DYF7_CAEEL
ID DYF7_CAEEL Reviewed; 446 AA.
AC Q09276;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein dyf-7 {ECO:0000305};
DE AltName: Full=Abnormal dye filling protein 7 {ECO:0000312|WormBase:C43C3.3};
DE Flags: Precursor;
GN Name=dyf-7 {ECO:0000312|WormBase:C43C3.3};
GN ORFNames=C43C3.3 {ECO:0000312|WormBase:C43C3.3};
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].
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 GENE NAME, AND FUNCTION.
RX PubMed=7705621; DOI=10.1093/genetics/139.1.171;
RA Starich T.A., Herman R.K., Kari C.K., Yeh W.H., Schackwitz W.S.,
RA Schuyler M.W., Collet J., Thomas J.H., Riddle D.L.;
RT "Mutations affecting the chemosensory neurons of Caenorhabditis elegans.";
RL Genetics 139:171-188(1995).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF VAL-52; PRO-107; VAL-191; GLU-217 AND GLY-394.
RX PubMed=19344940; DOI=10.1016/j.cell.2009.01.057;
RA Heiman M.G., Shaham S.;
RT "DEX-1 and DYF-7 establish sensory dendrite length by anchoring dendritic
RT tips during cell migration.";
RL Cell 137:344-355(2009).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF PRO-107.
RX PubMed=34115759; DOI=10.1371/journal.pgen.1009618;
RA Hong H., Chen H., Zhang Y., Wu Z., Zhang Y., Zhang Y., Hu Z., Zhang J.V.,
RA Ling K., Hu J., Wei Q.;
RT "DYF-4 regulates patched-related/DAF-6-mediated sensory compartment
RT formation in C. elegans.";
RL PLoS Genet. 17:e1009618-e1009618(2021).
CC -!- FUNCTION: Required for permeability of amphid and phasmid neurons to
CC external dyes, chemotaxis to ammonium chloride, avoidance of high
CC osmotic stimuli, male mating and dauer formation (PubMed:7705621).
CC Along with dex-1, enables neurite growth and maintenance by anchoring
CC amphid dendritic tips during neuron cell body migration in embryonic
CC and larval development (PubMed:19344940, PubMed:34115759).
CC {ECO:0000269|PubMed:19344940, ECO:0000269|PubMed:34115759,
CC ECO:0000269|PubMed:7705621}.
CC -!- SUBUNIT: Monomer under reducing conditions. Homodimer under non-
CC reducing conditions. May also form higher order oligomers.
CC {ECO:0000269|PubMed:19344940}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19344940};
CC Single-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19344940}. Secreted {ECO:0000269|PubMed:19344940}.
CC Note=Located at dendritic tips. Secreted following proteolytic cleavage
CC in vitro. {ECO:0000269|PubMed:19344940}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in the excretory cell and,
CC during dendrite formation, in the non-neuronal cells surrounding the
CC sensory neurons, including hypodermal cells.
CC {ECO:0000269|PubMed:19344940}.
CC -!- DEVELOPMENTAL STAGE: Expression is first apparent in bean-stage
CC embryos, peaks in late embryogenesis, reduces in L1 larvae and is
CC negligible in later larval stages and adults.
CC {ECO:0000269|PubMed:19344940}.
CC -!- PTM: Proteolytically cleaved and secreted in vitro.
CC {ECO:0000269|PubMed:19344940}.
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DR EMBL; BX284606; CAA87330.2; -; Genomic_DNA.
DR PIR; B89614; B89614.
DR PIR; T19902; T19902.
DR RefSeq; NP_509630.1; NM_077229.4.
DR AlphaFoldDB; Q09276; -.
DR BioGRID; 46099; 1.
DR STRING; 6239.C43C3.3; -.
DR EPD; Q09276; -.
DR PaxDb; Q09276; -.
DR PeptideAtlas; Q09276; -.
DR EnsemblMetazoa; C43C3.3.1; C43C3.3.1; WBGene00001123.
DR GeneID; 181183; -.
DR UCSC; C43C3.3; c. elegans.
DR CTD; 181183; -.
DR WormBase; C43C3.3; CE23591; WBGene00001123; dyf-7.
DR eggNOG; ENOG502S06H; Eukaryota.
DR HOGENOM; CLU_618620_0_0_1; -.
DR InParanoid; Q09276; -.
DR OMA; TIRFNDI; -.
DR OrthoDB; 682275at2759; -.
DR PRO; PR:Q09276; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001123; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0032590; C:dendrite membrane; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:WormBase.
DR GO; GO:0003391; P:amphid sensory organ dendrite retrograde extension; IMP:WormBase.
DR GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00100; Zona_pellucida; 1.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; Membrane; Neurogenesis;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..446
FT /note="Protein dyf-7"
FT /evidence="ECO:0000305"
FT /id="PRO_0000067427"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..295
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT DISULFID 211..273
FT /evidence="ECO:0000250"
FT MUTAGEN 52
FT /note="V->E: In ns120; results in defective neurite
FT extension."
FT /evidence="ECO:0000269|PubMed:19344940"
FT MUTAGEN 107
FT /note="P->S: In ns117; results in defective neurite
FT extension. The dendrite extension defect is suppressed in a
FT wsp-1 gm324 mutant background."
FT /evidence="ECO:0000269|PubMed:19344940,
FT ECO:0000269|PubMed:34115759"
FT MUTAGEN 191
FT /note="V->D: In ns116; results in defective neurite
FT extension."
FT /evidence="ECO:0000269|PubMed:19344940"
FT MUTAGEN 217
FT /note="E->K: In ns88; results in defective neurite
FT extension."
FT /evidence="ECO:0000269|PubMed:19344940"
FT MUTAGEN 394
FT /note="G->D: In ns118; results in defective neurite
FT extension."
FT /evidence="ECO:0000269|PubMed:19344940"
SQ SEQUENCE 446 AA; 49954 MW; ACC4B69B30032D84 CRC64;
MNQLWRASCL QVLITFLLIH QNKASEKDRF VELVDCIADS FTVVLNKSDP EVMRMISNPK
SQPVVYVYGH KTRHPCGTSM KDEKGLTNFN LTIPYGSECD VTLTDLPKHR YAETTVVLED
NADLSFGKTT RLNHVFCLYT RNVKTIRFSD VSNGHEVIAS TGGKPKPKVE MLFRSTDSGK
TLQAARENEF VEFFIALSPD SAYHGISPKE CTFSDREDIS APDAKKITFV QGGCPVNGMN
DIIDPLANVN DQIYFSKFRT FRFGNQSTVF VHCQVQVCLK KDECSKTCYK KVSDSNLTAE
RLRFRHKRSI TDLERRTTRS APTDDNGSLD LTNSLTVVSR IESAELVASP ISQPTIVDTP
SEQRRDPCPK SSNMGFIPLI IMGSLASLLL FSAGAAIYFG CKLKSMKKKD SFDMMSAFSN
PTVSMPVTYS HYQRSAYNAS VDSLYR
