PHM2_CAEEL
ID PHM2_CAEEL Reviewed; 1073 AA.
AC O62203; F5GUF6; Q7Z0X2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Pharyngeal muscle protein 2 {ECO:0000312|WormBase:F32B4.4a};
GN Name=phm-2 {ECO:0000312|WormBase:F32B4.4a};
GN ORFNames=F32B4.4 {ECO:0000312|WormBase:F32B4.4a};
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, AND DISRUPTION PHENOTYPE.
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 [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 44-ARG--TYR-1073.
RX PubMed=21750263; DOI=10.1534/genetics.111.130450;
RA Hughes S.E., Huang C., Kornfeld K.;
RT "Identification of mutations that delay somatic or reproductive aging of
RT Caenorhabditis elegans.";
RL Genetics 189:341-356(2011).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 44-ARG--TYR-1073.
RX PubMed=30965033; DOI=10.1016/j.devcel.2019.03.010;
RA Kumar S., Egan B.M., Kocsisova Z., Schneider D.L., Murphy J.T., Diwan A.,
RA Kornfeld K.;
RT "Lifespan extension in C. elegans caused by bacterial colonization of the
RT intestine and subsequent activation of an innate immune response.";
RL Dev. Cell 49:100-117(2019).
CC -!- FUNCTION: Involved in pharyngeal muscle development and ensures
CC pharyngeal grinder function during feeding (PubMed:8462849,
CC PubMed:21750263, PubMed:30965033). Plays a role in the defense against
CC the accumulation of ingested live pathogenic bacteria in the intestine
CC (PubMed:30965033). Has a role in the determination of life span
CC (PubMed:30965033). {ECO:0000269|PubMed:21750263,
CC ECO:0000269|PubMed:30965033, ECO:0000269|PubMed:8462849}.
CC -!- INTERACTION:
CC O62203; Q10929: abi-1; NbExp=6; IntAct=EBI-320780, EBI-315750;
CC O62203; G5EC32: sorb-1; NbExp=7; IntAct=EBI-320780, EBI-325337;
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Nucleus
CC {ECO:0000269|PubMed:30965033}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F32B4.4a};
CC IsoId=O62203-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F32B4.4b};
CC IsoId=O62203-2; Sequence=VSP_060473;
CC Name=c {ECO:0000312|WormBase:F32B4.4c};
CC IsoId=O62203-3; Sequence=VSP_060472;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues including the hypodermal,
CC muscle, neuronal, vulval and intestinal tissues (PubMed:30965033).
CC Isoform a: Expressed in the pharynx, nerve ring, intestine, neurons and
CC ventral nerve cord (PubMed:30965033). {ECO:0000269|PubMed:30965033}.
CC -!- DISRUPTION PHENOTYPE: Viable, but have an extended lifespan
CC (PubMed:30965033). There is a decrease in early progeny production,
CC resulting in smaller self-fertile brood size, and an increase in late
CC progeny production, which results in an extended self-fertile
CC reproductive lifespan (PubMed:30965033). Defective pharyngeal grinder
CC positioning, which results in feeding defects (PubMed:8462849). Animals
CC also have protruding male spicules (PubMed:8462849).
CC {ECO:0000269|PubMed:30965033, ECO:0000269|PubMed:8462849}.
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DR EMBL; BX284601; CAB04233.3; -; Genomic_DNA.
DR EMBL; BX284601; CAD98731.1; -; Genomic_DNA.
DR EMBL; BX284601; CCA65561.1; -; Genomic_DNA.
DR RefSeq; NP_001021440.2; NM_001026269.2. [O62203-1]
DR RefSeq; NP_001021441.1; NM_001026270.3.
DR RefSeq; NP_001251667.1; NM_001264738.1. [O62203-3]
DR AlphaFoldDB; O62203; -.
DR SMR; O62203; -.
DR DIP; DIP-25849N; -.
DR IntAct; O62203; 18.
DR STRING; 6239.F32B4.4a; -.
DR EPD; O62203; -.
DR PaxDb; O62203; -.
DR PeptideAtlas; O62203; -.
DR EnsemblMetazoa; F32B4.4a.1; F32B4.4a.1; WBGene00009314. [O62203-1]
DR EnsemblMetazoa; F32B4.4b.1; F32B4.4b.1; WBGene00009314. [O62203-2]
DR EnsemblMetazoa; F32B4.4b.2; F32B4.4b.2; WBGene00009314. [O62203-2]
DR EnsemblMetazoa; F32B4.4b.3; F32B4.4b.3; WBGene00009314. [O62203-2]
DR EnsemblMetazoa; F32B4.4c.1; F32B4.4c.1; WBGene00009314. [O62203-3]
DR GeneID; 185193; -.
DR KEGG; cel:CELE_F32B4.4; -.
DR UCSC; F32B4.4b.1; c. elegans.
DR CTD; 185193; -.
DR WormBase; F32B4.4a; CE46007; WBGene00009314; phm-2. [O62203-1]
DR WormBase; F32B4.4b; CE34301; WBGene00009314; phm-2. [O62203-2]
DR WormBase; F32B4.4c; CE46087; WBGene00009314; phm-2. [O62203-3]
DR eggNOG; KOG4661; Eukaryota.
DR GeneTree; ENSGT00940000175782; -.
DR HOGENOM; CLU_287330_0_0_1; -.
