UNC80_CAEEL
ID UNC80_CAEEL Reviewed; 3263 AA.
AC Q9XV66; B5U8P2; C1P651; H9G315; Q7JKT8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein unc-80;
DE AltName: Full=Uncoordinated protein 80;
GN Name=unc-80; ORFNames=F25C8.3;
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=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]
RP FUNCTION.
RX PubMed=3576211; DOI=10.1126/science.3576211;
RA Sedensky M.M., Meneely P.M.;
RT "Genetic analysis of halothane sensitivity in Caenorhabditis elegans.";
RL Science 236:952-954(1987).
RN [3]
RP FUNCTION.
RX PubMed=2900611; DOI=10.1097/00000542-198808000-00015;
RA Morgan P.G., Sedensky M.M., Meneely P.M., Cascorbi H.F.;
RT "The effect of two genes on anesthetic response in the nematode
RT Caenorhabditis elegans.";
RL Anesthesiology 69:246-251(1988).
RN [4]
RP FUNCTION.
RX PubMed=2326259; DOI=10.1073/pnas.87.8.2965;
RA Morgan P.G., Sedensky M., Meneely P.M.;
RT "Multiple sites of action of volatile anesthetics in Caenorhabditis
RT elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2965-2969(1990).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17825559; DOI=10.1016/j.cub.2007.08.036;
RA Jospin M., Watanabe S., Joshi D., Young S., Hamming K., Thacker C.,
RA Snutch T.P., Jorgensen E.M., Schuske K.;
RT "UNC-80 and the NCA ion channels contribute to endocytosis defects in
RT synaptojanin mutants.";
RL Curr. Biol. 17:1595-1600(2007).
RN [6]
RP FUNCTION.
RX PubMed=18336069; DOI=10.1371/journal.pbio.0060055;
RA Yeh E., Ng S., Zhang M., Bouhours M., Wang Y., Wang M., Hung W., Aoyagi K.,
RA Melnik-Martinez K., Li M., Liu F., Schafer W.R., Zhen M.;
RT "A putative cation channel, NCA-1, and a novel protein, UNC-80, transmit
RT neuronal activity in C. elegans.";
RL PLoS Biol. 6:E55-E55(2008).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19074276; DOI=10.1073/pnas.0810359105;
RA Pierce-Shimomura J.T., Chen B.L., Mun J.J., Ho R., Sarkis R.,
RA McIntire S.L.;
RT "Genetic analysis of crawling and swimming locomotory patterns in C.
RT elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20982-20987(2008).
CC -!- FUNCTION: Probable component of the nca-1 sodium channel complex, a
CC cation channel that regulates neuronal activity by transmitting
CC depolarization signals to synapses. Regulates the transition from slow
CC to rapid forms of locomotion. Required for localization of nca-1 along
CC axons and in non-synaptic regions. Contributes to endocytosis defects
CC in synaptojanin mutants. Involved in the control of anasthetic response
CC to halothane. {ECO:0000269|PubMed:17825559,
CC ECO:0000269|PubMed:18336069, ECO:0000269|PubMed:19074276,
CC ECO:0000269|PubMed:2326259, ECO:0000269|PubMed:2900611,
CC ECO:0000269|PubMed:3576211}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=d;
CC IsoId=Q9XV66-4; Sequence=Displayed;
CC Name=a;
CC IsoId=Q9XV66-1; Sequence=VSP_044200;
CC Name=b;
CC IsoId=Q9XV66-2; Sequence=VSP_044200, VSP_044201, VSP_044202;
CC Name=c;
CC IsoId=Q9XV66-3; Sequence=VSP_044199, VSP_044200, VSP_044202;
CC Name=e;
CC IsoId=Q9XV66-5; Sequence=VSP_044203, VSP_044200, VSP_044201,
CC VSP_044202;
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system. Expressed in both
CC acetylcholine and GABA motor neurons. {ECO:0000269|PubMed:17825559,
CC ECO:0000269|PubMed:19074276}.
