ID A0A0V0U076_9BILA Unreviewed; 833 AA.
AC A0A0V0U076;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Neurogenic locus Notch protein {ECO:0000313|EMBL:KRX44689.1};
GN Name=N {ECO:0000313|EMBL:KRX44689.1};
GN ORFNames=T05_5294 {ECO:0000313|EMBL:KRX44689.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX44689.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX44689.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX44689.1};
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: 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:KRX44689.1}.
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DR EMBL; JYDJ01000091; KRX44689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0U076; -.
DR STRING; 144512.A0A0V0U076; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 4.
DR Gene3D; 2.10.25.10; Laminin; 10.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF12661; hEGF; 3.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 12.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 11.
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 Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 770..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..295
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 303..340
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 342..379
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 381..419
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 464..502
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 505..542
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 544..580
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 582..618
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 620..656
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 658..698
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 700..736
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 799..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 285..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 330..339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 369..378
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 409..418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 532..541
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 570..579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 608..617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 646..655
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 669..686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 688..697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 726..735
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 833 AA; 93523 MW; 244136B29BD20F66 CRC64;
MAPSAVLVHF SRVRAMENFS TILGLLCLVF HLATSELFGY CPNGVRGVYD STNNRCLTMV
KIDLVGEEPN WFESAYNSCT TKYPNSVLFS WFNEEEQIAM IKDAIWKLSG NTTEFSILNG
LYIADVVNNE YDSTMTWEFS NYTHTMTEQL YIMYNKTHQY DWEYETKLIL STKDIYDIYN
LFYSTPICML HKINVGKREF SDKAIPIECY NTTVTAVKAL CSITYDGPQI LNPCDEGFQG
VFCNETIKET TEFPPLYNMS VACANLNCSD HGVCVEIDGK YTCKCYPGHT GKHCEKEHRR
FVDPLGCMNG PFCGSNGDCY QSGDDWKCAC HPGFTGIRCE ESIDLCEIYN PCLNKGKCIT
ENGRLRCKCD RHHVGEFCDF RVNPCTNETI NCGKAGRCVR LNSTEKCWCS AGFTGKECEE
KVDLCDENNM CNFAKQCLTV HEETHSYMQC KCNDWESGKY CTQKRDTCRR KGPCLSRGVC
GLLDDDSYIC HCKQGYHGKF CEIERIHACD DNSTCGEHGK CIRLGNDFLC QCNFGFTGKY
CETRLNSCEF KPCGANGKCN RKHDGYECIC NPGYTGHFCE NTIDMCYTLN PCRRGKCLNK
INGFYCICPE GYMGMACEQK YESCNSELCL NGGTCYMVGE ELKCHCMPGY KGANCARKNN
ICKMHRNICG DHGRCTYDDI DGQIKCVCNI GYDGKYCEKK VTSCSNGNPC RYGNCTVGEN
FFTCQCPTNV TGELCEIGSP ANDDTETDIA DDEDILDDEV DDGIKYDKTY FSLLATAYGI
AISGWIVAIV MLLKHLKNKK TPPPTTTESV TASAGNSVKD EPNNGSNSKA CEA
//
