ID A0A0M3K4Y4_ANISI Unreviewed; 313 AA.
AC A0A0M3K4Y4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:ASIM_0001602501-mRNA-1};
GN ORFNames=ASIM_LOCUS15432 {ECO:0000313|EMBL:VDK55147.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001602501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001602501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK55147.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYRR01032320; VDK55147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3K4Y4; -.
DR WBParaSite; ASIM_0001602501-mRNA-1; ASIM_0001602501-mRNA-1; ASIM_0001602501.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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:SF348; 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 Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..55
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 83..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 31884 MW; 1F26B0CC60060DEE CRC64;
MRWIAIVAVS VSMCATLMAI VTIPVLYSYA HTLQNRVLDE TTYCRMSSRD MWHEMFVLQN
REPVRQKRGW LFGKWIPDGG AGGGGASGYG DDEPSGYSPD ANSAVLDDSK RASDHSECCT
CQQGPVGAPG EPGDDGKDGK DGVSGKDGEP GRNGAILQLD GVINEPCIIC PAGPPGVPGP
AGNKGPQGPR GATGFAGLDG KRGEQGMVGP PGPMGAPGPE GPQGRRGEDG RVTAIDGPVG
RPGKPGPQGL KGIPGYKGPP GQSIPGPQGP IGEPGAPGRD GKKGRRGPQG STGPKGSDGD
CNHCPAPRTP PGY
//
