ID A0A077ZF73_TRITR Unreviewed; 519 AA.
AC A0A077ZF73;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Protein kinase C binding protein NELL1 {ECO:0000313|EMBL:CDW57280.1};
GN ORFNames=TTRE_0000557101 {ECO:0000313|EMBL:CDW57280.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57280.1};
RN [1] {ECO:0000313|EMBL:CDW57280.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW57280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; HG806144; CDW57280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZF73; -.
DR STRING; 36087.A0A077ZF73; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 6.20.200.20; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24042:SF5; EGF_CA DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24042; NEL HOMOLOG; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00093; VWC; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00214; VWC; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57603; FnI-like domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Kinase {ECO:0000313|EMBL:CDW57280.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CDW57280.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..519
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001728701"
FT DOMAIN 312..370
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 371..433
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 434..473
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 474..514
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 519 AA; 59110 MW; FDF8882F7EBCAC7A CRC64;
MAFSIGPLLV VIAAIEAFCL SSTAGQHLEL DGIKEPVTLD ERQTQDVASL LLRKNFSILL
QFVQVEHTQG TLFYVHTSRG KIFELYSSGI KGQLIVFWRR KYRVANLEVR YELDDEDTHQ
IIFELRNQYL RLVVDCIEAV TGEYPEIDFK LLLQAQLVHA HIGQRDQRKS RFYGEIKKFI
ISSAPLSHRF CGARYYETQR LPTVSPSITV RDDPASLSGF RGSQSDVDLM RNIERRMQQL
EEITRNWGKQ ENDQVGAANA EEPTVPTGTG TCPNCWEYLR FKVNYLEEEF KRWRESISTI
GERVNSVLLQ NRGCVLNGTL LNDGFRWRNE TACIDCVCHL GELYCHPIGC PQLACSNVVK
VDGQCCPECG QSCHYMGKDY DHGKVFWPKL CVRCRCNNGD MQCSYESTSM CPRLQCPKEL
QITLENRCCP VCIHNDFCSL DPCHPDATCT NEQYGRKCRC KNGFFGDGEE HCVDINECLN
QSACGIGSRC VNTPGSYKCQ CLPGYHKLND FNCLNVIIH
//
