CUTI_CAEEL
ID CUTI_CAEEL Reviewed; 202 AA.
AC O02051;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein cuti-1 {ECO:0000305};
DE AltName: Full=Cuticle and epithelial integrity protein 1 {ECO:0000312|WormBase:ZC328.1};
GN Name=cuti-1 {ECO:0000303|PubMed:19357781, ECO:0000312|WormBase:ZC328.1};
GN ORFNames=ZC328.1 {ECO:0000312|WormBase:ZC328.1};
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, INTERACTION WITH VPS-39, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19357781; DOI=10.1371/journal.pone.0005117;
RA Fritz J.A., Behm C.A.;
RT "CUTI-1: A novel tetraspan protein involved in C. elegans CUTicle formation
RT and epithelial integrity.";
RL PLoS ONE 4:e5117-e5117(2009).
CC -!- FUNCTION: Involved in cuticle formation and ensures cuticle shedding
CC during larval development (PubMed:19357781). Plays a role in
CC maintaining the hypodermis (PubMed:19357781). In association with vps-
CC 39, may play a role in vesicle tethering (PubMed:19357781).
CC {ECO:0000269|PubMed:19357781}.
CC -!- SUBUNIT: Interacts with vps-39. {ECO:0000269|PubMed:19357781}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:19357781}.
CC -!- DEVELOPMENTAL STAGE: Temporally expressed in embryos and larvae
CC (PubMed:19357781). Expression peaks prior to each larval molt
CC (PubMed:19357781). In L4 larvae, expressed in the hypodermis, in the
CC vulval and anal epithelium, in the excretory pore, the seam cells and
CC at the seam cell boundary (PubMed:19357781). Not expressed in adults
CC (PubMed:19357781). {ECO:0000269|PubMed:19357781}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a squat body
CC statue referred to as a dumpy phenotype, uncoordinated movements, and
CC while animals can move in a sinusoidal manner, they cannot progress
CC forward or backward, (referred to as a skiddy phenotype)
CC (PubMed:19357781). Animals also display cuticle formation defects where
CC the cuticle blisters at the point where the outer layers dissociate
CC from the body, and furthermore the cuticle fails to shed and wraps
CC tightly around the body (PubMed:19357781). In 10% of animals, the
CC cuticle tapers in the posterior region of the body (PubMed:19357781).
CC RNAi-mediated knockdown also results the formation of vesicle-like
CC structures in the hypodermis, thickening of the hypodermis and in its
CC degeneration, and as a consequence as hermaphrodites reach gravidity,
CC the vulva protrudes and eventually ruptures, leading to death
CC (PubMed:19357781). In addition, animals display seam cell fusion and
CC function defects resulting from bifurcation of alae (PubMed:19357781).
CC RNAi-mediated knockdown in males results in sensory ray defects where
CC the rays fail to fully extend, and a reduced sized cuticular fan
CC (PubMed:19357781). {ECO:0000269|PubMed:19357781}.
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DR EMBL; BX284601; CCD73295.1; -; Genomic_DNA.
DR RefSeq; NP_491844.1; NM_059443.4.
DR AlphaFoldDB; O02051; -.
DR SMR; O02051; -.
DR STRING; 6239.ZC328.1; -.
DR EPD; O02051; -.
DR PaxDb; O02051; -.
DR PeptideAtlas; O02051; -.
DR EnsemblMetazoa; ZC328.1.1; ZC328.1.1; WBGene00022591.
DR GeneID; 172340; -.
DR UCSC; ZC328.1; c. elegans.
DR CTD; 172340; -.
DR WormBase; ZC328.1; CE27347; WBGene00022591; cuti-1.
DR eggNOG; ENOG502S5IK; Eukaryota.
DR HOGENOM; CLU_1311457_0_0_1; -.
DR InParanoid; O02051; -.
DR OMA; HFGPIWP; -.
DR OrthoDB; 1619605at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022591; Expressed in embryo and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..202
FT /note="Protein cuti-1"
FT /id="PRO_0000451863"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..68
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..148
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22999 MW; D6687767003C0F70 CRC64;
MPNDRVAPLP PNFVYSPHDK FYYAPATCNS MHYTTASYIS AFIEFLVMGT GAICFYVMSH
KSDSIGKWLF YIQAGITVLS LLTSALMAFG LWKENPQMLG SKLKFIEFII CFLLIWAVIS
IVCMAFGIQF TRQVFGIFGK VHRIEQDYGP IWPFNIAVVS FFTAAIAIWT RIIIQGAADY
LYDKAYFADK QNVELRESSK TR
