ID A0A0V1N011_9BILA Unreviewed; 1468 AA.
AC A0A0V1N011;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Protein NDNF {ECO:0000256|ARBA:ARBA00024096};
GN Name=NDNF {ECO:0000313|EMBL:KRZ77164.1};
GN ORFNames=T10_8026 {ECO:0000313|EMBL:KRZ77164.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77164.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ77164.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77164.1};
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: 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:KRZ77164.1}.
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DR EMBL; JYDO01000022; KRZ77164.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR CDD; cd19941; TIL; 1.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019326; NDNF.
DR InterPro; IPR045805; NDNF_C.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR14619:SF3; FI20196P1; 1.
DR PANTHER; PTHR14619; NEURON-DERIVED NEUROTROPHIC FACTOR; 1.
DR Pfam; PF10179; NDNF; 1.
DR Pfam; PF19433; NDNF_C; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00095; WAP; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00217; WAP; 1.
DR SMART; SM00289; WR1; 1.
DR SUPFAM; SSF57256; Elafin-like; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS51390; WAP; 1.
PE 4: Predicted;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1468
FT /note="Protein NDNF"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006882997"
FT DOMAIN 23..72
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 790..998
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1046..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 166296 MW; FA1477C960844CAD CRC64;
MLYTRLLFSL CVVTCLTSVS HLQRVKVGRC PELPARYLTH QLQHDRCRDD YDCESTMKCC
ESIIGKVCMM PKDYDQKEVC KQPYTKWDSC GSGCMTTCYN IGWQQPCRQQ CQPGCTCISG
FVRLYLHPYA PCVPQIHCPN QRTTRTKFGV CPTLPHGAEI DYHRRRDRCG TDFDCSGTCP
DGQKTSIFCD ERDSCPWGYT CRSGLCCPNA PWQSPTATWP GQVTTAAGNC PHYAYIGTWA
QLAPSCITNS NCAYNQLCCY TYYGNRCIQV SQLEAHHQKT IDPNHQKIFY IRKQNYMTNR
LYDDVFNKPH YSDSWYKDEE TLYKNAGEKQ MNYVSKTASM LHVRLYLTGL RRICKVEIHF
GTTPVEKHLF FQLFHLTQPK IDNIQSKSVT LSWQPSMSAL LYTGGRLVYV IALSTVRPFA
TLCDLETDLK LDRVDLLEHR RQEHVAHRLI PQHHSGAVRS LTVLDATGPA KLQLISLQQN
TNYYANVFAL NLNTGENIAY DTVSFTTTSE NQISQHRLVS SLTEAQLQTG YLGPSRVAFK
VYQFSAPVAI SELYILIQPC TGPLQAAIYQ DGQKTLHYSI EELQAINLTD VNVGIVQIQI
ANDDNQAKMF NIWASNNLSA YPYPKLPYDT SITVTERKCD SVQLSWLAST DAHVYCLYKK
VQRFDYFKQL TLEDWNLCQQ PDENLQPLFC NQFKGNQYRN EILIQEIAAL KPATTYRFDL
FVSKHSQPSL AYRTVWNRSF SVVLNEDLVA DGADRLNSDF LRTISLWVNK YLRRSRTQEM
DSPPNPLVLS GLRSLLYTFA DGVTFTVPIF LHKAFSVLEA HYLTTEGIFR KPGIASKLRV
LKNCFNASSA LELNFKIEEV SPFDLCDLIK LFLREIDEPI LTWGLQPQFL QFADLNTPRD
VRTKCLLQLC HALPPRHKET LAFIMRFLKM ISNSSAYNKM DVKNLATVFV PCIFRESAKA
RPVKHGQALL DELAASKSDI ALKVDVLEML IQNADSIGVL SEQERAILAA ESSDKLNDDL
NILKRSAKKA ASKVLVRSRN SLSGNRNSQI YRRSVQPKLK SAESIERHER IKGSRITEPY
KRRSRSSMFE TIMYSSAFTE GIATSNAIEE QCTTSPILRT SSLPDRKVIS TENRECLKVN
KAESELVRAE PVQTVLRGTT VQFMSSDNEL QDAYSKQSCL YEELSSALDN FAKTINVGLK
SPVERMEVCC TEAELLHAEK EEEEDEKKTK KNDAKGKEAR LPRCISAPVE SVPQAGGTFA
KKRNTSLGAS KLRRGMPNSL KSGLREPKTP FSSPLKNQQQ ANIKASLDNM DKNNSVVVAV
DEPERNLEIE SKENIIQTTK VSSINMDIVE DDEFKDSDTK KQIILQQINP DDDDNHPASE
VGFCIRPSVN FIREHRKGHV RSKIQEFTDR ESRLEFVGEE TDSSSVIGQS PAEISKRTTT
TSKPTATRKP SSSSGTSKPL NIKFSACF
//
