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Database: UniProt
Entry: E3LCS6_CAERE
LinkDB: E3LCS6_CAERE
Original site: E3LCS6_CAERE 
ID   E3LCS6_CAERE            Unreviewed;       468 AA.
AC   E3LCS6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=CRE-COL-164 protein {ECO:0000313|EMBL:EFO82818.1};
GN   Name=Cre-col-164 {ECO:0000313|EMBL:EFO82818.1};
GN   ORFNames=CRE_00459 {ECO:0000313|EMBL:EFO82818.1};
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; DS268407; EFO82818.1; -; Genomic_DNA.
DR   RefSeq; XP_003118220.1; XM_003118172.1.
DR   AlphaFoldDB; E3LCS6; -.
DR   STRING; 31234.E3LCS6; -.
DR   EnsemblMetazoa; CRE00459.1; CRE00459.1; WBGene00052071.
DR   eggNOG; KOG3544; Eukaryota.
DR   HOGENOM; CLU_696841_0_0_1; -.
DR   InParanoid; E3LCS6; -.
DR   OMA; ETSNVLW; -.
DR   OrthoDB; 5655238at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
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:SF355; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   SMART; SM01088; Col_cuticle_N; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          11..63
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          68..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  45101 MW;  3D8C823EC43645B5 CRC64;
     MSYKSMESSS STVSFAVILS GCAFLIMVTA TPVLFYTMSD MTSQLESAKT GFEETSNVLW
     KELVTNESHR RVARQTYKEA GGGAPTDTAP AAGTAPEGAP TVVVDNTCPP GPKGEAGAPG
     EPGTDGTDGT PGKDGSDGSN EQAASSAGDL CTACPAGPPG VTGYKGKRGS RGEKGDKGGP
     GNAGRDGAPG DDGPEGDHGH PGPMGPPGER GSPGADGKGF AKGAPGPKGP TGMDGLPGDE
     GLPGERGEDG TGGAQGETGP QGSPGEKGPD GFPGLPGAAG TAGEDAAYCP CPSRKGDVAG
     GGGGGYAAPT GTEFEGSPVG AETAGSSAEI PAPAPVGESP APESAPSGEA SSNGEALSTE
     EKPTSEGAEK TPATEGTPSE GEGAPAGGTE SGKYAGKEGE GAPTGAGGGE TAPAEAAATG
     ESSPTKAEEA PAGAGGGSTG SGDTTYPTKN RARFTARQRA ASRIRRTF
//
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