ID A0A0V0WJ49_9BILA Unreviewed; 3609 AA.
AC A0A0V0WJ49;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Fibropellin-1 {ECO:0000313|EMBL:KRX75714.1};
GN Name=EGF1 {ECO:0000313|EMBL:KRX75714.1};
GN ORFNames=T06_13904 {ECO:0000313|EMBL:KRX75714.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75714.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75714.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75714.1};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRX75714.1}.
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DR EMBL; JYDK01000116; KRX75714.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0WJ49; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 13.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 17.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 7.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 7.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02494; HYR; 3.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00084; Sushi; 4.
DR PRINTS; PR01983; NOTCH.
DR SMART; SM00032; CCP; 10.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 21.
DR SMART; SM00179; EGF_CA; 15.
DR SMART; SM01411; Ephrin_rec_like; 7.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 17.
DR PROSITE; PS01187; EGF_CA; 4.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50825; HYR; 3.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 8.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 3453..3478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..195
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 242..354
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 358..471
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 587..649
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 650..711
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 712..771
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 772..830
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 830..871
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1082..1141
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1215..1281
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1331..1485
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1511..1597
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1598..1681
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1682..1747
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 2060..2102
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2104..2140
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2142..2180
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2182..2222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2224..2260
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2262..2297
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2299..2335
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2337..2373
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2375..2413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2415..2451
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2453..2489
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2491..2527
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2529..2565
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2567..2603
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2841..2921
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 2922..2991
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 3367..3408
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3409..3443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 199..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 206..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 218..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 714..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1112..1139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2092..2101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2130..2139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2151..2168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2170..2179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2212..2221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2250..2259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2266..2276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2287..2296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2325..2334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2363..2372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2403..2412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2441..2450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2479..2488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2517..2526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2555..2564
