UNC36_CAEEL
ID UNC36_CAEEL Reviewed; 1249 AA.
AC P34374; A9Z1J5; P34372; P34373;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Voltage-dependent calcium channel unc-36;
DE AltName: Full=Pharyngeal calcium channel subunit alpha-2;
DE AltName: Full=Uncoordinated protein 36;
DE Flags: Precursor;
GN Name=unc-36; Synonyms=unc-72; ORFNames=C50C3.9/C50C3.10/C50C3.11;
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
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).
RN [3]
RP FUNCTION.
RX PubMed=8462849; DOI=10.1093/genetics/133.4.897;
RA Avery L.;
RT "The genetics of feeding in Caenorhabditis elegans.";
RL Genetics 133:897-917(1993).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8807295; DOI=10.1093/genetics/143.3.1219;
RA Schafer W.R., Sanchez B.M., Kenyon C.J.;
RT "Genes affecting sensitivity to serotonin in Caenorhabditis elegans.";
RL Genetics 143:1219-1230(1996).
RN [5]
RP FUNCTION.
RX PubMed=10571181; DOI=10.1016/s0092-8674(00)81525-1;
RA Troemel E.R., Sagasti A., Bargmann C.I.;
RT "Lateral signaling mediated by axon contact and calcium entry regulates
RT asymmetric odorant receptor expression in C. elegans.";
RL Cell 99:387-398(1999).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16838374; DOI=10.1002/neu.20261;
RA Frokjaer-Jensen C., Kindt K.S., Kerr R.A., Suzuki H., Melnik-Martinez K.,
RA Gerstbreih B., Driscol M., Schafer W.R.;
RT "Effects of voltage-gated calcium channel subunit genes on calcium influx
RT in cultured C. elegans mechanosensory neurons.";
RL J. Neurobiol. 66:1125-1139(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100 AND ASN-757, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: May act as an auxiliary subunit of the unc-2 voltage-gated
CC calcium channel which appears to trigger calcium-activated signaling
CC pathways that control the serotonin response. Inhibiting serotonin
CC sensitivity of the vulval muscles results in egg laying defects. May
CC act in both neurons and muscle cells to enhance motor activity as it is
CC required for coordinated movement. Has a role in neural depolarization-
CC induced calcium influx and pharyngeal pumping (PubMed:8462849,
CC PubMed:8807295, PubMed:16838374). Involved in restricting the
CC expression of the putative olfactory receptor str-2 to only one of the
CC two AWC neurons (PubMed:10571181). {ECO:0000269|PubMed:10571181,
CC ECO:0000269|PubMed:16838374, ECO:0000269|PubMed:8462849,
CC ECO:0000269|PubMed:8807295}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34374-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34374-2; Sequence=VSP_036007;
CC -!- TISSUE SPECIFICITY: Decendants of the cells AB and AB.p (that give rise
CC to nearly all non-pharyngeal neurons), decendants of P1 (that give rise
CC to body muscle) and cell lineages that give rise to the adult and
CC juvenile motor neurons. Expressed in body wall, vulval muscle and
CC pharyngeal muscle. {ECO:0000269|PubMed:16838374,
CC ECO:0000269|PubMed:8807295}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a weak egg-laying constitutive
CC (Egl-c) phenotype and slow irregular pharyngeal pumping.
CC {ECO:0000269|PubMed:16838374}.
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DR EMBL; FO080718; CCD66125.1; -; Genomic_DNA.
DR EMBL; FO080718; CCD66126.1; -; Genomic_DNA.
DR PIR; S44617; S44617.
DR PIR; S44618; S44618.
DR PIR; S44619; S44619.
DR RefSeq; NP_001040851.1; NM_001047386.2. [P34374-1]
DR RefSeq; NP_001040852.1; NM_001047387.2. [P34374-2]
DR AlphaFoldDB; P34374; -.
DR SMR; P34374; -.
DR BioGRID; 41360; 1.
DR STRING; 6239.C50C3.9a; -.
DR iPTMnet; P34374; -.
DR PaxDb; P34374; -.
DR EnsemblMetazoa; C50C3.9a.1; C50C3.9a.1; WBGene00006772. [P34374-1]
DR EnsemblMetazoa; C50C3.9b.1; C50C3.9b.1; WBGene00006772. [P34374-2]
DR GeneID; 176155; -.
DR UCSC; C50C3.9a; c. elegans.
DR CTD; 176155; -.
