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Database: UniProt
Entry: A0A026WRV7_OOCBI
LinkDB: A0A026WRV7_OOCBI
Original site: A0A026WRV7_OOCBI 
ID   A0A026WRV7_OOCBI        Unreviewed;       870 AA.
AC   A0A026WRV7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Protein kinase C-binding protein NELL1 {ECO:0000313|EMBL:EZA57839.1};
GN   ORFNames=X777_00941 {ECO:0000313|EMBL:EZA57839.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA57839.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA57839.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
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; KK107139; EZA57839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WRV7; -.
DR   STRING; 2015173.A0A026WRV7; -.
DR   OMA; TCGQFLE; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 5.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 6.20.200.20; -; 3.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
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; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR24042:SF5; EGF_CA DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24042; NEL HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF00093; VWC; 3.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57603; FnI-like domain; 4.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 5.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 4.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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}; Kinase {ECO:0000313|EMBL:EZA57839.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:EZA57839.1}.
FT   DOMAIN          273..329
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          330..393
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          394..433
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          434..479
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          480..520
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          521..551
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          553..591
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          600..644
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          645..701
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          704..763
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   REGION          823..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          235..269
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        523..533
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        541..550
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   870 AA;  96863 MW;  6BE3BB49930F3117 CRC64;
     MAVLICLMDG YSHKQQPFGR DVLIEYARSM IDLHIASFSN DIDAERLTPA TELKIRRLCE
     ERELRLNEAS FERAAALLRR VPEFTIAAAL RQEEANSGTI VAFSHGNNRY LELQSSGRKD
     ELRLHYVSRR DGTVHVEAFP FRLADGAWHR VALSISGSQV ELLVDCHPLY RRLLRPGPPD
     TNFTLPQLQL WVGQRNVRHF LFKGALQDVK LIAGPHGYLS QCPQLDSSCP TCGQFSILQN
     TVEQLMHNLN ELTRRLAAAE GRISKVEECE CQKSCRANGT VHEDGAIWEK GCQQCSCIHG
     EVECRPTPCS PVTCKNPVIR KGECCPSCLK QCYLRGVIYD HGEKVSPKQC VECDCYDGSF
     TCNRFDTDTR CPPLPCPPEK QISVAEECCK FCPGVDYCAK GHKCHANASC LNLQTTYACH
     CHIGFQGDGL NCHDVDECKQ QGGSDGHHCN ANTRCVNAIG SYTCECLPGY YRIDKFNCAE
     MDECANNSHK CDKHATCVNT AGSYYCICND GYVGDGYTCK PVCNQTCQNG GECVAPERCS
     CRRGYIGNSC ELDLDECASD LHRCHQSSTC FNMPGWYYCR CKPGYRSALH DSTQGTQCVD
     IDECNDLTLE RKHTCHPTAK CVNTEGGYEC VCPKDSDESG VECKLSCWFE DREVNNGDVL
     APAGNPCRRC TCQDGVITCK DPVCDCSAPG SHRDKCCPQC DPAASCRHQE LHHLVFRSGE
     RWIYQCQTCE CLYGEIDCWQ MECPPVTCSN PVTEEGDCCP RCEDDPCARE VLANGTLLTV
     PSRPQPCSYA GIIHDSGSSW QDPYDKCTTC ECKVRTRIGC NNRPSQDQQS PVLRSGPVRD
     LKDTDRIRGV SPKNADAMGT ETADDRLEDY
//
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