DR InParanoid; O62203; -.
DR OMA; RASYQTE; -.
DR OrthoDB; 1582842at2759; -.
DR SignaLink; O62203; -.
DR PRO; PR:O62203; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009314; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Digestion; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..1073
FT /note="Pharyngeal muscle protein 2"
FT /id="PRO_0000448940"
FT DOMAIN 9..43
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 396..478
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 59..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060472"
FT VAR_SEQ 2..413
FT /note="PLESGKLINDLRVSELKTELEKRGLSTQGVKVVLTVRLNKALRDEGLDPADH
FT VFEHAVSPMKKSTRRSNEMARAAAAAAAEKVEKGAGDEGNDENVLVEEKEEEEEEEDSH
FT DLQIIEDHELEVPSDEKDDTLVEDEEFEEAEQVEPEPEAVEPVVEEKPEEKLEEKPEEK
FT LEEKPEEKPVEPEVVTVEEPVAEVIEVEKAVAEPVELKEKPEKEPEVVLVEEPVEQLEN
FT EPEVVPMEVEEAKKSDEQDGEDEFEEDDSSSDIEIIEPTLQESEPLAEEKVEKKEKKPE
FT EIPHNLEQNEPISMETEEKVEEEVIILNSSINNVSQDDEIVLDYEEDLLEDPLDEPIEQ
FT KEPKAAEPTPKQLQKVEASTPQATPSKAASSSAGSGKSMLFGDDVKKTSIWIRGMTPAT
FT KASSVK -> RM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060473"
FT MUTAGEN 44..1073
FT /note="Missing: In am117; extended lifespan, decrease in
FT early progeny production, resulting in smaller self-fertile
FT brood size, and an increase in late progeny production,
FT which results in an extended self-fertile reproductive
FT lifespan. Increased movement characterized by an increased
FT number of body bends per minute. Animals are thinner and
FT smaller with a reduced body volume (also known as a scrawny
FT phenotype), and this is most likely due to heightened
FT bacteria avoidance behavior and impaired food digestion.
FT Older animals exhibit increased pharyngeal pumping.
FT Abnormal pharyngeal grinder morphology and defective
FT function results in the accumulation of pathogenic
FT bacteria, such as E.coli, in the intestine. Accumulation of
FT the transcription factor hlh-30 in the nucleus following
FT exposure to E.coli, which likely leads to increased
FT expression of pathogen response genes including clec-7,
FT clec-60 and clec-82. Reduced survival following exposure to
FT Gram-negative bacteria P.aeruginosa."
FT /evidence="ECO:0000269|PubMed:21750263,
FT ECO:0000269|PubMed:30965033"
SQ SEQUENCE 1073 AA; 117885 MW; 165FB3262A9C44C0 CRC64;
MPLESGKLIN DLRVSELKTE LEKRGLSTQG VKVVLTVRLN KALRDEGLDP ADHVFEHAVS
PMKKSTRRSN EMARAAAAAA AEKVEKGAGD EGNDENVLVE EKEEEEEEED SHDLQIIEDH
ELEVPSDEKD DTLVEDEEFE EAEQVEPEPE AVEPVVEEKP EEKLEEKPEE KLEEKPEEKP
VEPEVVTVEE PVAEVIEVEK AVAEPVELKE KPEKEPEVVL VEEPVEQLEN EPEVVPMEVE
EAKKSDEQDG EDEFEEDDSS SDIEIIEPTL QESEPLAEEK VEKKEKKPEE IPHNLEQNEP
ISMETEEKVE EEVIILNSSI NNVSQDDEIV LDYEEDLLED PLDEPIEQKE PKAAEPTPKQ
LQKVEASTPQ ATPSKAASSS AGSGKSMLFG DDVKKTSIWI RGMTPATKAS SVKQLASQYG
KVIQSKIFNS KAADANGDVK NCFALIQFAD VTAMELAMTS LHQKNYQGRV LRVEKVSESH
LTSSAEKLAR EKHVAEAAST MSTSPAPTPT PEPVVTTTTT TSAAPKRKEP IHAPESSSSE
GQRAKRRAIE APVRSRSRSR GGGGEPRSSR KPITFDREEE SNRDSRRTIA AAPPARTSRM
ARSPLRAPLR AARGSESSRS STRGGGGGGE SLTISSRVDT SGCRGGAIKR SVERSVPNNI
STSELRRKHH QIHVTVQQDA PRASYQTEQY ARERSSSTTT SSRRRQVSPD RSEQRRHRDE
PPPRRAPQEQ PSRRRGASPP EPPRRQEGAR RSEEPERRRL FDEREQLAHI MAAKDMYAEQ
QKIRAEKALI AFQMQQLEKK KLEAELQIAQ KALLMQQAAL GGGGALVVDG GALVAGGGAV
GYHHQEHRSS YGGGGSSSNG GSSNRRRQTR RSPSPPQQHH SSSRRQRRDS GGAGRYRQST
SSSNSNRNSN SGGRNLVVTA TTTNNTNATN AGRSYGIQSV PDASSYSTNN YQQRSSAASA
YDLQITATMP QAGAANSGAA YHQPYGNVYQ HNTAAYPVWG GLDAQGHMAM DTNWSQNAAT
PSTSTSSGGG GGQQWQQQSY GSNQHQHHQN NNSSQPSSSN RRGNDYGNYR GNY