CC -!- DISRUPTION PHENOTYPE: Fainters phenotype, characterized by defects in
CC locomotion, vesicle depletion, and electrophysiological defects in
CC synaptojanin mutants. {ECO:0000269|PubMed:17825559}.
CC -!- SIMILARITY: Belongs to the unc-80 family. {ECO:0000305}.
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DR EMBL; Z81512; CAB04172.3; -; Genomic_DNA.
DR EMBL; Z81512; CAE46668.2; -; Genomic_DNA.
DR EMBL; Z81512; CAR64667.2; -; Genomic_DNA.
DR EMBL; Z81512; CAX65056.1; -; Genomic_DNA.
DR EMBL; Z81512; CCG28158.1; -; Genomic_DNA.
DR RefSeq; NP_001023839.2; NM_001028668.2. [Q9XV66-1]
DR RefSeq; NP_001023840.2; NM_001028669.3. [Q9XV66-2]
DR RefSeq; NP_001129895.2; NM_001136423.2. [Q9XV66-3]
DR RefSeq; NP_001256961.1; NM_001270032.1. [Q9XV66-4]
DR RefSeq; NP_001256962.1; NM_001270033.1. [Q9XV66-5]
DR SMR; Q9XV66; -.
DR BioGRID; 45330; 1.
DR STRING; 6239.F25C8.3d; -.
DR EPD; Q9XV66; -.
DR PaxDb; Q9XV66; -.
DR PeptideAtlas; Q9XV66; -.
DR EnsemblMetazoa; F25C8.3a.1; F25C8.3a.1; WBGene00006812. [Q9XV66-1]
DR EnsemblMetazoa; F25C8.3b.1; F25C8.3b.1; WBGene00006812. [Q9XV66-2]
DR EnsemblMetazoa; F25C8.3c.1; F25C8.3c.1; WBGene00006812. [Q9XV66-3]
DR EnsemblMetazoa; F25C8.3d.1; F25C8.3d.1; WBGene00006812. [Q9XV66-4]
DR EnsemblMetazoa; F25C8.3e.1; F25C8.3e.1; WBGene00006812. [Q9XV66-5]
DR GeneID; 180374; -.
DR KEGG; cel:CELE_F25C8.3; -.
DR UCSC; F25C8.3a; c. elegans.
DR CTD; 180374; -.
DR WormBase; F25C8.3a; CE41563; WBGene00006812; unc-80. [Q9XV66-1]
DR WormBase; F25C8.3b; CE47117; WBGene00006812; unc-80. [Q9XV66-2]
DR WormBase; F25C8.3c; CE47217; WBGene00006812; unc-80. [Q9XV66-3]
DR WormBase; F25C8.3d; CE43592; WBGene00006812; unc-80. [Q9XV66-4]
DR WormBase; F25C8.3e; CE47428; WBGene00006812; unc-80. [Q9XV66-5]
DR eggNOG; ENOG502QSTP; Eukaryota.
DR GeneTree; ENSGT00640000091496; -.
DR InParanoid; Q9XV66; -.
DR OMA; FYQWAEA; -.
DR OrthoDB; 82175at2759; -.
DR PhylomeDB; Q9XV66; -.
DR PRO; PR:Q9XV66; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006812; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0034703; C:cation channel complex; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IMP:UniProtKB.
DR GO; GO:0055080; P:cation homeostasis; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IGI:WormBase.
DR GO; GO:0072347; P:response to anesthetic; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:WormBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045852; UNC80.
DR InterPro; IPR031542; UNC80_N.
DR Pfam; PF19424; UNC80; 4.
