ID E3M542_CAERE Unreviewed; 326 AA.
AC E3M542;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=CRE-COL-14 protein {ECO:0000313|EMBL:EFO92458.1};
GN Name=Cre-col-14 {ECO:0000313|EMBL:EFO92458.1};
GN ORFNames=CRE_11032 {ECO:0000313|EMBL:EFO92458.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000256|ARBA:ARBA00011518}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS268425; EFO92458.1; -; Genomic_DNA.
DR RefSeq; XP_003108766.1; XM_003108718.1.
DR AlphaFoldDB; E3M542; -.
DR STRING; 31234.E3M542; -.
DR EnsemblMetazoa; CRE11032.1; CRE11032.1; WBGene00059324.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; E3M542; -.
DR OMA; FPPQCPC; -.
DR OrthoDB; 2883138at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF390; CUTICLE COLLAGEN 14; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..64
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 139..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 33004 MW; E8926310E891EC2C CRC64;
MSDEKEKRSL RPVAFVAVVF STVAITSCLI TFPLILHYIQ TLESQVQLDL EFCQARARDM
WKEMLDIETG GKKDSAKLAN IVLNHRRLEK RDTLQDFWAR RLHDQELRDQ PVGYDNPSVG
VESFNSEGGG CCTCHRGPPG PAGDGGRDGV DGVDGTPGEI GPPGPPAPPG PDPHSLFPPQ
CPCEAPPGDA GPPGQPGPDG PPGAPGNPGE DGKPGDQGPR GPPGIPGAPG QPGRPGPPGE
PGTYKTEVGP AGRAGAPGRP GPPGQPGPAG PPGENGKGGS QGPSGLPGPP GQPGQNGAPG
DVGQPGDNGA PGSCDHCPPA RLAPGY
//