expression is higher in the right parietal giant interneurons compared
CC to the left. {ECO:0000269|PubMed:9622259}.
CC -!- INDUCTION: In isolated central nervous system neurons, up-regulated or
CC down-regulated in the cerebral, parietal, pleural and pedal ganglia in
CC response to different stimuli. Up-regulated in response to noxious
CC input such as injury, as well as by the application of
CC neurotransmitters and second messengers such as serotonin that are
CC known to be involved in withdrawal behavior. Also up-regulated by
CC thapsigargin which increases the intracellular free calcium
CC concentration. Down-regulated by a decrease in synaptic activity in the
CC nervous system induced by increased Mg(2+) concentration.
CC {ECO:0000269|PubMed:11246168}.
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DR EMBL; X92111; CAA63082.1; -; mRNA.
DR AlphaFoldDB; Q25077; -.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0120111; C:neuron projection cytoplasm; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Amidation; Calcium; Cleavage on pair of basic residues; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Metal-binding; Neuropeptide;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..172
FT /note="HCS2 neuropeptides"
FT /evidence="ECO:0000255"
FT /id="PRO_5004202478"
FT PEPTIDE 20..25
FT /note="Peptide CNP1"
FT /evidence="ECO:0000269|PubMed:9622259"
FT /id="PRO_0000445969"
FT PEPTIDE 27..31
FT /note="Peptide CNP2"
FT /evidence="ECO:0000269|PubMed:9622259"
FT /id="PRO_0000445970"
FT PEPTIDE 35..48
FT /note="Peptide CNP3"
FT /evidence="ECO:0000269|PubMed:9622259"
FT /id="PRO_0000445971"
FT PEPTIDE 75..88
FT /note="Peptide CNP4"
FT /evidence="ECO:0000269|PubMed:9622259"
FT /id="PRO_0000445972"
FT DOMAIN 133..168
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 31
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:9622259"
FT MOD_RES 48
FT /note="Isoleucine amide"
FT /evidence="ECO:0000305|PubMed:9622259"
FT MOD_RES 88
FT /note="Valine amide"
FT /evidence="ECO:0000305|PubMed:9622259"
SQ SEQUENCE 172 AA; 19155 MW; 3C52B7285A2CC373 CRC64;
MQHQIRALLL FLLSGSACAM FYPRPKDYPR LGKRSFFTTV NGNHYPRIGR RDATGSSLVL
PEADYTDLGD LTKRGVFTQG AHGSYPRVGR GGAVLSRDYL NERSKNLEKM SGDKDDDLEV
DNGDGSRRLQ AGHSGIPLEI LFIAYDSDND GKLSKEEFVT GLAQYQMQCP LY
