MACO1_CAEEL
ID MACO1_CAEEL Reviewed; 897 AA.
AC P91193;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Macoilin {ECO:0000303|PubMed:21437263, ECO:0000303|PubMed:21589894};
GN Name=maco-1 {ECO:0000312|WormBase:D2092.5};
GN ORFNames=D2092.5 {ECO:0000312|WormBase:D2092.5};
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].
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21437263; DOI=10.1371/journal.pgen.1001341;
RA Arellano-Carbajal F., Briseno-Roa L., Couto A., Cheung B.H., Labouesse M.,
RA de Bono M.;
RT "Macoilin, a conserved nervous system-specific ER membrane protein that
RT regulates neuronal excitability.";
RL PLoS Genet. 7:E1001341-E1001341(2011).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21589894; DOI=10.1371/journal.pgen.1001384;
RA Miyara A., Ohta A., Okochi Y., Tsukada Y., Kuhara A., Mori I.;
RT "Novel and conserved protein macoilin is required for diverse neuronal
RT functions in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1001384-E1001384(2011).
RN [4]
RP FUNCTION.
RX PubMed=26976437; DOI=10.1534/g3.115.026450;
RA Neal S.J., Park J., DiTirro D., Yoon J., Shibuya M., Choi W.,
RA Schroeder F.C., Butcher R.A., Kim K., Sengupta P.;
RT "A Forward Genetic Screen for Molecules Involved in Pheromone-Induced Dauer
RT Formation in Caenorhabditis elegans.";
RL G3 (Bethesda) 6:1475-1487(2016).
RN [5]
RP FUNCTION.
RX PubMed=28924007; DOI=10.1523/jneurosci.0031-17.2017;
RA Kitazono T., Hara-Kuge S., Matsuda O., Inoue A., Fujiwara M., Ishihara T.;
RT "Multiple Signaling Pathways Coordinately Regulate Forgetting of Olfactory
RT Adaptation through Control of Sensory Responses in Caenorhabditis
RT elegans.";
RL J. Neurosci. 37:10240-10251(2017).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32908307; DOI=10.1038/s41586-020-2699-5;
RA Kaletsky R., Moore R.S., Vrla G.D., Parsons L.R., Gitai Z., Murphy C.T.;
RT "C. elegans interprets bacterial non-coding RNAs to learn pathogenic
RT avoidance.";
RL Nature 586:445-451(2020).
CC -!- FUNCTION: Plays a role in the regulation of neuronal activity. In AWA
CC and AWC neurons, plays a role in regulating olfactory adaptation by
CC controlling the forgetting sensory responses to odorants such as
CC diacetyl and isoamyl alcohol (PubMed:28924007). May play a role in
CC regulating daf-7 expression in ASI neurons in response to bacterial
CC small RNAs (PubMed:32908307). In ASI neurons, promotes dauer formation
CC in response to pheromones such as the ascarosides ascr#2 and ascr#3
CC (PubMed:26976437). {ECO:0000269|PubMed:21437263,
CC ECO:0000269|PubMed:21589894, ECO:0000269|PubMed:26976437,
CC ECO:0000269|PubMed:28924007, ECO:0000269|PubMed:32908307}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus membrane
CC {ECO:0000269|PubMed:21437263}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Restricted to neuronal cell bodies, absent from
CC dendrites and axons (PubMed:21437263). {ECO:0000269|PubMed:21437263}.
CC -!- TISSUE SPECIFICITY: Strong expression in many neurons, very weak
CC expression is also detected in others tissues.
CC {ECO:0000269|PubMed:21437263, ECO:0000269|PubMed:21589894}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC avoidance behavior in response to P.aeruginosa.
CC {ECO:0000269|PubMed:32908307}.
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DR EMBL; BX284601; CCD68500.1; -; Genomic_DNA.
DR RefSeq; NP_491902.4; NM_059501.4.
DR AlphaFoldDB; P91193; -.
DR SMR; P91193; -.
DR STRING; 6239.D2092.5; -.
DR TCDB; 8.A.38.1.2; the animal macoilin regulator of ion channels (macoilin) family.
DR EPD; P91193; -.
DR PaxDb; P91193; -.
DR PeptideAtlas; P91193; -.
DR EnsemblMetazoa; D2092.5.1; D2092.5.1; WBGene00017066.
DR GeneID; 183963; -.
DR KEGG; cel:CELE_D2092.5; -.
DR UCSC; D2092.5; c. elegans.
DR CTD; 183963; -.
DR WormBase; D2092.5; CE45670; WBGene00017066; maco-1.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR HOGENOM; CLU_321894_0_0_1; -.
DR InParanoid; P91193; -.
DR OMA; GENTHAD; -.
DR OrthoDB; 482580at2759; -.
DR PhylomeDB; P91193; -.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR PRO; PR:P91193; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00017066; Expressed in embryo and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0023041; P:neuronal signal transduction; IMP:WormBase.
DR GO; GO:0043052; P:thermotaxis; IMP:WormBase.
DR InterPro; IPR019130; Macoilin.
DR PANTHER; PTHR13289; PTHR13289; 1.
DR Pfam; PF09726; Macoilin; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..897
FT /note="Macoilin"
FT /id="PRO_0000443037"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 291..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 503..726
FT /evidence="ECO:0000255"
FT COMPBIAS 291..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 100707 MW; FEE5B70E365442E1 CRC64;
MMQQQKPGKP KKINRIDKIK RLQINRSRRP DINQTVPSPL FYVRIVVTWL GMVSLDAMTG
FRFELLWPTW LMIRAAAESI QMRNQHCVTT IANPTAARFS VLFICVTATS DLICYLFIPI
RMLIFLATTY VWISLYYHTQ GGFLRSLATV YGGERLQSWP IVFITCFIVI FELFLRIRSH
PILISFFPNV AEYAGVSPVW PRSLNAFFGA HSIGYPVILI TVSMHYYFNE WKLRRKQCDV
SNRNEQLFRI LVEGLPAEYE GPKDYTSQQC LEDDLYYLDP PVQTLQPMQA IQAASATPPT
SSKKNGIHKR NGDVTSSTTT SSRKKKHNGN SGFNSTPPND KKKGKSIRDV DMDDGDDSDD
DYSYRDTSSS TIEDQRRGGG ISIIRFIFSS AAWLFSFVFE SSTPSENSLS NQQIDDDEDY
EDGDGDKKNG RTDSMTSTTK GRANTMPSTT RSQNNNNSQK QQKQSNGKSH HQHSSHQNNH
QKSNGNSNGH ARGFAAVRDS SHDTNASNET DIRSMSRELE SLRSEISSRR SQEEDFKLQV
SMHESNETRL SQQLSNMRLK VEQMEIKCSS IERHRESDKH QLEQAERKYA DLLGKKAEIE
ATLSAERKAR MEVTSKKYDV AEHQRERERQ LESEIDKLRI ELKSKDESNM RMESELHGLR
NYKEENDIDS LNMELRFVRD KSHQMEESLA GENKLKQSLF KCLGDARDTI KSLERRVQEF
QIKNGSSIGG GSSETLMNGR SSTEANNEND TTASDQSSPH QHSAMGSPVP FAKMPLSVNV
SNRHGSPFNG KVSPIASIGS VLAAAGGPAP PDYMMAVGAN VTATTGPVPQ KQPRAGFHGI
SRYNEFTNIA SGGEHRLFDT PASAISASAI NGSNPEDDFL MNKGKFGAPS QPAARLA
