UNC93_CAEEL
ID UNC93_CAEEL Reviewed; 705 AA.
AC Q93380; Q23024; Q23025; Q58A93; Q7JN54; Q7JN55;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative potassium channel regulatory protein unc-93;
DE AltName: Full=Uncoordinated protein 93;
GN Name=unc-93; ORFNames=C46F11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA45760.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), FUNCTION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ALA-49; GLY-388 AND GLY-562.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA45760.1};
RX PubMed=1313436; DOI=10.1083/jcb.117.1.143;
RA Levin J.Z., Horvitz H.R.;
RT "The Caenorhabditis elegans unc-93 gene encodes a putative transmembrane
RT protein that regulates muscle contraction.";
RL J. Cell Biol. 117:143-155(1992).
RN [2] {ECO:0000312|EMBL:CAB03760.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB03760.3};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14534247; DOI=10.1523/jneurosci.23-27-09133.2003;
RA de la Cruz I.P., Levin J.Z., Cummins C., Anderson P., Horvitz H.R.;
RT "sup-9, sup-10, and unc-93 may encode components of a two-pore K+ channel
RT that coordinates muscle contraction in Caenorhabditis elegans.";
RL J. Neurosci. 23:9133-9145(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
CC -!- FUNCTION: May contribute to coordination of muscle contraction as
CC regulatory subunit of a nonessential potassium channel complex
CC (PubMed:1313436, PubMed:14534247). Plays a role in the formation of
CC muscle connections, also called muscle arm extensions, between the body
CC wall and the motor axons in the dorsal and ventral cord
CC (PubMed:27123983). {ECO:0000269|PubMed:27123983,
CC ECO:0000303|PubMed:1313436, ECO:0000303|PubMed:14534247}.
CC -!- SUBUNIT: May form a complex with sup-9 and sup-10 where unc-93 and sup-
CC 10 act as regulatory subunits of the two pore potassium channel sup-9.
CC {ECO:0000303|PubMed:14534247}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Associated with dense bodies.
CC {ECO:0000269|PubMed:14534247}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=a;
CC IsoId=Q93380-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q93380-2; Sequence=VSP_018911;
CC -!- TISSUE SPECIFICITY: Low levels in body-wall muscles, eight vulval
CC muscles, intestinal muscles and a subset of head neurons.
CC {ECO:0000269|PubMed:14534247}.
CC -!- DEVELOPMENTAL STAGE: More highly expressed in L1 larvae than in eggs
CC and adults. {ECO:0000269|PubMed:1313436}.
CC -!- DISRUPTION PHENOTYPE: Defective extension of body wall muscle
CC connections or arms towards the ventral nerve cord. Double knockout
CC with madd-3 results in severe muscle arm extension defects.
CC {ECO:0000269|PubMed:27123983}.
CC -!- MISCELLANEOUS: Gain of function phenotype is phenocopied by exposure to
CC the unc-49 agonist muscimol. {ECO:0000269|PubMed:14534247}.
CC -!- SIMILARITY: Belongs to the unc-93 family. {ECO:0000305}.
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DR EMBL; X64415; CAA45760.1; -; Genomic_DNA.
DR EMBL; X64415; CAA45761.1; -; Genomic_DNA.
DR EMBL; Z81449; CAB03760.3; -; Genomic_DNA.
DR EMBL; Z81449; CAI70399.1; -; Genomic_DNA.
DR PIR; S23352; S23352.
DR PIR; T19969; T19969.
DR RefSeq; NP_001021218.1; NM_001026047.4. [Q93380-1]
DR RefSeq; NP_001021219.1; NM_001026048.2.
DR AlphaFoldDB; Q93380; -.
DR SMR; Q93380; -.
DR BioGRID; 40706; 2.
DR DIP; DIP-24405N; -.
DR IntAct; Q93380; 1.
DR STRING; 6239.C46F11.1a; -.
DR TCDB; 2.A.1.58.2; the major facilitator superfamily (mfs).
