ID A0A0V1LTL8_9BILA Unreviewed; 1588 AA.
AC A0A0V1LTL8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protein NDNF {ECO:0000313|EMBL:KRZ62446.1};
GN Name=NDNF {ECO:0000313|EMBL:KRZ62446.1};
GN ORFNames=T02_6545 {ECO:0000313|EMBL:KRZ62446.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62446.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ62446.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62446.1};
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 -!- 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:KRZ62446.1}.
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DR EMBL; JYDW01000009; KRZ62446.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 4.10.75.10; Elafin-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR036645; Elafin-like_sf.
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; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00217; WAP; 2.
DR SUPFAM; SSF57256; Elafin-like; 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS51390; WAP; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..139
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 211..261
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 873..1081
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1371..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 179275 MW; 621A2C00E502F670 CRC64;
MLPQQVPWVC INSNWRSGWV STFVQTGRHL RFVCRRSVLA NDAGSVAQFR LPRYTAKLIY
CILIVFHMLY TRLLFSLCVV ICLTPVSHLQ RVKVGRCPEL PARYPTPQPQ YDRCRDDYDC
ESTMKCCESI IGKVCMMPKD YDQREVCKQP YTKWDSCGSG CMITCYNIGW QQPCRQPCQP
GCTCISGFVR LYLHPYAPCV PQTHCPNQRT TRTKFGVCPT LPHGAEIDYH RRRDRCGTDF
DCSGYMKCCE SIIGKACMLP LCTCPDGQKT SIFCDERDSC PWGYTCRSGL CCPNAQWQSP
TATWPGQVTT AAGNCPHYAY IGTWAQLAPT CFTNSNCAYN QLCCYTYFGN RCIQVSQLGN
STMYVTVSPC GGAVRWKLTN LPVSTLNNKP TLSFYIKKQN YMTNVIKESY YSDSLYEYEE
TLYKNAGEKQ MNYVSHKASI LHLRLYLTGL RSICKVEIHF GTTPVEKRPF FQLFHLTQPK
IDNVQSKSAT LSWQPSISAL LYTGGRLVYV IALSTVRPFA TLCDLETDLK LDRVDILEHR
RQEHVAHRLI PQHHSGAVRS LTVLDAARPA KLQLISLQQN TNYYVNVFAL DLNTGENIAY
DTVSFTTTSE NQVSQHRLVS SITEAQLQTG YLGPSRVAFK VYQFSAPVAI SELYILIQPC
TGPLQAAIYQ DGQKTLHYSI EELQTINLTD VNAGIVQIQI ANDDNQAKMF NIWASNNLSA
YPYPKLPYDT SITVTERKCD SVQLSWLAST DAHVYCLYKR LQRFDYFKQL ILEDWNLCQQ
PDENLQPLFC NRFRGNHYRN EILIQEIAAL KPATTYRFDL FVSKHSQPSL AYRTVWMMTQ
STTCQTISLW VNKYLRRSRT QEMDSPPNPL VLSGLRSLLY TFADGVTFTV PIFLHKAFSV
LEAHYLTTEG IFRKPGIASK LRVLKNCFNA SSALELNFKI EEVSPFDLCD LIKLFLREID
EPILTWGLQP QFLQFADLNT PRDVRTKCLL QLCHALPPRH KETLAFIMRF LKMISNSSAY
NKMDVKNLAT VFVPCIFRES AKARPVKHGQ ALLDELAASK NDIALKVDVL EMLIQNADSI
GVLSEQERAI LAAESSDKLN DDLNIFKRSA KKAASKVLVR SRNSLSGNRN SQIYRRSVQP
KLKSAESIER HERIKGSRIT EPYKRRSVCS LEKSQGLSDK GENGIIRQNR CLEEKHVKPM
RSSMFETMMY SSAFTEGVAA TSGAVEEQCT TSSPIVRTSS LPDRKVISIS TENRESVKVN
KAESELVRAE PIQTVLRGTT VQFMSSDNEL QDAYGKQSCL YEELSSALDN FAKTINVGAM
KSPVERMEVC TEEEKKKKNA DDGKEKEARL PRCISAPVES VPQVGGTFAK KRNTSLGASK
LRRGMPNSLK SGLREPKTPF SSPLKSQQQA NMMRSSSSSS NNLDKKNNMV VVGVDQREQN
LEIESKENII QPTKPSSINM DIVEDDEFKD SDTKKQIILQ QINPDDDPAS AVGFCIRPSV
NFIREHRKGH VRSKIQEFTD RESRLEFVGE EADSSSVIGQ SLAEVSKRVT ATATTTTSKP
TATRKPSSTS GNNNNKGCSL NIKFSACF
//
