PAN1_CAEEL
ID PAN1_CAEEL Reviewed; 594 AA.
AC Q9U3A0; Q21604; S6FWR2;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=P-granule-associated novel protein 1;
DE Flags: Precursor;
GN Name=pan-1 {ECO:0000312|WormBase:M88.6b};
GN ORFNames=M88.6 {ECO:0000312|WormBase:M88.6b};
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}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23682709; DOI=10.1186/1471-213x-13-21;
RA Gissendanner C.R., Kelley T.D.;
RT "The C. elegans gene pan-1 encodes novel transmembrane and cytoplasmic
RT leucine-rich repeat proteins and promotes molting and the larva to adult
RT transition.";
RL BMC Dev. Biol. 13:21-21(2013).
RN [2] {ECO:0000312|EMBL:CAB54282.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB54282.1};
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, INTERACTION WITH GLH-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22342905; DOI=10.1016/j.ydbio.2012.02.006;
RA Gao G., Deeb F., Mercurio J.M., Parfenova A., Smith P.A., Bennett K.L.;
RT "PAN-1, a P-granule component important for C. elegans fertility, has dual
RT roles in the germline and soma.";
RL Dev. Biol. 364:202-213(2012).
RN [4]
RP FUNCTION (ISOFORM B), INTERACTION WITH MYRF-1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=33950834; DOI=10.7554/elife.67628;
RA Xia S.L., Li M., Chen B., Wang C., Yan Y.H., Dong M.Q., Qi Y.B.;
RT "The LRR-TM protein PAN-1 interacts with MYRF to promote its nuclear
RT translocation in synaptic remodeling.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Regulates diverse developmental processes including larval
CC molting and gonad maturation. {ECO:0000269|PubMed:22342905,
CC ECO:0000269|PubMed:23682709}.
CC -!- FUNCTION: [Isoform b]: Promotes the localization of myrf-1 and myrf-2
CC to the cell membrane (PubMed:33950834). In association with myrf-1,
CC promotes the synaptic remodeling of DD GABAergic motor neurons whereby
CC new synapses form in the dorsal processes of DD neurons
CC (PubMed:33950834). {ECO:0000269|PubMed:33950834}.
CC -!- SUBUNIT: Interacts with glh-1 (PubMed:22342905). Interacts (via LRR
CC regions) with myrf-1 (via C-terminus); the interaction promotes the
CC role of myrf-1 in the synaptic remodeling of DD GABAergic motor neurons
CC at the cell membrane (PubMed:33950834). {ECO:0000269|PubMed:22342905,
CC ECO:0000269|PubMed:33950834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22342905,
CC ECO:0000269|PubMed:23682709, ECO:0000269|PubMed:33950834}. Apical cell
CC membrane {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709,
CC ECO:0000269|PubMed:33950834}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709}.
CC Note=Detected throughout the cytoplasm in germline and somatic
CC blastomeres during embryogenesis and in germline and somatic tissue in
CC adult hermaphrodites. Localizes to P-granules in L1 larval Z2 and Z3
CC germline precursor cells. Expression in P-granules is most pronounced
CC during the meiotic stage of the germline; in mature oocytes and sperm
CC expression switches to a cytoplasmic pattern.
CC {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:M88.6b}; Synonyms=pan-1b
CC {ECO:0000303|PubMed:33950834};
CC IsoId=Q9U3A0-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:M88.6a};
CC IsoId=Q9U3A0-2; Sequence=VSP_053556;
CC Name=c {ECO:0000312|WormBase:M88.6c};
CC IsoId=Q9U3A0-3; Sequence=VSP_053555;
CC -!- TISSUE SPECIFICITY: [Isoform a]: Expressed in the germline and somatic
CC cells (PubMed:22342905). {ECO:0000269|PubMed:22342905}.
CC -!- TISSUE SPECIFICITY: [Isoform b]: Expressed in the germline and somatic
CC cells (PubMed:22342905). Expressed at higher levels in germline cells
CC relative to somatic cells (PubMed:22342905).
CC {ECO:0000269|PubMed:22342905}.
CC -!- TISSUE SPECIFICITY: [Isoform c]: Expressed in germline cells
CC (PubMed:22342905). {ECO:0000269|PubMed:22342905}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the pharynx and at lower levels
CC in the intestine, but not detected in other tissues (PubMed:22342905).
CC Other studies suggest a broader expression pattern in somatic tissues:
CC from embryogenesis to adult stages, expressed strongly in body wall
CC muscle, vulva, somatic gonad and pharynx, at lower levels in the nerve
CC ring, hypodermis, and rectal epithelia, and very weakly in the
CC intestine (PubMed:23682709). {ECO:0000269|PubMed:22342905,
CC ECO:0000269|PubMed:23682709}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages from embryos
CC undergoing morphogenesis to gravid adults (PubMed:23682709). Broadly
CC expressed in embryos and early larvae, but expression decreases in late
CC larvae and adults (PubMed:33950834). Expressed in seam cells during
CC larval development (PubMed:33950834). Expressed in DD GABAergic motor
CC neurons in L1 and L2 stage larva (PubMed:33950834). During larval stage
CC L1, expressed in the pharynx and in intestinal cells (PubMed:22342905).
