ID   A0A915CPW7_9BILA        Unreviewed;      1305 AA.
AC   A0A915CPW7;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   08-OCT-2025, entry version 12.
DE   SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|WBParaSite:jg11281.2};
OS   Ditylenchus dipsaci.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Sphaerularioidea; Anguinidae; Anguininae;
OC   Ditylenchus.
OX   NCBI_TaxID=166011 {ECO:0000313|Proteomes:UP000887574, ECO:0000313|WBParaSite:jg11281.2};
RN   [1] {ECO:0000313|WBParaSite:jg11281.2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
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DR   WBParaSite; jg11281.2; jg11281.2; jg11281.
DR   Proteomes; UP000887574; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00629; MAM; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50060; MAM_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000887574};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1305
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5037525477"
FT   DOMAIN          28..124
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          136..242
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          256..421
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   REGION          824..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1022
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1305 AA;  144632 MW;  B6458437111A4B0E CRC64;
     MTGQVCGRHV PLHIIWLISC LIGQGSTTHW DILDPLALQS PKEWRVPDPP ENVRSKATSD
     SITLWWDPPS SAEQEIVIEG SDTNSFTIES LKPNTTYVFS ITSYNEAEGE DSERVLLTAT
     TLAANKDTDQ AFRLVAPTGL ISKPTTSPGE LLVSWNDTNP PIPSTNTGTS MTTASPSRRQ
     HYIVQYGPSG KTPTNKLTTE STSTIISQLK LGENYDISVR LVRPNHHLSP WSSKFTANVP
     NNLYYVANEE VGDKKEICDF ESPGVCDYIN DANAAMQWKR KKMPSREDTP SEHSMVLTCS
     STETNQLNDF GRLLSPVYDL AKSQHICLSL RYQIRPGSYG GYFKVSVLFE TDDFSKAVLL
     FRKSVDKSKN NQWQNISLEV KAHPRHGFQV VIEGGRSINS EESNFLISVD DVQVIAAACP
     EQDRYFGVAA DEETEADLLI PLENLIHTDP RVFRTKGLDG LPAVGIKRGV EIVVPYRIYL
     PRKFYRNFAI LASVKPADNL GGYLFAVLNA FDTVVDLGVL LQPAGGSQTN ISVLYTDSQA
     ESSSQVLASF LVPSFVNQWT QLALEVNENT VALYFRCMRF ATRQVYRKPI QLQLDDASKL
     YIANAGPIIG GGFEPAHLYI LVIITFVYPL IITSNNLQDS QHANKNDHLL PLHPNNKRSR
     HRRQFTGKIK EKPFIRPIGT TSEEQYVVQV HTDPPTSTYP TTSIHWMDPK QAQDFEDKIQ
     LKDPVEEHRP QIIPATPKLD DEEEDAANKL LKMIVVYGGG VEDEGDSENF EVPEVKAVAS
     PMDPAIVDSK SGSQGLSEDE EEVKLKLQDD PAEAANQCNW KGRRRNFRRK GDEGSGLKEF
     TPEIPAQPFQ QHEWPPDDGR QPVENTEQVK TTRSPEYLST PTADQVGNER LLVKGAKGDQ
     GESGPPGVCT AQCVGTAGPV GPPGPPGPKG VQGDPGVPGI GRPGLPGTFD GLTQSDLERI
     VVWPGVKGEK GECIEASARP SSQHVQVDLD SPPVLPYDSR THRYTSSSSN KGEKGDRGEK
     GEQGVPGMPG LPAPRVEQQY PQHQPPVHHP NGGVTIFQTS VELLASAHHT SVGTLAFSIS
     SQQLFIRVNN GWRQVQLDRF HPVIEQRPSA RTQEDQVLPL QLPRPSMMSN GKGACSAPPW
     THSWPYFQTK EPVYNRYDIE YQPDAKHSHE QKAEEMNEAG VRHKNRVLHL IALNQPVTGD
     FRGVRGADLE CYRQARQAGF STTFRAFISS RVQDLNKIVH YDDRRFTPIV NLRGERLFDS
     WNAVFDGGAH SHVLCIPLTE GIFMTTIFGV TDGCGMAPTQ MVLDQ
//