ID E3LJV9_CAERE Unreviewed; 313 AA.
AC E3LJV9;
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-139 protein {ECO:0000313|EMBL:EFP00362.1};
GN Name=Cre-col-139 {ECO:0000313|EMBL:EFP00362.1};
GN ORFNames=CRE_18909 {ECO:0000313|EMBL:EFP00362.1};
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}.
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DR EMBL; DS268410; EFP00362.1; -; Genomic_DNA.
DR RefSeq; XP_003115874.1; XM_003115826.1.
DR AlphaFoldDB; E3LJV9; -.
DR STRING; 31234.E3LJV9; -.
DR EnsemblMetazoa; CRE18909.1; CRE18909.1; WBGene00058024.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; E3LJV9; -.
DR OMA; IFSEMAH; -.
DR OrthoDB; 5652136at2759; -.
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:SF297; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM01088; Col_cuticle_N; 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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..66
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 30728 MW; A316077B0F8D1054 CRC64;
MDMELQTRLK AYRFIAYSAV TLSVAAVFGI CFTLPLLHNY VEGMKSHVDK ELSHCRHTTA
DIFSEMAHIK KAKNGTRFAR QAGYGGDAAE YDDDAAVEVA PSRVSGGSCS GCCLPGPQGP
PGPAGRPGRP GKPGACGNHG NPGKPTGLPC DPVTVPPCKP CPPGAPGEPG HDGAPGAPGK
PGAPGVGGGS GAPGAPGPKG APGGPGQPGR DGQPGQAGQP GASSSEPGQP GQAGQPGPRG
PPGQAGQPGG NGQPGAPGQP GSRGNDGQPG NDGQPGSPGQ PGQSGGSGEK GICPKYCAID
GGVFFEDGTR RRR
//
