ID A0A0V1A4U9_9BILA Unreviewed; 1661 AA.
AC A0A0V1A4U9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KRY19466.1};
GN Name=COL15A1 {ECO:0000313|EMBL:KRY19466.1};
GN ORFNames=T12_8831 {ECO:0000313|EMBL:KRY19466.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19466.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19466.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19466.1};
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:KRY19466.1}.
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DR EMBL; JYDQ01000035; KRY19466.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1A4U9; -.
DR Proteomes; UP000054783; 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; cd00096; Ig; 1.
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; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00060; FN3; 3.
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; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KRY19466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 28..122
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 128..223
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 270..377
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 507..678
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 964..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1661 AA; 183737 MW; D36D14247B6A9B91 CRC64;
MEKKQQFHVA FLREIRIDEI LENQPPGVPT NVQYEVLSQD TIYLWWNPPA DSDRIVVRGY
TVGWGVGDSI DSMAISLSGK DSTSVKLDDL LPNTNYTISL SAFNDKGDGK QEKKIICTKP
DLLDYLKPPI NLHAETWSSS EILLTWDDFP CDRCPDFGQA NYLVRYAPHN DEHGVVKTVA
VDERQVLLSD LLPDTEYEFS IKTRHQYADS EWSTLAFGKT MPKAHPQKQP VPAINAGNEM
LRTVYVDRDP SSNLPTSLSE NLHQIDNEDS PTIVRLLASH PNLLHIEWER PLRLRRTITG
YDIFYKLLFD DADVNGGWLK KTVYGNLESY DLDVNYNRLG DAPVDSIQVK IRALTSSGPG
KFSDVATHDF DIFTRVGYLK SDAKKEAEME IRRSVKVVVE NEKDVLKVNE IFVASVLNVD
GTFQMKLSFL STPALKGNDN FIHLQAYVSF WKNHTVLRLV IENVQPEDSG TYICGKKYRN
KLYGQSVHLT VKPLYVKQPS DNGFKRIVCK FEKLNQSEFC QWKVEAESAN SWHLAYIDPE
SPNLNVADGH GSRNQQVMLF ESDSTTQRAI SRLISPVLPS DFSFHYCFNF AYRIRPESNG
KIFIYALPQP EQFDNQVLLM HFKLSPVHGQ QHHWQNCAVK LLPIKHNFRI AIEVIKSAGE
KVFIAIDSLQ LMPGICKSAC NQPNPTANHR QLERVHQPLQ YSSVKDDEVE IDLLKAVKAP
LDPNIYHAKG KQGLPGFGFH QGANVVAPYR FYMPRRFFRD FAILITVRPD DDRGGYLFAV
VNPFDTVVEL GVLLEPLNDR NANLSLVYSD SRRDADPGRA IASFQIPPIN GKWTELAFKI
EGNEVTLYYN CQRYETQTLQ RRQKQLNFDD ASKLYIAQAG PIINKPFVMK IATTSLLINM
VTMVVVVTIA GNADQQLTNT TAQGSLNLTD EGALQELKIF ANPAEAETQC DDIAFDGNGS
GDNELFTDVG LSGESPDPPS LTDPPPHYPD LELARYRILP ADSSRRRLHW FEKPNAVDSL
IVAWGDTDSA SDLPSLDYLY TNSDNSKEPL LSEIQGPPGP KGDPGVPGLS IKGEKGDPGP
PGVCSCPAVA EVDKSSQAAV GPVGPKGEPG EKGEPCKSDV DYEAIIKKYA LKGDRGYPGP
PGPPGPPGQK GDTGDAGPVG SIGPPGFPGP PGKPGATEVV DSAPKEVARS RYGHRRHEYD
QYELRMEQLQ GPPGPPGHRG PEGPQGPPGY PGLPGNPGPP GPPGPPGPAG LPASVGSRGP
YTNGFSNIIP GAERLRIYQG EDKQRQNFGY PGYPGPPGPP GPPGPPGPPG SSVYANAAVK
GAQEGEQLKK AHGANYIIPG TLVYPTNLDT FYASEHIQIG SLAFSLSSEE LFIRVKGGWR
QVKLEGFQSS MEEKMSLLSD ATARKTETVR PPVDASSKHT SSEPMAPTDV NKNEVLHLIA
LNDPFTGNMH GVRGADFACY HQARAAGFTT TFRAFVSSQV QDLDKIVHHS DRGTPVVNLR
GQILFNSWDD MFRDGGAFFS LNTPIYSFDR KDVFSHHGWP EKYVWHGSDT KGTRRSGKFC
DAWRSNSPKR TGMASSLHAR SLLGQKDFPC NSTLVVLCIE NMSKGNVDRR LAKKRFGPTL
RDQSNLMYDF ENTIYLMSVT ALMPALYKIA STNKRSAEPT I
//
