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Database: UniProt
Entry: A0A0M3IZ68_ANISI
LinkDB: A0A0M3IZ68_ANISI
Original site: A0A0M3IZ68_ANISI 
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
//
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