ID   CUT3_CAEEL              Reviewed;         389 AA.
AC   Q19707;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Cuticlin-3 {ECO:0000312|WormBase:F22B5.3};
DE   Flags: Precursor;
GN   Name=cut-3 {ECO:0000312|WormBase:F22B5.3};
GN   ORFNames=F22B5.3 {ECO:0000312|WormBase:F22B5.3};
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).
CC   -!- FUNCTION: Plays a role in alae formation in L1 larvae.
CC       {ECO:0000269|PubMed:15936343}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Only expressed in late embryos.
CC       {ECO:0000269|PubMed:15936343}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in shorter and
CC       fatter dauer phase animals (dumpy phenotype), which have no alae
CC       (PubMed:15936343). RNAi-mediated knockdown results in a folded pharynx
CC       and intestine in some animals (PubMed:15936343).
CC       {ECO:0000269|PubMed:15936343}.
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DR   EMBL; BX284602; CAA90355.1; -; Genomic_DNA.
DR   PIR; T21239; T21239.
DR   RefSeq; NP_495780.1; NM_063379.5.
DR   AlphaFoldDB; Q19707; -.
DR   SMR; Q19707; -.
DR   DIP; DIP-24862N; -.
DR   IntAct; Q19707; 1.
DR   STRING; 6239.F22B5.3; -.
DR   EPD; Q19707; -.
DR   PaxDb; Q19707; -.
DR   PeptideAtlas; Q19707; -.
DR   EnsemblMetazoa; F22B5.3.1; F22B5.3.1; WBGene00009041.
DR   GeneID; 174347; -.
DR   KEGG; cel:CELE_F22B5.3; -.
DR   UCSC; F22B5.3; c. elegans.
DR   CTD; 174347; -.
DR   WormBase; F22B5.3; CE02198; WBGene00009041; cut-3.
DR   eggNOG; ENOG502QV41; Eukaryota.
DR   GeneTree; ENSGT00940000163650; -.
DR   HOGENOM; CLU_037896_1_1_1; -.
DR   InParanoid; Q19707; -.
DR   OMA; LFDQQEC; -.
DR   OrthoDB; 877658at2759; -.
DR   PhylomeDB; Q19707; -.
DR   PRO; PR:Q19707; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00009041; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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   Pfam; PF00100; Zona_pellucida; 1.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cuticle; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..389
FT                   /note="Cuticlin-3"
FT                   /id="PRO_5004187366"
FT   TOPO_DOM        20..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          33..278
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   389 AA;  42983 MW;  40BAB9C5CE031BB5 CRC64;
     MARYSLGLGL CLLVASVSAI PVDNNVEGEP EVECGPTSIT VNFNTRNAFE GHVYVKGLFD
     QQECRNDEGG RQVAGIELPF DTCNVARTRS LNPKGVFVTT TVVVSFHPQF VTKVDRAYRV
     QCFYMEADKT VSTQIEVSDL TTAFQTQVVP MPICKYEILN GGPTGEPVQF ATIGQQVYHK
     WTCDSETVDT FCAVVHSCTV DDGNGDTVQI LDENGCALDK FLLNNLEYPT DLMAGQEAHV
     YKYADRSQLF YQCQISITVK EPNEECARPT CSEPQGFGAV KQANQTAQFF RVLKKRSAPV
     MENILDVRAE LTTLEVLEGN LPSSLTQAQA LVASREIGED SFRQELCISS FHISVVTVFL
     GLTVFVAIFI TYMIVSRMMV PSDKMQSAC