CUT1_CAEEL
ID CUT1_CAEEL Reviewed; 424 AA.
AC Q03755; Q18693;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cuticlin-1;
DE Flags: Precursor;
GN Name=cut-1 {ECO:0000303|PubMed:1864469, ECO:0000312|WormBase:C47G2.1};
GN ORFNames=C47G2.1 {ECO:0000312|WormBase:C47G2.1};
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1864469; DOI=10.1016/0012-1606(91)90253-y;
RA Sebastiano M., Lassandro F., Bazzicalupo P.;
RT "cut-1 a Caenorhabditis elegans gene coding for a dauer-specific
RT noncollagenous component of the cuticle.";
RL Dev. Biol. 146:519-530(1991).
RN [2]
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 [3]
RP FUNCTION, DOMAIN, AND REGION.
RX PubMed=7935621; DOI=10.1016/0166-6851(94)90123-6;
RA Lassandro F., Sebastiano M., Zei F., Bazzicalupo P.;
RT "The role of dityrosine formation in the crosslinking of CUT-2, the product
RT of a second cuticlin gene of Caenorhabditis elegans.";
RL Mol. Biochem. Parasitol. 65:147-159(1994).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP 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 [5]
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: Component of the cuticles, which contributes to the formation
CC of extracellular envelopes protecting the organism from the environment
CC (PubMed:1864469) (Probable). Plays a role in alae formation in dauer
CC larvae (PubMed:15936343, PubMed:30409788).
CC {ECO:0000269|PubMed:15936343, ECO:0000269|PubMed:1864469,
CC ECO:0000269|PubMed:30409788, ECO:0000305|PubMed:7935621}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted {ECO:0000305|PubMed:15936343}.
CC -!- DEVELOPMENTAL STAGE: Expressed in head and tail seam cells during dauer
CC larva formation (PubMed:1864469, PubMed:15936343). In dauer phase
CC larvae, expressed in two ribbons approximately 2 microns wide running
CC along the lateral lines underneath the alae (PubMed:1864469). Not
CC expressed in late embryogenesis or adults (PubMed:15936343).
CC {ECO:0000269|PubMed:15936343, ECO:0000269|PubMed:1864469}.
CC -!- DOMAIN: The small repeats A-A-P-[AVI] are also present in many proteins
CC constituting the protective envelope of other species.
CC {ECO:0000305|PubMed:7935621}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in no alae in
CC dauer stage larvae, which results in a wider lateral cuticle and larger
CC body diameter. {ECO:0000269|PubMed:15936343}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27995.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M55997; AAA27995.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX284602; CAA88934.1; -; Genomic_DNA.
DR PIR; A49772; A49772.
DR PIR; T20032; T20032.
DR RefSeq; NP_496410.1; NM_064009.3.
DR AlphaFoldDB; Q03755; -.
DR BioGRID; 40028; 1.
DR IntAct; Q03755; 1.
DR STRING; 6239.C47G2.1; -.
DR EPD; Q03755; -.
DR PaxDb; Q03755; -.
DR PeptideAtlas; Q03755; -.
DR EnsemblMetazoa; C47G2.1.1; C47G2.1.1; WBGene00000851.
DR GeneID; 174720; -.
DR KEGG; cel:CELE_C47G2.1; -.
DR UCSC; C47G2.1; c. elegans.
DR CTD; 174720; -.
DR WormBase; C47G2.1; CE02165; WBGene00000851; cut-1.
DR eggNOG; ENOG502QV41; Eukaryota.
DR GeneTree; ENSGT00940000163650; -.
DR HOGENOM; CLU_037896_1_1_1; -.
DR InParanoid; Q03755; -.
DR OMA; DIMEGAN; -.
DR OrthoDB; 877658at2759; -.
DR PhylomeDB; Q03755; -.
DR PRO; PR:Q03755; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000851; Expressed in material anatomical entity and 1 other tissue.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; 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: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; Disulfide bond; Membrane; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..424
FT /note="Cuticlin-1"
FT /id="PRO_0000041747"
FT TOPO_DOM 19..392
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..277
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REPEAT 302..305
FT /note="1"
FT /evidence="ECO:0000305|PubMed:7935621"
FT REPEAT 307..311
FT /note="2"
FT /evidence="ECO:0000305|PubMed:7935621"
FT REPEAT 312..315
FT /note="3"
FT /evidence="ECO:0000305|PubMed:7935621"
FT REPEAT 320..323
FT /note="4"
FT /evidence="ECO:0000305|PubMed:7935621"
FT REGION 302..323
FT /note="4 X 4 AA repeats of A-A-P-[AVI]"
FT /evidence="ECO:0000305|PubMed:7935621"
FT DISULFID 197..252
FT /evidence="ECO:0000250"
FT CONFLICT 27..29
FT /note="GEP -> PEG (in Ref. 1; AAA27995)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="AA -> G (in Ref. 1; AAA27995)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="CL -> SS (in Ref. 1; AAA27995)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..396
FT /note="FA -> LP (in Ref. 1; AAA27995)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="IG -> MR (in Ref. 1; AAA27995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 45168 MW; 2D178A602C1500B5 CRC64;
MTWKPIICLA ALVLSASAIP VDNNVEGEPE VECGPNSITV NFNTRNPFEG HVYVKGLYDQ
AGCRSDEGGR QVAGIELPFD SCNTARTRSL NPKGVFVSTT VVISFHPQFV TKVDRAYRIQ
CFYMESDKTV STQIEVSDLT TAFQTQVVPM PVCKYEILDG GPSGQPIQFA TIGQQVYHKW
TCDSETTDTF CAVVHSCTVD DGNGDTVQIL NEEGCALDKF LLNNLEYPTD LMAGQEAHVY
KYADRSQLFY QCQISITIKD PGSECARPTC SEPQGFGAVK QAGAGGAHAA AAPQAGVEEV
QAAPVAAAAP VAAPVAAAAA APAVPRATLA QLRLLRKKRS FGENEGILDV RVEINTLDIM
EGASPSAPEA AALVSEESVR RRATSTGICL TPIGFASFLG IGTIVATALS ATIFYVARPT
SHKH
