ID A0A0V0S5T7_9BILA Unreviewed; 1601 AA.
AC A0A0V0S5T7;
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:KRX22052.1};
GN Name=COL15A1 {ECO:0000313|EMBL:KRX22052.1};
GN ORFNames=T07_5602 {ECO:0000313|EMBL:KRX22052.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22052.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22052.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22052.1};
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:KRX22052.1}.
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DR EMBL; JYDL01000034; KRX22052.1; -; Genomic_DNA.
DR Proteomes; UP000054630; 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; IPR003599; Ig_sub.
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; 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:KRX22052.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 23..117
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 123..218
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 265..372
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 472..643
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 929..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 176728 MW; 95E0F97C95AC875F CRC64;
MQNDSILHKI RIDEILENQP PGVPTNVQYE VLSQDTIYLW WNPPADSDRI VVRGYTVGWG
IGDSIDSMAI SLSGKDSTSV KLDDLLPNTN YTISLSAFND KGDGKQEKKI ICTKPDLSDY
LKPPINLHAE TWSSSEILLT WDDFPCERCP DFGQANYLVR YAPHNDEHGV VKTVAVDERQ
VLLSDLLPDT EYEFSIKTRH QYADSEWSTL AFGKTMPKAH PQKQPLPAIN AGNEMLRTVY
VDRDPSSNLP TSLSENLHQI DNEDSPTIVR LLASHPNLLH IEWERPLRLR RTITGYDIFY
KLLFDDADVN GGWLKKTVYG NLESYDLDVS YNRLGDAPVD SIQVKIRALT SSGPGKFSDV
ATHDFDIFTR VGYLKSDAKK EAEMEIRRSV KVVVENEKDV LKVNEIFVAS AYVSFWKNHT
VLRLVIENVQ PEDSGTYICG KKYRNKLYGQ SVHLTVKPLY VKQPSDNGFK RIVCKFEKMN
QSEFCQWKVE AESANSWHLA YIDLDSSNLN VADGHGSRNQ QVMLFESDST TTRAISRLIS
PVLPSDFSFH YCFNFAYRIR PESNGKLFIY ALPQPEQFDN QVLLMHFKLS PVHGQQHHWQ
NCAVKLLPIK HNFRIAIEVI KSAGEKVFIA IDSFQLMPGI CKSACNQPNP TANHRQLERV
HQPLQYSSVK ANEMEDELGS VLRHDEVEID LLKAVKAPLD PNIYHAKGKQ GLPGFGFHQG
ANVVAPYRFY MPRRFFRDFA ILITVRPDDD RGGYLFAVVN PFDTVVELGV LLEPLNDRNA
NLSLVYSDSK RDADPGRAIA SFQIPPINGK WTELAFKIEG NEVTLYYNCQ RYETQTLQRR
QKQLNFDDAS KLYIAQAGPI INKPFVMKIA TTSLLITMVT MVVVVTIAGS PDQQLTNTTA
QGSLNLTDEG ALQELKIFAN PAEAETQCDD IAFDGNGSGD NELFTDVGLS GESPDPPSLT
DPPPHYPDLD NSKEPLLSEI QGPPGPKGDP GVPGLSIKGE KGDPGPPGVC SCPAVAEVDK
SSQAAVGPVG PKGEPGEKGE PCKSDVDYEA IIKKYALKGD RGYPGPPGPP GPPGQKGDTG
DAGPVGSIGP PGFPGPPGKP GATEVVDSAP KEVARSRYGH RRHEYGQYEL RMEQLQGPPG
PPGHRGPEGP QGPPGYPGLP GNPGPPGPPG PPGPAGLPAS VGSRGPYTNG FSNIIPGAER
LRIYQGEDKQ RQNFGYPGYP GPPGPPGPPG PPGPPGSSAY ANAAVKGAQE GEQLKKAHGA
NYVIPGTLVY PTNLDTFYAS EHIQIGSLAF SLSSEELFIR VKGGWRQVKL EGFQSSMEEK
MSLLSDATAR KTETVGPPVD ASSKHTSSEP MAPTDVNKNE VLHLIALNDP FTGNMHGVRG
ADFACYHQAR AAGFTTTFRA FVSSQVQDLD KIVHHSDRGT PVVNLRGQIL FNSWDDMFRD
GGAFFSLNTP IYSFDRKDVF SHHGWPEKYV WHGSDTKGTR RSGKFCDAWR SNSPKRTGMA
SSLHARSLLG QKDFPCNSTL VVLCIENMSK GNVDRRLAKK RFGPTLRDQS NLIYDFENTS
WPIRHAPKML FEESFLFDVS HCLDACAVQN SFYKRSAEST I
//
