ID A0A0M3IZ68_ANISI Unreviewed; 363 AA.
AC A0A0M3IZ68;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:ASIM_0000054901-mRNA-1};
GN ORFNames=ASIM_LOCUS451 {ECO:0000313|EMBL:VDK17723.1};
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_0000054901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0000054901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK17723.1, 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; UYRR01000281; VDK17723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3IZ68; -.
DR WBParaSite; ASIM_0000054901-mRNA-1; ASIM_0000054901-mRNA-1; ASIM_0000054901.
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 PANTHER; PTHR24637:SF282; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035041187"
FT DOMAIN 5..57
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 64..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 36242 MW; 93F744565D18B3A2 CRC64;
MKVYTATFIA SSLSGIALVL SLLAISQLCQ DVNSIWNELD REMMTFRDVT NDLWADIMKL
GKQSGRARRQ AGNNGKDEKV KAGLKSKGEV VAESSNGTDD RQETARSADV SGSTTSSDAN
KCVGKHCSKQ PIKGCVGSAC ASFNQASGVG GLGRDEAPGT PYDTQAPAGP PAGNGCNCQI
KNNKCPAGPP GPKGASGPPG SNAPPGIDGV AGKGSEDITL DLQATPACYY CPAGPVGPPG
AMGRSGPRGM QGANGMLGHR GMDGQPGFPG DRGDSGQEGL KGVTGSPGAK GFDGRKPMGG
PGPKGKTGPP GNAGEQGDYG NDVLAGPEGP AGKQGPPGPP GPEGPDGVTG PIGRHGKTGR
DAE
//