CUT6_CAEEL
ID CUT6_CAEEL Reviewed; 572 AA.
AC Q21540;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cuticlin-6 {ECO:0000312|WormBase:M142.2};
DE AltName: Full=Cuticulin 6 {ECO:0000303|PubMed:12921736};
DE Flags: Precursor;
GN Name=cut-6 {ECO:0000303|PubMed:12921736, ECO:0000312|WormBase:M142.2};
GN ORFNames=M142.2 {ECO:0000312|WormBase:M142.2};
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12921736; DOI=10.1016/s0012-1606(03)00237-9;
RA Muriel J.M., Brannan M., Taylor K., Johnstone I.L., Lithgow G.J.,
RA Tuckwell D.;
RT "M142.2 (cut-6), a novel Caenorhabditis elegans matrix gene important for
RT dauer body shape.";
RL Dev. Biol. 260:339-351(2003).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15936343; DOI=10.1016/j.ydbio.2005.03.011;
RA Sapio M.R., Hilliard M.A., Cermola M., Favre R., Bazzicalupo P.;
RT "The Zona Pellucida domain containing proteins, CUT-1, CUT-3 and CUT-5,
RT play essential roles in the development of the larval alae in
RT Caenorhabditis elegans.";
RL Dev. Biol. 282:231-245(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=30409788; DOI=10.1534/genetics.118.301557;
RA Flatt K.M., Beshers C., Unal C., Cohen J.D., Sundaram M.V., Schroeder N.E.;
RT "Epidermal Remodeling in Caenorhabditis elegans Dauers Requires the Nidogen
RT Domain Protein DEX-1.";
RL Genetics 211:169-183(2019).
CC -!- FUNCTION: Plays a role in alae formation in dauer larvae probably by
CC regulating cuticle assembly. {ECO:0000269|PubMed:12921736,
CC ECO:0000269|PubMed:15936343, ECO:0000269|PubMed:30409788}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late embryos (PubMed:12921736). At
CC the L1 larval stage and during the dauer stages, it is expressed
CC adjacent to the lateral edges of the alae (at protein level)
CC (PubMed:12921736). In the L2 pre-dauer stage, expressed in the head
CC hypodermal cells hyp3, hyp4, hyp5, hyp6 and hyp7, along the main body
CC and in tail hyp8, hyp9, hyp10 and hyp11 (PubMed:12921736). Not
CC expressed at adult stages (at protein level) (PubMed:12921736).
CC {ECO:0000269|PubMed:12921736}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in shorter and
CC fatter dauer phase animals (dumpy phenotype) (PubMed:12921736,
CC PubMed:15936343). RNAi-mediated knockdown results in a folded pharynx
CC in some animals (PubMed:12921736). RNAi-mediated knockdown results in
CC no alae formation (PubMed:12921736). However, other studies indicate
CC that RNAi-mediated knockdown results in partially formed alae
CC (PubMed:15936343). {ECO:0000269|PubMed:12921736,
CC ECO:0000269|PubMed:15936343}.
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DR EMBL; BX284603; CAA97806.2; -; Genomic_DNA.
DR PIR; T23760; T23760.
DR RefSeq; NP_499400.2; NM_066999.5.
DR AlphaFoldDB; Q21540; -.
DR SMR; Q21540; -.
DR STRING; 6239.M142.2.2; -.
DR EPD; Q21540; -.
DR PaxDb; Q21540; -.
DR EnsemblMetazoa; M142.2.1; M142.2.1; WBGene00000853.
DR GeneID; 176520; -.
DR KEGG; cel:CELE_M142.2; -.
DR UCSC; M142.2.1; c. elegans.
DR CTD; 176520; -.
DR WormBase; M142.2; CE35746; WBGene00000853; cut-6.
DR eggNOG; KOG1217; Eukaryota.
DR HOGENOM; CLU_473470_0_0_1; -.
DR InParanoid; Q21540; -.
DR OMA; HTLFMTK; -.
DR OrthoDB; 877658at2759; -.
DR PhylomeDB; Q21540; -.
DR PRO; PR:Q21540; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000853; Expressed in embryo and 3 other tissues.
DR GO; GO:0060111; C:alae of collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00327; VWA; 1.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cuticle; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..572
FT /note="Cuticlin-6"
FT /id="PRO_5004199393"
FT TOPO_DOM 25..541
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 47..216
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 233..479
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 572 AA; 64132 MW; E653C6335EC5F144 CRC64;
MRPIPYDISL SITSFLSLIL ICSANPIDNG LVDSELIHEC VTHKAVEVIL LLDASGSIGD
DTFKKQLSFA MHLASRLNIS EDGSHMALIQ YAETPKLEFS LGQFNHPTQL EWAIQRIEYQ
SGATNTGQAL RLTLEKGLQG ARPGIPKVAI VITDGQSQDD VSEPSQLLRD ADVMVYAIGV
TNLVNVHQLH QMTGNPVRVF TVESFEQLDR ALADSLTWSM CKTEFRPGTP EIICGPDRIG
VKASTKQPFE GNVFVMDHYH DEECRAGPEK FPDSRSIGLT VPFSACNVHR YRSLNPKGIF
VEVSIVFMFH SLFMTKTDQT VKVQCFYMEA DKHVTVPLSV SMITTVFREQ IYQMPQCAYT
LRKGAPDGPI VRFATLGESV YHRWECIEVE GADKDTFGML VHSCYVDNGY GDRVDILDSN
GCGLDAVLLS TPDYDTSLRL ATKPYHVFKY ADRPVLQFQC QITLCLKYDG GCEGITPPQN
CKKLPGEDGH HHHHHPEKRR KLVRRLADGV GTIDVFTDSV TVLEQEPACQ QPLPYPLINT
NLWIMGIITL TNIFVFILTV WFTFRKRRCK PA
