ID F1KTR9_ASCSU Unreviewed; 997 AA.
AC F1KTR9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Neurogenic locus notch protein {ECO:0000313|EMBL:ADY41273.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY41273.1};
RN [1] {ECO:0000313|EMBL:ADY41273.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JI165734; ADY41273.1; -; mRNA.
DR AlphaFoldDB; F1KTR9; -.
DR EnsemblMetazoa; AgE14_g007_t04; AgE14_g007_t04; AgE14_g007.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 3.30.70.3310; -; 1.
DR Gene3D; 4.10.470.20; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR000800; Notch_dom.
DR PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00066; Notch; 2.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF90193; Notch domain; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50258; LNR; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..997
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003266473"
FT TRANSMEM 443..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..75
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 77..121
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 123..161
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 163..196
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 210..250
FT /note="LNR"
FT /evidence="ECO:0000259|PROSITE:PS50258"
FT REPEAT 741..773
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 774..806
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 807..829
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 699..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 65..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 111..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 151..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 186..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 997 AA; 110398 MW; 91499DC90D43C048 CRC64;
MKRCCATSAY SDAIFEWMLL LIGGLKCAVE VGGCTQMPCN NGGICIVDRN VSSPHIKGIG
GSCICPAGFG GELCEVKLRS CYEEPCRNGA LCIPLDESAD NSKEEQFICR CRYGWKGTFC
EEDVDECEEY AQYCGNGGTC VNSNGSAMCL CPMGFTGDNC ERPLDRCKLE GFCKNGGTCD
EQFCICQDGY SGDRCERVVP YWEDYRRAHC TEYPEFCALR FADGKCNEEC NDQNCFYDGF
DCIRNSTAKC RMPAFCAAKY NDGECDHICS GVECGFDGGD CDMSSSRQSD KENSLALIIN
ASPEIVLWKL RPLLASLARM LHSSVRISRD AANMSEIFVW STSDGVGERI DIRNTSRYVH
SGKNADGVIL FMDIDVSGCL RRRQESLGSP SFPCFTSASN AAVFLLAALS SETDGERKVL
GLTIDEVYAK GDRIKHSAPS KDIFRLLVAI AVVLLVVLSI IALFGFNGIL RRRKRQQTSS
LRTWIVPRDD RTKNFAVNGC DGMHSDYFPH EYKTVEVLPD KRFKCSSTEE QENVRLSYEN
VLDTTDEQAV PTETKEYFCD DSLFEPCVVC TENKNEEDTE PELIKAVREG CLDKVGELVA
KGIDVNCEDA DGNSALHHAI LANNVLVLRL LLATHKCNLY AVNALGQMPL TLTVSKPHVS
QECARILLDA MNEENTAIQR ATDDIALLRS DASLGNSTTP ISASTKIKKR SPPQCVSPSE
NGPLSRFVLC ESDERSVIDL YGRSALHYAA LNNRPQLLAL FYSNGLKLDH RDNKGETALH
LAAREGHYAS VEMLLSLGAN KEVTDQLGRT AYHMAAERNR AEVMELLLKS PKSSSRFTTL
PGVKRKRRTK LRRPARTSSP PHERGYSSAM ELQLPDMLKQ RHDLSKNDQD AHSKNSSGTL
TRSSPSSHFE ERPNASPAAS LRVLTPQEEI LQAAHFNFEF LPPAASEENN GQWYDEDFLD
GVPCIMSESL ISEQLFKNLE DITKDISAEL SDTMLDG
//
