ID A0A0V1L930_9BILA Unreviewed; 1672 AA.
AC A0A0V1L930;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KRZ55746.1};
GN Name=Col15a1 {ECO:0000313|EMBL:KRZ55746.1};
GN ORFNames=T02_14688 {ECO:0000313|EMBL:KRZ55746.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55746.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ55746.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55746.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ55746.1}.
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DR EMBL; JYDW01000108; KRZ55746.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1L930; -.
DR Proteomes; UP000054721; 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; 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; 2.
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; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KRZ55746.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 21..115
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 121..216
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 263..370
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 483..654
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 975..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1261
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1672 AA; 184967 MW; 5A63EB16D22129F5 CRC64;
MIAFLHEIRI DEILENQPPG VPTNVQYEVL SQDTIYLWWN PPADSDRIVV RGYTVGWGIG
DSIDSMAISL SGKDSTSVKL DDLLPNTNYT ISLSAFNDKG DGKQEKKIIC TKPDLLDYLK
PPINLHAETW SSSEILLTWD DFPCDRCPNF GQANYLVRYA PHNDDHGVVK TVAVDERQVL
LSDLLPDTEY EFSIKTRHQY ADSEWSTLAF GKTMPKAHPQ KQPVPAINAG NEMLRTVYVD
RDPSSNLPTS LSENLHQIDN EDSPTIVRLL ASHPNLLHIE WERPLRLRRT ITGYDIFYKL
LFDDADVNGG WLKKTVYGNL ESYDLDVNYN RLGDAPVDSI QVKIRALTSS GPGKFSDVAT
HDFDIFTRVG YLKSDAKKEA EMEIRRSVKV VVENEKDVLK VNEIFVASCV IETNSQRSQR
RAYVSFWKNH TVLRLVIENV QPEDSGTYIC GKKYRNKLYG QSVHLTVKPL YVKQPSDNGF
KRIVCKFEKL NQSEFCQWKV ETESANSWHL AYIDPESPNF NVADGHGSRN QQVMLFESDS
TTQRAISRLI SPVLPSDFSF HYCFNFAYRI RPESNGKIFI YALPQPEQFD NQVLLMHFKL
SPVHGQQHHW QNCAVKLLPI KHNFRIAIEV IKSAGEKVFI AIDSLQLMPG ICKSACNQPN
PTANHRQLER VHQPLQYSSV KVEISLSALP TNEMEDELGS VLRRLEKKFP LVDPLAHDEV
EIDLLKAVKA PLDPNIYHAK GKQGLPGFGF HQGANVVAPY RFYMPRRFFR DFAILITVRP
DDDRGGYLFA VVNPFDTVVE LGVLLEPLND RNANLSLVYS DSRRDADPGR AIASFQIPPI
NGKWTELAFK IEGNEVTLYY NCQRYETQTL QRRQKQLNFD DASKLYIAQA GPIINKPFVM
KIATTSLLIN MVTVVVVVTI AGNADQQLTN TTAQGSLNLT DEGALQELKI FANPAEAETQ
CDDIAFDGNG SGDNELFTDV GLSGESPDPP SLTDPPPHYP DLELARYRIL PADSSRRRLP
WFEKPNAVDS LIVAWGDTDS ASDLPSLDYL YTNSDNSKEP LLSEIQGPPG PKGDPGVPGL
SIKGEKGDPG PPGVCSCPAV AEVDKSSQAA VGPVGPKGEP GEKGEPCKSD VDYEAIIKKY
ALKGDRGYPG PPGPPGSPGQ KGDTGDAGPV GSIGPPGFPG PPGKPGATEV VDSAPKEVAR
SRYGHRRHEY DQYELRMEQL QGPPGPPGHR GPEGPQGPPG YPGLPGNPGP PGPPGPPGPA
GLPASVGSRG PYTNGFSNII PGAERLRIYQ GEDKQRQNFG YPGYPGPPGP PGPPGPPGPP
GSSVYANAAV KGAQEGEQLK KAHGANYIIP GTLVYPTNLD TFYASEHIQI GSLAFSLSSE
ELFIRVKGGW RQVKLEGFQS SMEEKMSLLS DATARKTETV RPLVDASSKH TSSEPMAQTD
VNKNEVLHLI ALNDPFTGNM HGVRGADFAC YHQARAAGFT TTFRAFVSSQ VQDLDKIVHH
SDRGTPVVNL RGQILFNSWD DMFRDGGAFF SLNTPIYSFD RKDVFSHHGW PEKYVWHGSD
TKGTRRSGKF CDAWRSNSPK RTGMASSLHA RSLLGQKDFP CNSTLVVLCI ENMSKGNVDR
RLAKKRFGPT LRDQSNLMYD FENTIYLMSV TALMPALYKI ASTNKRSAES TI
//