ID   A0A2G5VV73_9PELO        Unreviewed;       281 AA.
AC   A0A2G5VV73;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Cni-col-53 {ECO:0000313|EMBL:PIC55678.1};
GN   Synonyms=Cnig_chr_I.g856 {ECO:0000313|EMBL:PIC55678.1};
GN   ORFNames=B9Z55_000856 {ECO:0000313|EMBL:PIC55678.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC55678.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC55678.1}.
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DR   EMBL; PDUG01000001; PIC55678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5VV73; -.
DR   STRING; 1611254.A0A2G5VV73; -.
DR   Proteomes; UP000230233; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF371; COLLAGEN; 1.
DR   Pfam; PF01391; Collagen; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          83..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  29744 MW;  F72004DB1F49B936 CRC64;
     MSLPSYIWRK TASPTVAITL SVSAVIYVTA ICPLVFLYLF GDASNVLENE QCPTQMSELR
     ERVNIVKEHI HDSIRQKREL ASCCVGPPGM KGFPGKNSRD GYDGEPGRDG QPGRPADGDS
     RMICIRECPA GRPGREGGDG PKGQKGQRGR TGQQGDTAPP SIRGEPGERG DKGFPGAPGT
     SGEPGEPGRV YVSDGPPGKD GETGPRGPPG DKGRTGRNGE DGLPGERGER GYQGLKGEVG
     KRGPMGTFGP IGPKGEPWPC ESCPPPRVSP GYYLNSRNKK H
//