DR Pfam; PF15778; UNC80_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..3263
FT /note="Protein unc-80"
FT /id="PRO_0000367808"
FT TRANSMEM 2088..2108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2318..2338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2352..2372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2953..2973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2995..3015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 491..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1680..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3078..3166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3178..3198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3080..3106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3107..3124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3135..3166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3180..3198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044199"
FT VAR_SEQ 1363..1406
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_044203"
FT VAR_SEQ 1460..1497
FT /note="Missing (in isoform a, isoform b, isoform c and
FT isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_044200"
FT VAR_SEQ 1636..1644
FT /note="Missing (in isoform b and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_044201"
FT VAR_SEQ 2030..2041
FT /note="Missing (in isoform b, isoform c and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_044202"
SQ SEQUENCE 3263 AA; 366998 MW; 288614628F597E23 CRC64;
MHVRYLQHEH TGTVQLLLMP LSTAASFKSA KWTEEEGEEE CDSVPLPIQT FLWRQTNPFL
GDKIGKLHEA SCVTFERVVV QNILHGLSPS LSNALASVSR WKLVRAALPH VIQCCGSLLL
ANVGEKKLPT SLQKILYILH WMLIDSSSEC IENASTKDDR SVCQSRTQGL FNISSIQLFI
YLIAPLADVI SEEEVVDNIR LESGLKVWQA IWQFRQPDVW CFSAPVKQRR DELPQITFAR
RQNPAQLDTQ GIYLGKDENT VRRPSIVPPP KPPRTDVTVL NEKRKLEEEK MKMKEDYVAI
EIEAPSLKPN DLLIDMSQGV RNKEFERTSS IVRSVSEYKT NLCGQKEKLA TVSKSRTSDA
FDSSPTSDSS ANMLEEVEGI KFSENENCSL SAVFFSSDQA PLVNLSDICS GFSIEEPHDS
TQSSVEVPQH PVLESSMFLS TTSSASDVPP FVLTRASTAE DTTSSCSQQT VIPLAMPVTT
ETTTLPVTLP KSALTKTTNE NRRTDHQRMP STQKSVSGST DDELDEGSFS DPTIASYLDV
AVIRALLITH WQEKGVYWAL SYIHNRLIEI KAYMIIRKST RQRSNSLPSG ERKLSVAPEQ
LTNPVWDDLK IENKPEEGRS HLHVAFNDTE RRKSSDNCLA PHPTTNSRRS SLNTLSRRGI
NRSNPSLSNS VEVLSIRDDA EDDVSNISSK SIEKENTKLN AVFYPEALGS TNFIEKDGKI
SATVIVQTVN QVMDRCTGVR QCELALNIAD VLLGTPLEQT ETFFVQLNIM VFKIYLCLGC
PHGCNEGVKS PHGDFLRAKA KAILAGLERV QPDKFKNILN DYVDNYGTQQ VIDLLHSITS
FCRSELTALD GRRASESRVP SYRNTFNEKD KGIEGRIINA TYKTLITKIS VISAELSLPE
NMSLQQDVRL LVNFVQEHHG NPFRRVGLSA LKDATCKNPT TSDFHTKEDQ TGGSPGAQSQ