DR iPTMnet; Q93380; -.
DR EPD; Q93380; -.
DR PaxDb; Q93380; -.
DR EnsemblMetazoa; C46F11.1a.1; C46F11.1a.1; WBGene00006822. [Q93380-1]
DR EnsemblMetazoa; C46F11.1b.1; C46F11.1b.1; WBGene00006822. [Q93380-2]
DR GeneID; 175466; -.
DR KEGG; cel:CELE_C46F11.1; -.
DR UCSC; C46F11.1a; c. elegans. [Q93380-1]
DR CTD; 175466; -.
DR WormBase; C46F11.1a; CE30906; WBGene00006822; unc-93. [Q93380-1]
DR WormBase; C46F11.1b; CE37957; WBGene00006822; unc-93. [Q93380-2]
DR eggNOG; KOG3097; Eukaryota.
DR GeneTree; ENSGT00530000063359; -.
DR InParanoid; Q93380; -.
DR OMA; GYFFMIV; -.
DR OrthoDB; 282870at2759; -.
DR PhylomeDB; Q93380; -.
DR PRO; PR:Q93380; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006822; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0015459; F:potassium channel regulator activity; IGI:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR GO; GO:0043266; P:regulation of potassium ion transport; IGI:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR010291; Ion_channel_UNC-93.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF05978; UNC-93; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Glycoprotein; Ion transport;
KW Membrane; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..705
FT /note="Putative potassium channel regulatory protein unc-
FT 93"
FT /id="PRO_0000036083"
FT TOPO_DOM 1..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_018911"
FT MUTAGEN 49
FT /note="A->V: In n200; confers 'rubber band' muscle
FT contraction; when associated with V-562."
FT /evidence="ECO:0000269|PubMed:1313436"
FT MUTAGEN 388
FT /note="G->A: In e1500; confers 'rubber band' muscle
FT contraction."
FT /evidence="ECO:0000269|PubMed:1313436"
FT MUTAGEN 562
FT /note="G->V: In n200; confers 'rubber band' muscle
FT contraction; when associated with V-49."
FT /evidence="ECO:0000269|PubMed:1313436"
SQ SEQUENCE 705 AA; 80352 MW; 91D49A788A3EAC58 CRC64;
MKFQKMGDSN TWDLVGEQQQ RKKSRSPSRA SRVDSELLVG VENAAELEAL GLGKEQLEEE
ARRHKKQRSK SPALENIRKT SIHLLQKFGA IPKKKDDSVL LFRFHDIPDI PLESLCIRPK
EFFEEPKVFS FRDMGREQQK AEVNEKCSYL FRGTSFDHDD HFELPTETGR VPEYDHFCPI
HGSRRRLPRN KLVTMQTLMH SVDDEDNEDL AYIYGHDFLA KLVRKKKREM MSGTEKERAN
KIKRKIMSNL WILSVAFLFL FTAFNGLQNL QTSVNGDLGS DSLVALYLSL AISSLFVPSF
MINRLGCKLT FLIAIFVYFL YIVINLRPTY SSMIPASIFC GIAASCIWGA KCAYITEMGI
RYASLNFESQ TTVIVRFFGY FFMIVHCGQV VGNMVSSYIF TLSYSQALRG PEDSIYDSCG
YQFPKNLSDL TELAESNLAR PPQKVYVAVC LAYLACVIIS GMIMSMFLNA LAKDARNRKM
AQKFNSEIFY LMLKHLINIK FMLLVPLTIF NGLEQAFLVG VYTKAFVGCG LGIWQIGFVM
ACFGISDAVC SLVFGPLIKL FGRMPLFVFG AVVNLLMIVT LMVWPLNAAD TQIFYVVAAM
WGMADGVWNT QINGFWVALV GRQSLQFAFT KYRFWESLGI AIGFALIRHV TVEIYLLITF
FMLLLGMCGF LAIENFDHII KFWHHLIHTS CPEKEPLDDR NSDFE