CC Expressed most strongly during mid-to-late intermolt periods (at
CC protein level) (PubMed:23682709). {ECO:0000269|PubMed:22342905,
CC ECO:0000269|PubMed:23682709, ECO:0000269|PubMed:33950834}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal. Animals developmentally arrest
CC prior to the first larval molt and subsequent growth is slow, although
CC larvae survive for up to 8 days at 20 degrees Celsius. Animals also
CC display uncoordinated locomotion, a shortened cuticle, pharyngeal
CC defects, stunted gonad development, and abnormal vulval morphogenesis.
CC Heterozygous worms have reduced brood sizes. Knockout in DD GABAergic
CC motor neurons results in defective synaptic remodeling of DD GABAergic
CC motor neurons (PubMed:33950834). RNAi-mediated knockdown in the
CC germline, results in sterility and gametogenesis phenotypes including
CC complete absence of oocytes, endomitotically replicating oocytes, and
CC failure to lay eggs. Animals surviving to the L4 stage have hypodermal
CC defects including lack of lateral alae and incomplete seam cell fusion,
CC and fail to express col-19 and mlt-10. RNAi-mediated knockdown in lin-
CC 29 null mutants results in partial suppression of the molting and
CC vulval RNAi phenotypes in L4 stage larvae.
CC {ECO:0000269|PubMed:22342905, ECO:0000269|PubMed:23682709,
CC ECO:0000269|PubMed:33950834}.
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DR EMBL; BX284603; CAA84337.2; -; Genomic_DNA.
DR EMBL; BX284603; CAB54282.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24160.1; -; Genomic_DNA.
DR PIR; T23841; T23841.
DR RefSeq; NP_001293622.1; NM_001306693.1. [Q9U3A0-3]
DR RefSeq; NP_497924.2; NM_065523.6. [Q9U3A0-2]
DR RefSeq; NP_497925.1; NM_065524.3. [Q9U3A0-1]
DR AlphaFoldDB; Q9U3A0; -.
DR SMR; Q9U3A0; -.
DR BioGRID; 40832; 5.
DR STRING; 6239.M88.6b; -.
DR TCDB; 8.A.43.1.26; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR EPD; Q9U3A0; -.
DR PaxDb; Q9U3A0; -.
DR EnsemblMetazoa; M88.6a.1; M88.6a.1; WBGene00003915. [Q9U3A0-2]
DR EnsemblMetazoa; M88.6b.1; M88.6b.1; WBGene00003915. [Q9U3A0-1]
DR EnsemblMetazoa; M88.6c.1; M88.6c.1; WBGene00003915. [Q9U3A0-3]
DR GeneID; 175596; -.
DR KEGG; cel:CELE_M88.6; -.
DR UCSC; M88.6b; c. elegans.
DR CTD; 175596; -.
DR WormBase; M88.6a; CE47659; WBGene00003915; pan-1. [Q9U3A0-2]
DR WormBase; M88.6b; CE23886; WBGene00003915; pan-1. [Q9U3A0-1]
DR WormBase; M88.6c; CE48435; WBGene00003915; pan-1. [Q9U3A0-3]
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_029738_0_0_1; -.
DR InParanoid; Q9U3A0; -.
DR OMA; SKLWIWD; -.
DR OrthoDB; 727078at2759; -.
DR PhylomeDB; Q9U3A0; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q9U3A0; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003915; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 4.
DR SMART; SM00369; LRR_TYP; 11.
DR PROSITE; PS51450; LRR; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..594
FT /note="P-granule-associated novel protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424891"
FT TOPO_DOM 19..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 78..101
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 103..124
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 125..149
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 150..173
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 175..197
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 198..221
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 222..245
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 246..269
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 271..290
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 291..315
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 318..341
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 343..365
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 374..397
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 399..419
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 420..442
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..502
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053555"
FT VAR_SEQ 1..309
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_053556"
SQ SEQUENCE 594 AA; 66371 MW; B73452578EEFAFBF CRC64;
MRSLLSFVLL ALARIAISEE TKSCIDIEKG FKEEFNAHKQ PVCICADNGI FSTVKGFTIE
CESASIASVS ENLASLNGTE LGRLTIRDST VNVLPQDLFE NVFAKQVKLE RCGLSTLQPN
SFQSLGGSAE LLSLRENRIK KLEKGLFTGL KSLKTLDLAM NKIQEIDVGA FEELKKVEEL
LLNENDIRVL KTGTFDGMKN LKKLTLQNCN LEIIQKGAFR GLNSLEQLIL SNNNLENIDW
TIFSALKNLR VLDLGSNKIS NVEMKSFPKL EKLVLNNNTI DSMKSIKLKD LPSLVVALFD
RNKIESIGDM DMFGLTRSDR IETLSLARNN LSQISPKAFQ HTPNLITLLL QYNQIEELSS
HSPSQVRTPF LASLKKLVTL QLSSNNLSVI RSDELPKSLS SLALDHNVIS KIEARALEGM
EIKRLYLHSN KLNYLYQGTF DSFSPKSVEA VDVSLNPWVC VCNDPKEWLP RWLEASEEAD
VAEGALGCLA IPNCGQKEGS TVMPEEEEVY RSGWITVAAT ILTIVTIVIM VIIAMLYFKD
ARYQFPLRGR RSDSDLHKLI ENDPLNIASD SILVVPAMPK RNTGPKKTVR FQNF