KQSNDQASLR RGLFKKKNEK SGGTTTGNDD SEGDSSPSTP RTVSSMDDGV SPLASTSYYK
KKSAPKLHFA FGLLKSVKPD MDEEISDNEN EEGTSNEEAG LPQRRPLRQS SKQVKARLPI
DSKGGMRLWG TYVPPPNYID AKGIFDGARR FAFLLETARP GTFPDAPLIA AIMHLKSPVL
ARASLLLECA NLVSRCNRGQ WPEWIRSSHH RTFSLGGALA NRGTPSATRR MHSLQRQAGR
YFYQWGVQIG EHISKLLELS ENKSKKTLQM EDTIEDFFDD GIVNNQNGEK CPIALQFIAV
LLLQEITAFL RETFKTIPRS KNSKPQTGNS GWDKLLSHRR WSILSNTFNA QQTGSVNSIT
EINSSIHLND KERRISFSAT EEDSPRGSKD AIDEINAVDK KGSIHMQVVR PPSLSARLFS
RQSTHEESGG SAQGSTKSTT YVPETGRRIA TGRQRLLKRG SPMATGTQPS LESSHKRKSF
RNRKQSKQAH LEEEEKSDGG SLTSQQSPIV QRMRAASMRQ SSNFLALFHH AIPEFLDAGA
THILSARESL KPTDDGLQSP VESVHPVIIP HSNHGSAHSQ QPVVLKSSMD DEEQHMLSNL
PWIKVLIKFS NSFDLECNHV GVCSAKCFQR VHRQCFRMIE SLSTLYGMER NVSTRADKRN
LLADNWQAKQ QALRKQTETN SARASIHARQ STAVPRRESA MVGQPEFASK AIKMMLMEKM
QQEKEKEKEK EKEEKDALKK QSVEQDHSST DTEEDAQLPE KNKPMLTYLR SLVLQLVHSP
ISSVLKCCLL LSVEQHKQMI EVCWKMLIHE DPHVVASAAS MFIVASVKKS EESLLIIKTA
LDSQDPQVRT SGIQRFYTLW RNRFHAWLKM EDGAQASFKV PPPGIDFTLP SPAIGQSQLP
VVDPPWMPHL KTKIEELSLK EEEHATSQTI MTMTRTRRKQ KQEMVKRAVR EAEERQSEQR
QLFRLRSSAI VSLAAYEPAL FHHQQEQTEE SDNSHQHARH VMPVAQPLFP SALLSVVPQI
IELLDDPQVD NNGVSVGDVA KKVIWTCIVE DPSLFLRHFL EKLTNRDRQV LISEYAPTPA
YEALMSQLRK LVLRFHPLPS QAAHSLLNYL FGFVMHYVRA QCEGSEKAIG MALSICWLLS
PNIHGLYFKD LKQTLKKEQC DQALMITANV PSAKKIIVHG LDSTSGGIPS QFPVHEDTQF
HQILNDSLEF FNIDEDDLNC FYLTDTKTGV IHLPAAYVRD YYFFHRSFYP QLTLVKLSPE
VAEKKMKETA FHQKFIECGK VLLTHNILKY SPQHVIAQRV FFLHDEFTHL PSFPRKSLET
CFGMYFGPGG EQLKAMESMH KFVWAKMMSD MFEKMENAFM FADLHLFINV INGIMIMHCE
DVLILRRCAA TYISISIHFN TLFASQGFFL IMPTLLRCYS QRQTNKVFCG VVEFICRQFY
TLHRKPFLLQ MCGAIANIID NSSNDFEINP MRVKAKYWFN LIKKMEEITD EDPLDILGLV
PYEKPLKALD LCYRDDPNTF CALTDAMASC ICVCAFSPES KRSHHMLLIM QAMLPHMMKR
LEEETLQSGN SPAAVKHEIS QWITMAVEMK ALINSCEQLV RGPTRAFDLV NSVSERGKSF
VADSPQFFDP PTTNEDENSR PYHLKEKRST AVAWEAAEVE EQQKETYRRP RDTLLQLIAA
YIEMASVRLK ELTKLGANLE HAKIPDVLDH KCYVKLGEVA LALLKVAPYD LSTTTCHGLQ
KYFQIILPVT DWSIESNRSA LNIILRRLDK TLSKIAKRQS FRKRAIWIAL SSWINGICDT
LNAFPYIAHL HPLRTITQLC LRMMVGDPCV EDSAASTALH PTTVLHPTPP PQTFANAVLR
LTTILMQALG QFAFSLDFVT STEGMGVSSE RLEAVLCHVL IPLFLRIPNN PKEQSIFQAK
DLSQCLTVMQ NAISPPLVKQ QAPPLISTST LTTTFIRGAQ DVTGRQGSVS VTDRGHSATV
STHRIVRESI CQAIYLGLKV LMLTFGKLLA PMWPRVARIV KDLLAKKPGA PTSMAFVDFL
LHSNLPISLF ILPMIQNKMK QKPGTDQEAA WQTEILEKLD AKSHNIVPPS ILLVKCYQEL
QQLKEELTMK PIEMTRSYTP TMADPHSDSS AASTAPRGAS SRQSIDRRTS VHMKKVLPTM
KEDIPEDPED SEDVIDSNST GQVTSRISKS PSIPLNKTHQ SSRTRSVSGF GMWRSVRRKS
RHVSSAEESS EERGSVELHD VGHHSALHEP NRTPNRRSTE ALVLPLHESI DTNRHRFVSF
STPKKTHEVS EDVFQITEQH QLV
