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Database: UniProt
Entry: A0A2A2J874_9BILA
LinkDB: A0A2A2J874_9BILA
Original site: A0A2A2J874_9BILA 
ID   A0A2A2J874_9BILA        Unreviewed;       874 AA.
AC   A0A2A2J874;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   RecName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000259|SMART:SM01088};
GN   ORFNames=WR25_04423 {ECO:0000313|EMBL:PAV57978.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV57978.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV57978.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV57978.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RED family. {ECO:0000256|ARBA:ARBA00006660}.
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:PAV57978.1}.
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DR   EMBL; LIAE01010609; PAV57978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2J874; -.
DR   STRING; 2018661.A0A2A2J874; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR039896; Red-like.
DR   InterPro; IPR012492; RED_C.
DR   InterPro; IPR012916; RED_N.
DR   PANTHER; PTHR12765:SF5; PROTEIN RED; 1.
DR   PANTHER; PTHR12765; RED PROTEIN IK FACTOR CYTOKINE IK; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF07807; RED_C; 1.
DR   Pfam; PF07808; RED_N; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..58
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          107..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..124
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  99135 MW;  6844178B0BDD1B33 CRC64;
     MFEEKLLVGI ASTCSLIAVI TCLIVIPTIY KEINDIHDEV INSVNVFRVE TDTAWADMMD
     VQVLVTPPSK PRENPFASVF RQKRQYYGGL PSWCQCNAPV ARCPSGPPGP PGLPGQPGNP
     GPPGQPGADS HDFYPAISCP APPNDCKRCP RGDTLEPQDS QVSEDTAAHQ DPDNPDAVSS
     KAKIVRSNDA YNLIPAGLAG RSGARVAGRP GRAGANQEST EASQESQDIP EDQEKMVCQE
     SQDSQESQDQ TRLTAPAQQD PATTRPGDTG NTKRWFSPHT NCILSETCAY PGGCRQFFAD
     QHQSARIRVG RQFLSDNCVF DSIGQIVYSK LSLTRYPTMA DGSTNLRNED FRKLLAAPRS
     AGASSKASEP ASAKSDVAFQ RKQKVKPEKK KSRPFKSSAK EKLEPDEEEA KLKEILKNYR
     DRAAERRNKN DDDMDEATKL LAAYHSVPGD ARGTRDKANL RKQIIEESKF LGGDLAHTHL
     VKGLDYSLLN KVRSEMQKSH IERVNDELED ALEKGEEPKV EVKTENKMVQ RINSTLFKND
     LPEKNAMFAK GRMAYVVSFD DEEGEVPTTL LRSLHDLPRH ESNASINANN MLISKLTQVL
     AYLRADNKKK KRVDVPEEET RQQANSSIFE NEEEYVPSKH RDKRDDKDKR TSDRDRDRDA
     PRKDKERDYF GDKGRREKED RRDRRDRRSR SRSREVDKSR ERERDRDHRD RDRDRDRERD
     RDRKKDGDRN KKDDKQRRLQ EEQEREKKLE EKLEKKMKAT ANTGYDECYP GGFAEMGGAS
     DDEEDFSKMD PGNKKGVIKR WDFSTEEEFE SYQASREANP RAAYQFGIKA GDGRKTRKNA
     DPNKKLEREL NQINKLIEKR KTGGDDGFVF LSKL
//
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