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2593..2602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3411..3421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3433..3442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3609 AA; 399183 MW; CA5F9D63D680852E CRC64;
MQGRRRILVV DVLEIEEEEE EVDEPAIVLA DDQQTKYLQR DIKLICPEDW KLNGLTCYRV
YTQPRSWSQA LSLCSRYGSQ LARILTVEEN DFVYHLARAQ LKQSDHKEFW IGQFDQRPLQ
VNCRSEFNLP LKNRSSNFLW SNNEPTSKYG GFWHLGQPDL TVGSCVASSI AKANDNDHSA
WHLTACNHLY PFVCQLQACV EGMMFCHNGK CISKNGKCDG FDDCGDLSDE MNCRASQGNA
LCIRYAKGDS GIVESPNFPA EYKSNLNCQW TIEVAANAKI RLEFESFQTE PYYDIVTLLD
GGPVENTSVV VDHISGNVDP SKLIFLSSTN RMAVKFRSDA SVNFKGFKAN WRLVTFDCGG
RLKAHPNEQT INSPNYPQNY PNGAECLWII EATGNQLISI TVRINDVELE NGKDMLIIYD
GEHSTSRALF STSSAIDEPR VVISTRNRVS VYFFSNYLNS ARGFSISYRL GCDNTMQGTS
GFITSPGNNA VDYHGDHLCT FTVNPTQQVM PPRPVTLVIN HFTGNAETFL QIFDGMDNRG
HQLYPKGKEG SVLKSGGTLI SETGHFFLLF KETPLDSTVN WNITYSLNCP PLTLSKDVLL
SSTSTAYGTK VNISCPYGSE FINGIGSSTE LTCLLGGQWS QNFIPKCQPI YCSIMPVPAE
NGFVAAATNV TYLGKVSIKC YRGHAFSSGL DVEEIDCNED GTWSKIPQCK ALVCPELPEF
VSGNRTILRG DGRSYGTIYK YRCFSGSYME GADTVLCEMD GWSSPEPVCK KLSCEPISYT
GNVLLKTDAL KIYSGDVTPV ECRPGYKMVG KGEIICQDNQ QFTELPVCED IDECRLDGMF
DCSSLTTTCK NLQGGYACEC LEGYEPKLEC NSTSELIKSM AIPSDSIISE SETWKYPAKN
IATSGWCGKL PEPGANSISI ILDEPRIIEA VIIKKISDNT LAQVMAISLK YSLHSTHPLK
QYVDNDGSKI LLKSNGGIIM LPEPIEAEAV KITIEEYKSA PCMIMELQGC RRTSCTDINE
CLIDKGGCEH LCINRPGKYE CSCHPGYELF TKNGQNDMYV HPKESGTRLG DVFGLNKSCI
PRTCNSLIPP ENGDIVSTAT KFSYPIVVEF VCNFGFQLHG SQFLQCMSDG HWNASVPVCS
PAKCANFEND TEIGLHLYPG SQLIDFGENV TITCAQDTRP NGPTAFSHFR QCLFSPDSDG
PDYRLAGLPP TCELVDCGEP EFLPASIYKN FDEVQSFKFG SNFLFTCRKP FFVSGSSNAG
DHIVRCLADG SWDFGDLHCD GTVCPDPGIL QDGDVIIDSV EEGNIARFTC RKPGYMPYPI
SAMQCIIGAK CPKTEELGIS SGVVPDTAFA ANTETPIRGY EPHKARMSRG GWCGSPDAFM
FLSVDLQHVY TITTLRLAGV GGSGAIRGHV TKFQLFYKSL FNQNFDTYPE VWNSNFAILE
FEMPPGNHNK MYVFQLKEFI RARYILIGIL EFDNNPCLRF DLLGCSMPLF QNPEIHSEFM
FGWNDSLPIC RDSEPPTFTD CPMEPLYAPI DANGQMQPIE IPIPNAIDNS GSIAWIKTEP
PDVQNFHVLT KDTNVTYTAF DAAGNWAQCS IELKVPDNRP PVLVCPESYI VEVPKDVPGM
QMIFNRSSVD LMIDDASDTV KLTFSPGEIF LKLKQHVTVK VTAEDDFGNE ASCRFQVLLD
TPRCDESNLL LPPGVEKTCS SYKSGIKCTI SCIDGYQFLE SDASKKLYSC EADEKWTPGI
IAPACVPIAD EPAKYQLKVS VSYPIATTIP ESCLNDYKSS LTSVSQQIDT VLSQRCSASV
QAFVRIVEVD FFAEVKRVVG NYTIQVLPTV LDEVFYNLCG MTLATMFDLH FPSATEAVLP
LLEIKGENGC PVLKATNTTI DKGFSCSPGE ILQKTENALP GCYPCPMGTW LYNGTCRPCE
NGTYQDLNGQ INCKRCPAGT YTLHEGATMV EHCQPVCDNG MFSESGIVPC QQCPKDTYSS
PNKEGGYRKC EPCPKNTFTN DVGASDISMC KESCPGGYFS FSGLQPCSPC PKNFYQPERG
QSACIECPKD RYTENSGAVL ENECLEANYT DLVYCRNGAV SEVVEHVAVC QCLPGYTGIH
CEQLIDPCLA QPCFNNGRCV TNGVRYECEC PEKYSGERCE FSENECQDVV CDNGGICQDL
PGIGTTKCLC RTGFYGERCE FMVNLCEKQG SELCLNGATC LPLQLNRYMC ICAAGWTGRN
CDINIDDCAG QPCAVNATCH DEINDFRCDC PPGFSGKRCH IKQDLCSDNP CVNGRCIDRN
FYYQCVCESG WTGKNCEQEI DNCASNPCLN GATCTKQFNS YECECADGYE GSRCQHQVDH
CAKEPCLNGA LCVNKGANYS CICKNGFEGM LCERAVKECS MDHHCGIGSE QCIELTNGFA
CKCRPGFTGR LCDVEIDECE DNPCLNGGTC TDGVSSFKCA CPAGWTGSRC EVSANYCDRQ
PCQNNGQCVN LGKDYFCLCP KGFDGKSCEI DSATCFTDAC LNGGECIDNG HEIACKCPPG
FFGSGCQYQQ KLCSENTCQN GGTCAESEVS IVCICPAGFT GLYCENDIDD CATSPCPPGS
TCIDMPNGHI CQCMFNKTGI NCDRAVDSDF ELRFYDPILP SFASLDLPFP FSSEVMTLAL
WVRFDHPGQT ATFLTIYSGG LFNKEETADE LLVVSSSGVE MKFPNEHSKS VLLNFPQQHR
VDDGNWNNVV FQWDSTMGIY TLYWNSIRVA TIKDQSKTKH LNTSAWVKLG TPNGHQRGES
KFVGSISRLN IWNRTLSFEK EIPRLAQNCR SSDDMLANLV LRWTGFNRLS GKVDRVAPST
CGQALCQRSI DVKLCDPSKM LDKNAPKVHG CPEYINKQSE ERSSKVEWPE PSFTDELSLE
RIERNIKPGT VLGQGLYHVI YAAYDKAGNV AQCMFDLRVQ ESFCPTLADP KNGLSYCLNW
GPDMKFEACT VRCQEGYEFS EVTPEFYTCG YDGFWRPRYS IGEFRYPDCS PTSPSVRIVS
VQLDYPSSSV ACSKANRATL ESSIRKRFIT MNAVWNLCEA RNSNEIGCPS LNVTVSCMGR
ASASTFQKRQ VKASDVYRVD LSFVANRDPV RHRHSDIRAN IIDTLKDDIV KENGFDFSSV
LPSGTPDLRS LKISDDFHCP IGQVNRNDVC VPCAMGSFFN ITTLKCQLCP IGMYQNQVGQ
LACEACPAGY TTTGFASSQR TDCKESCPAG HFYNLKKENC EPCGYGFYQP SAGSFQCIHC
DLGKSTYDTV STSKQQCSDI CPDGMQLSAG GDCQPCPMAT YRRRNENDHC ESCPAGLTTE
DKGSISIEQC NLPLCLEGQY LDESTKTCFP CEKGFYQDQK MQRQCLACPK DHTTADIGAS
QKSECYSTNQ CETLEHNCHW HAVCLDLPGE AFECQCQPGY RGNGTFCEDS CINFCTNDAV
CKKSDNGDPF CQCKDTFTGA HCEVRYMPSQ QRIAYIAGGV GGVVGVIVLI MIVIWMIYFR
FRSQDKLAES MEKLPNGNGA ASSDEKSIAE MAGNTAAPNF TYGRTYSEDS HAPTFYYEDD
DDYGVKTMYI GEGFDENDNG SRIGNDVETN NEAVFERLQR INKHVYKPKY QESISDTESM
RKVDTGIDL
//
