ID A0A0V1HFQ7_9BILA Unreviewed; 1622 AA.
AC A0A0V1HFQ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:KRZ09539.1};
GN Name=Col15a1 {ECO:0000313|EMBL:KRZ09539.1};
GN ORFNames=T11_13131 {ECO:0000313|EMBL:KRZ09539.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ09539.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ09539.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ09539.1};
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:KRZ09539.1}.
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DR EMBL; JYDP01000071; KRZ09539.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; 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; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1079; COLLAGEN ALPHA-1(IV) CHAIN; 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:KRZ09539.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
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 1002..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1622 AA; 180199 MW; 6D01603B9A801211 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 WTEFDGNGSG DNELFTDVGL
SGESPDPPSL TDPPPHYPDL DNSKEPLLSE IQGPPGPKGD PGVPGLSIKG EKGDPGPPGV
CSCPAVGEVE KSIQTVGPVG PKGEPGEKGE PCKLDVDYEA IIKKYALKGD RGYPGPPGPP
GSPGQKGDTG DAGPVGSIGP PGFPRRHEYD QYELRMEQLQ GPPGPPGHRG PEGPQGPPGY
PGLPGNPGPP GPPGPPGPPG PAGLPVSVGS RGTSYTNGFS NIIPGAERLR IFQGEEKQRQ
NYGYPGYPGP PGPPGPPGPP GPPGSSAYAN AAVKGAQGEQ LRKAHGANYI TPGTLVYSTN
LDTFYASEHI QIGSLAFSLS SEELFIRVKG GWRQVKLEGF QSSMEEKMSL LSDATARKTE
TVKPPVDASS KHTSSEPMAA NDLNKNEVLH LIALNDPFTG NMHGVRGADF ACYHQARAAG
FTTTFRAFVS SQVQDLDKIV HHSDRGTPVV NLRGEVLFNS WDDMFRDGGA FFSLNTPIYS
FDRKDVFSHH GWPEKYVWHG SDTKGTRRSG KFCDAWRSNS PKRTGMASSL YARSLLGQKD
FPCNSTLVVL CIENMSKGNV DRRLAKKRFG PTLRDQSNLV YDFENSTWPL RHGPKMLFEE
SL
//