CUT5_CAEEL
ID CUT5_CAEEL Reviewed; 395 AA.
AC Q21808; D0VWM7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cuticlin-5 {ECO:0000312|WormBase:R07E3.3a};
DE Flags: Precursor;
GN Name=cut-5 {ECO:0000312|WormBase:R07E3.3a};
GN ORFNames=R07E3.3 {ECO:0000312|WormBase:R07E3.3a};
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=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 [3] {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 L1 and dauer stage larvae.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:R07E3.3a};
CC IsoId=Q21808-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R07E3.3b};
CC IsoId=Q21808-2; Sequence=VSP_060615;
CC -!- DEVELOPMENTAL STAGE: Expressed in seam cells in three-fold stage
CC embryos and during dauer larvae formation (PubMed:15936343). Not
CC expressed in adults (PubMed:15936343). {ECO:0000269|PubMed:15936343}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in disrupted alae
CC formation in L1 and dauer stage larvae with alae often present on only
CC one side of the larvae. {ECO:0000269|PubMed:15936343}.
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DR EMBL; BX284606; CAA89068.3; -; Genomic_DNA.
DR EMBL; BX284606; CBH29667.1; -; Genomic_DNA.
DR RefSeq; NP_001257099.1; NM_001270170.1. [Q21808-2]
DR RefSeq; NP_001257100.1; NM_001270171.1. [Q21808-1]
DR AlphaFoldDB; Q21808; -.
DR DIP; DIP-27317N; -.
DR STRING; 6239.R07E3.3a; -.
DR PaxDb; Q21808; -.
DR EnsemblMetazoa; R07E3.3a.1; R07E3.3a.1; WBGene00011104. [Q21808-1]
DR EnsemblMetazoa; R07E3.3b.1; R07E3.3b.1; WBGene00011104. [Q21808-2]
DR GeneID; 187677; -.
DR KEGG; cel:CELE_R07E3.3; -.
DR UCSC; R07E3.3; c. elegans. [Q21808-1]
DR CTD; 187677; -.
DR WormBase; R07E3.3a; CE42566; WBGene00011104; cut-5. [Q21808-1]
DR WormBase; R07E3.3b; CE40396; WBGene00011104; cut-5. [Q21808-2]
DR eggNOG; ENOG502QUTR; Eukaryota.
DR GeneTree; ENSGT00940000163650; -.
DR HOGENOM; CLU_037896_3_0_1; -.
DR InParanoid; Q21808; -.
DR OMA; QMVYHKW; -.
DR OrthoDB; 877658at2759; -.
DR PhylomeDB; Q21808; -.
DR PRO; PR:Q21808; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00011104; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; Q21808; baseline and differential.
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 InterPro; IPR001507; ZP_dom.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cuticle; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..395
FT /note="Cuticlin-5"
FT /id="PRO_5004199434"
FT TOPO_DOM 19..358
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 46..291
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 39..54
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060615"
SQ SEQUENCE 395 AA; 44884 MW; 2AA8C4103B27B1D6 CRC64;
MNFILAVFAI ILLQAVRGEI DNAIVGDPSV ECGDDFFEVN IYHSCSCVGN FIIKVKFDTR
TTFHGLAFVQ NHLDNPDCRS FASKTDSAKN SSLRLTFDQC AIEKRHSTSP RGLFLSTNVV
VAFNPEFLTK NDRVFKVQCF YMEMERRIQK VIQISMPPPT MHSKQLNMPV CKYEVLDGSP
TGPPVYFATV GQMVYHKWTC DTEHENTFCM LVHSCFVDDG NGQRVQLLND KGCALDKYLL
TNLEYPTDLM AGREAHVYKY ADRDNMYFDC QISITVKEPG LDYCDVPSCP DPPRRRRSNT
LPAPDDNITA IAAHIEYEDS EIISDYIIPN DDIISLNWLQ RNFDMRISEL CMTAIGTTLL
VFLNAFLFII SLVSIVHVCC FRTSPKLEKT KSTML
