ID   CUT4_CAEEL              Reviewed;         507 AA.
AC   Q19053;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Cuticlin-4 {ECO:0000312|WormBase:E04D5.3};
DE   Flags: Precursor;
GN   Name=cut-4 {ECO:0000312|WormBase:E04D5.3};
GN   ORFNames=E04D5.3 {ECO:0000312|WormBase:E04D5.3};
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 and subsequent cuticle
CC       attachment in adults. {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 adults.
CC       {ECO:0000269|PubMed:15936343}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in cuticle
CC       defects in adults, where the external and internal cuticle under the
CC       alae are detached (PubMed:15936343). In addition, alae are present, but
CC       they are shallower and often have two or four ridges rather than the
CC       three in adult wild-type animals (PubMed:15936343).
CC       {ECO:0000269|PubMed:15936343}.
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DR   EMBL; BX284602; CAA91280.2; -; Genomic_DNA.
DR   PIR; T20451; T20451.
DR   RefSeq; NP_496242.2; NM_063841.2.
DR   AlphaFoldDB; Q19053; -.
DR   SMR; Q19053; -.
DR   STRING; 6239.E04D5.3; -.
DR   EPD; Q19053; -.
DR   PaxDb; Q19053; -.
DR   EnsemblMetazoa; E04D5.3.1; E04D5.3.1; WBGene00008482.
DR   GeneID; 184037; -.
DR   KEGG; cel:CELE_E04D5.3; -.
DR   UCSC; E04D5.3; c. elegans.
DR   CTD; 184037; -.
DR   WormBase; E04D5.3; CE37892; WBGene00008482; cut-4.
DR   eggNOG; ENOG502RXCC; Eukaryota.
DR   GeneTree; ENSGT00940000163650; -.
DR   HOGENOM; CLU_037896_1_0_1; -.
DR   InParanoid; Q19053; -.
DR   OMA; ESGYPTR; -.
DR   OrthoDB; 877658at2759; -.
DR   PhylomeDB; Q19053; -.
DR   PRO; PR:Q19053; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00008482; Expressed in larva and 2 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   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   CHAIN           20..507
FT                   /note="Cuticlin-4"
FT                   /id="PRO_5004187096"
FT   TOPO_DOM        20..471
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..507
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          42..280
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   REGION          292..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   507 AA;  55846 MW;  C5366483937EC8CE CRC64;
     MFHFTRILAA FLLPTLCFCG YSTAPSSTVS IDNSLIGEPE VVCETASISL LFKTRNSFNG
     KVFVKGYVSE PSCMTVGDGK TGHRFEVRHD SCGVRRQREI NGVVISATVI ISFHSIFITK
     IDRAYRVSCF YVEGTKKVHN HVDISALTTQ LLESETQLPV CRYEILNEAG GSPIKYARIG
     DQVYHKWTCV AELENVYCMK VHSCTVYDGQ GGPPVTVIDA NGCSVDGVIL QNLEYTSDLT
     AGKLAPVFKF ADKAGLYFNC QIQLTIKDVN YGCSNTQPQC PTSQYVVEPA QKTTETAEPY
     PYDSHESGYP TRPANYPVAS SRYPIPTTQA PASYPSSPAP PPPGADIDNG YPEPQPIYIA
     ETPENAYDGI VGFNDTEQPF TTSAAYTEDG VYSRLIKRNV VESTEQINAS NKKRPVTVGD
     IDLPERGILV FGLEEMEDGE TTNAGDHGAT RALREARNSQ EKTCFSTSRM YFTLILLCLL
     FATTVVVFIV IVQKQRQILA QTAFFKP