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Database: UniProt
Entry: A0A0M3I2K0_ASCLU
LinkDB: A0A0M3I2K0_ASCLU
Original site: A0A0M3I2K0_ASCLU 
ID   A0A0M3I2K0_ASCLU        Unreviewed;       401 AA.
AC   A0A0M3I2K0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 2.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:ALUE_0001073801-mRNA-1};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001073801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0001073801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (MAY-2016) to UniProtKB.
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   AlphaFoldDB; A0A0M3I2K0; -.
DR   WBParaSite; ALUE_0001073801-mRNA-1; ALUE_0001073801-mRNA-1; ALUE_0001073801.
DR   Proteomes; UP000036681; Unplaced.
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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          7..59
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          80..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  42263 MW;  8F0FE4BFDE55798B CRC64;
     MWSAMRWSAT VSASVAGIAL LSLLIAFPTV MNEIATMEEE LALHRSEFIA MSNEMWDDLL
     TQSTIIRHAQ NIRRRSISGI RSRRQYEGGT YSGSSQEGGS EYSEDKIAGD AEGNKCPAGP
     KGPPGEPGEK GEDGADGEPG KPGTDGVSIS AKSGPCAPCP QGPPGFPGYK GRRGPRGQQG
     EKGAEGPPGR DGETGEEGPM GDIGPIGEIG PKGERGPRGK DGTKYARGPR GPKGETGPVG
     PEGDEGAPGE RGIDAKPGPQ GEIGPIGPPG SPGRKGQPGL PGRPGPAGGD GEYCPCPDRT
     KGEHIKPGNE VKQHYEGPIA PAERESRERV TTRPYTRPAI RPNTVHPPKT EESERKRPNG
     LSRYPNEESP ESAPSKEDVE EEDEVAEVRK EVRPKKNIAM S
//
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