ID A0A0V1HGQ8_9BILA Unreviewed; 1697 AA.
AC A0A0V1HGQ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:KRZ09532.1};
GN Name=Col15a1 {ECO:0000313|EMBL:KRZ09532.1};
GN ORFNames=T11_13131 {ECO:0000313|EMBL:KRZ09532.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ09532.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ09532.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ09532.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ09532.1}.
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DR EMBL; JYDP01000071; KRZ09532.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
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; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF428; SCAVENGER RECEPTOR CLASS A MEMBER 3; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
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 SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KRZ09532.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 78..172
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 198..293
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 340..447
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 485..560
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 577..749
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 1036..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1697 AA; 188597 MW; ABDA0261A52B79FC CRC64;
MPVSQVEISL LISAFIIVEK NGRFSVLRFA RWRDNCFAQS GIVAFIYYEI KQIHVVILWG
ILYEIRVDKV LENQPPGVPT NVQFEVLSQD TIYLWWNPPA DSDQIVVRGY TVGWGIGDSI
DSMAISLSGK DSTSVKLDNL LPNTNYTISL SAFNDKGDGK QEKKVICTKP EFLKDSKKAT
PSVQFSFSLS DPLDYLKPPI NLHAEAWSSS EILLTWDDFP CERCPDFGHA NYLVRYAPHN
DEHAAVRTAV VNERQVLLSD LMPDTEYEFS IKTRNQYANS EWSTLTFGKT LPKAYPQKQT
VPTISAGNEM LRTVYVDRDQ SSNLPASLSE HLQQIDNEDS PTIVRLLASH PNLLHIEWER
PLRLKRTITG YDIFYKLLFD DADVNGGWLK KTVYGNLESY DLDVSYNRLG DAPVDSIQVK
IRALTSSGPG KFSDVATHDF DIFTRVGYLK SDAKKEAEME IRRSVKVVIE NEKDVLKVNE
IFVASCVIET NSQRSQRRWY FPNETVVPFD TGIERAYVSF WKNHTILRLV IENVQPEDSG
TYICGNKHRN KLYGQSVHLT VKPLYVKQPS DNGFKPIVCK FEKLNQSEFC QWKVEAESAN
SWRLAYIDPY APNLSVTDGH ESNRQQVMLF ESDSTMAGAI GRLISPVLPS DFSFHYCFNF
AYRIRPESNG KIFIYALPQP EQFDNQVLLM HFKLSLAHGQ EHHQWQNCAI KLLPIKHNFR
IAIEVIKSAG EKIFIAIDSL QLMPGICKSA CNQPSPAANH RQLQSIHQPL QYSSVKDDEV
EIDLLKAVKA PLDPNIYHAK GKQGLPGFGF HQGANVVAPY RFYMPRRFFR DFAILITVRP
DDDRGGYLFA VVNPFDTVVE LGVLLEPLTD RKANLSLVYS DHKRDTECRA IASFQIPTIT
GKWTELALKI EGTEVSLYYN CQHYETQTVQ RRQKQLNFDD ASKLYIAQAG PIINKPFVMK
IATSLMMTMV TVMMMVMVMV VVADSPDQQN NITVEQGSLN WTEGALQELK IFANPAEAET
QCDDIAFDGN GSGDNELFTD VGLSGESPDP PSLTDPPPHY PDLELARYRI LPADSSRRRF
PWFEKPNAVD SLIVAWGDTD PASDLPSLDY LYTNSDNSKE PLLSEIQGPP GPKGDPGVPG
LSIKGEKGDP GPPGVCSCPA VGEVEKSIQT VGPVGPKGEP GEKGEPCKLD VDYEAIIKKY
ALKGDRGYPG PPGPPGSPGQ KGDTGDAGPV GSIGPPGFPR RHEYDQYELR MEQLQGPPGP
PGHRGPEGPQ GPPGYPGLPG NPGPPGPPGP PGPPGPAGLP VSVGSRGTSY TNGFSNIIPG
AERLRIFQGE EKQRQNYGYP GYPGPPGPPG PPGPPGPPGS SAYANAAVKG AQGEQLRKAH
GANYITPGTL VYSTNLDTFY ASEHIQIGSL AFSLSSEELF IRVKGGWRQV KLEGFQSSME
EKMSLLSDAT ARKTETVKPP VDASSKHTSS EPMAANDLNK NEVLHLIALN DPFTGNMHGV
RGADFACYHQ ARAAGFTTTF RAFVSSQVQD LDKIVHHSDR GTPVVNLRGE VLFNSWDDMF
RDGGAFFSLN TPIYSFDRKD VFSHHGWPEK YVWHGSDTKG TRRSGKFCDA WRSNSPKRTG
MASSLYARSL LGQKDFPCNS TLVVLCIENM SKGNVDRRLA KKRFGPTLRD QSNLVYDFEN
STWPLRHGPK MLFEESL
//