DR WormBase; C50C3.9a; CE32168; WBGene00006772; unc-36.
DR WormBase; C50C3.9b; CE39702; WBGene00006772; unc-36.
DR eggNOG; KOG2353; Eukaryota.
DR GeneTree; ENSGT00940000166626; -.
DR InParanoid; P34374; -.
DR OMA; NDYFNIM; -.
DR OrthoDB; 69856at2759; -.
DR PhylomeDB; P34374; -.
DR Reactome; R-CEL-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-CEL-422356; Regulation of insulin secretion.
DR Reactome; R-CEL-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-CEL-5576893; Phase 2 - plateau phase.
DR PRO; PR:P34374; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006772; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P34374; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:WormBase.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0018991; P:oviposition; IMP:UniProtKB.
DR GO; GO:0043050; P:pharyngeal pumping; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:WormBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013680; VDCC_a2/dsu.
DR InterPro; IPR013608; VWA_N.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF08473; VGCC_alpha2; 1.
DR Pfam; PF13519; VWA_2; 1.
DR Pfam; PF13768; VWA_3; 1.
DR Pfam; PF08399; VWA_N; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1249
FT /note="Voltage-dependent calcium channel unc-36"
FT /id="PRO_0000022627"
FT TOPO_DOM 20..1228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1229..1248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 250..479
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1145
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_036007"
SQ SEQUENCE 1249 AA; 144376 MW; 533FF6059D375FB2 CRC64;
MRVVHLLVVL ATYVSTTSSF NKESIKECAK VLSEHMKETF SKISHETILK QNYEKLVEEE
QFDPRAELKK SKHRIEDYLK VRSQFAYKAK ISLEARSVRN DSTVNDPQSK SFIRFMSAKQ
GNDGTTIYES NHLGKRLKVN ETKSFNLTQN ANFYTLPTSS VSSAVHIPTP LYDRNEDLLR
KIDWSDIDAV YRTNREETKD LAFQLFCSEA GYMRYYPAAS WFWDNQDEHL DLFDCRNTEW
YINSATNSKN VLIMLDMSGS MLGQRYEVAK QTTEAILETL SHNDYFNIMT FSKNTFLLDG
CNGTNGLLQA TMRNKKALRR KMDTYQSEGK AEYEKALPLA FSVLLDLKGS YALYTKEEMS
MMSANATNEY QFHLELPEHV LAATKQYIDS INNGGGDNNR GACENVIMLI TDGAPNAYKK
IFDMYNADKK VRVFTFLVGD EAIDFNEVRE MACNNRGYMV HVANMADVDE KIHHYIRRMS
RVVGRHYKES GQLSWWTGVY RERLYLPRPE IFAEPVPITN QSFAVMNKMA SRRKIRLQKS
EARSRMFVTT VSYPVIVNET FMGVAAVNIP LTEVAQKSHP ANIGSKSYFF MLDQNGFVMT
HPQLRPIDPF TKYHKQNYNN MDLLELEVGQ NQNVRSSQKS QAVSDLVCES GANYAECVDD
LRKAVRKMII DCDNSDVQQL DVLYATELLD RVYPQTNTYY AECINHANFV LGLAVAKGDD
YRVVKKQKKY DFGRVKMDWM GDKRWRLHPH WRYCFLNDTD THMSKEEAFE IYAQQMSDSG
KAPLLCEYRR NLVEKLLLDM EATSNLIDSW DTQFNFMKNN LIHLAFFATP SGMIRYYNLT
LQDYDYIDPY WSIFEHIGHL LSIEHAQESY NHFITDLNRK STDDRYYRRA VRMKDTIMFD
VSNNSKIWYK SETQLTGYGL NENLTMLGQA FKAIYLDKAV LGVSGFEFAY DHVVDTMAEH
GCPASDDRKW CVLLDEHAYV FFSNQNDISY EDYLVGKGKH ISQYFGGLNR IAQRAMALLV
ENKFYTKLTY TDNQAVCKAE KVVTTSGNRL RPFYPIFRFL MQTFNFMVRL ASQISGGFLI
WLPNIQFTEA YTASFHEGTD VYPCPKQSSF YFSNKDGKNR PGTTHLVNGN RSERPCKMNA
KCSVKMEASF VDGTNLVMVW ITQDKASENC YDESECSMEI SNQVPFGFEE VKNEETCEEN
EKRKSKANDV CYSIDDDDSE NERRPCSTSP TIVSIFQILF GVFLHFCIF
