CLHM1_CAEEL
ID CLHM1_CAEEL Reviewed; 329 AA.
AC Q18593;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Calcium homeostasis modulator protein {ECO:0000312|WormBase:C44B7.4};
GN Name=clhm-1 {ECO:0000312|WormBase:C44B7.4};
GN ORFNames=C44B7.4 {ECO:0000312|WormBase:C44B7.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-125.
RX PubMed=23884934; DOI=10.1523/jneurosci.5919-12.2013;
RA Tanis J.E., Ma Z., Krajacic P., He L., Foskett J.K., Lamitina T.;
RT "CLHM-1 is a functionally conserved and conditionally toxic Ca2+-permeable
RT ion channel in Caenorhabditis elegans.";
RL J. Neurosci. 33:12275-12286(2013).
CC -!- FUNCTION: Pore-forming subunit of a voltage-gated ion channel.
CC Permeable to monovalent cations, divalent cations and anions with
CC selectivity Ca(2+) > Mg(2+) > Na(+) = K(+) > Cl(-). Acts both as a
CC voltage-gated and calcium-activated ion channel. Required for normal
CC locomotion. {ECO:0000269|PubMed:23884934}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23884934};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in head and body wall muscles, IL2, ASG,
CC ASI, ASJ, PHA and PHB sensory neurons, and spermatheca.
CC {ECO:0000269|PubMed:23884934}.
CC -!- DISRUPTION PHENOTYPE: Uncoordinated locomotion with mutants showing
CC reduced forward velocity, muscle force and power production.
CC {ECO:0000269|PubMed:23884934}.
CC -!- SIMILARITY: Belongs to the CALHM family. {ECO:0000305}.
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DR EMBL; BX284602; CCD61557.1; -; Genomic_DNA.
DR PIR; T15797; T15797.
DR RefSeq; NP_495403.2; NM_063002.3.
DR PDB; 6LMV; EM; 3.60 A; A/B/C/D/E/F/G/H/I=1-329.
DR PDB; 6LOM; EM; 3.73 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-329.
DR PDBsum; 6LMV; -.
DR PDBsum; 6LOM; -.
DR AlphaFoldDB; Q18593; -.
DR SMR; Q18593; -.
DR STRING; 6239.C44B7.4; -.
DR TCDB; 1.A.84.1.4; the calcium homeostasis modulator ca(2+) channel (calhm-c) family.
DR PaxDb; Q18593; -.
DR EnsemblMetazoa; C44B7.4.1; C44B7.4.1; WBGene00016626.
DR GeneID; 183429; -.
DR KEGG; cel:CELE_C44B7.4; -.
DR UCSC; C44B7.4; c. elegans.
DR CTD; 183429; -.
DR WormBase; C44B7.4; CE34753; WBGene00016626; clhm-1.
DR eggNOG; ENOG502QSG7; Eukaryota.
DR GeneTree; ENSGT01030000234610; -.
DR HOGENOM; CLU_073171_0_0_1; -.
DR InParanoid; Q18593; -.
DR OMA; AVVFQCP; -.
DR OrthoDB; 833717at2759; -.
DR PhylomeDB; Q18593; -.
DR PRO; PR:Q18593; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016626; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:WormBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:WormBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR InterPro; IPR029569; CALHM.
DR PANTHER; PTHR32261; PTHR32261; 1.
DR Pfam; PF14798; Ca_hom_mod; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..329
FT /note="Calcium homeostasis modulator protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438169"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..53
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..191
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 125
FT /note="D->A: Changes relative Ca2+ and Cl-permeabilities."
FT /evidence="ECO:0000269|PubMed:23884934"
SQ SEQUENCE 329 AA; 37274 MW; B7EEBDC0CBF561BA CRC64;
MTTSINSVVT VFQNVFTNHG STLLNGILIA TTVGGQSLVR KLTFSCPCAY PLNIYHSLVF
MFGPTAALLL IGITVNSTTW KLAHGFFFRV RDTRHSWKTT CVSWIEVLIQ SSVAPIAWLF
VVFLDGGYYR CYRSHEFCLI SDAILCKNST ILNSYASTSS FNKISDNGKY CPPCICVPNP
TDASYLEAES QIYAWGLLLF SGVAAFLVIT CNRMCDKYTL VQRQYVETYK NVETQKFDAV
AKEHASQLAE HNARAFFGQK DWTKRDWDWV SGIPEVNNPL FARLRLIAAE KTQQTMYTPL
QLWNDNKGYR IPQPDLQLTQ IIVDETKED
