NIPI4_CAEEL
ID NIPI4_CAEEL Reviewed; 396 AA.
AC O16262;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein nipi-4 {ECO:0000305};
DE AltName: Full=No induction of peptide after drechmeria infection protein 4 {ECO:0000312|WormBase:F40A3.5};
GN Name=nipi-4 {ECO:0000312|WormBase:F40A3.5};
GN ORFNames=F40A3.5 {ECO:0000312|WormBase:F40A3.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLY-299.
RX PubMed=22470487; DOI=10.1371/journal.pone.0033887;
RA Labed S.A., Omi S., Gut M., Ewbank J.J., Pujol N.;
RT "The pseudokinase NIPI-4 is a novel regulator of antimicrobial peptide gene
RT expression.";
RL PLoS ONE 7:E33887-E33887(2012).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Pseudokinase which plays a role in resistance to fungal
CC infection by promoting expression of antimicrobial peptides (nlp-29,
CC nlp-31, nlp-34, cnc-1, cnc-2 and cnc-4) in the epidermis. In addition,
CC up-regulates nlp-29 expression upon physical wounding and in response
CC to phorbol ester PMA treatment. {ECO:0000269|PubMed:22470487}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis of larvae and adults and
CC in vulval and rectal cells. {ECO:0000269|PubMed:22470487}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; BX284605; CCD66964.1; -; Genomic_DNA.
DR RefSeq; NP_505028.3; NM_072627.5.
DR AlphaFoldDB; O16262; -.
DR SMR; O16262; -.
DR STRING; 6239.F40A3.5; -.
DR EPD; O16262; -.
DR PaxDb; O16262; -.
DR PeptideAtlas; O16262; -.
DR EnsemblMetazoa; F40A3.5.1; F40A3.5.1; WBGene00077712.
DR EnsemblMetazoa; F40A3.5.2; F40A3.5.2; WBGene00077712.
DR GeneID; 179167; -.
DR KEGG; cel:CELE_F40A3.5; -.
DR UCSC; F40A3.5; c. elegans.
DR CTD; 179167; -.
DR WormBase; F40A3.5; CE44387; WBGene00077712; nipi-4.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000168088; -.
DR HOGENOM; CLU_700648_0_0_1; -.
DR InParanoid; O16262; -.
DR OMA; EPHYQRT; -.
DR OrthoDB; 846812at2759; -.
DR PhylomeDB; O16262; -.
DR PRO; PR:O16262; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00077712; Expressed in embryo and 3 other tissues.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="Protein nipi-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433880"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 81..368
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 299
FT /note="G->E: In fr68; severe loss of nlp-29 expression upon
FT D.coniospora infection."
FT /evidence="ECO:0000269|PubMed:22470487"
SQ SEQUENCE 396 AA; 45182 MW; 32DA9C010848D149 CRC64;
MELDHTPPPS VLNDNCSASY MTPYATVIAM SGLYLLAIFY FCKKSKKMCQ PMSDSIYPYQ
KRLTQLEREL KNYLIDEESI EVDDFQIGQT ADGFIFRGGV FPKTRNRFNA KVTTAVKISF
PIVSKSISLL EDALRLSKLD HPNLIRLLAV SQLSFTVFRP MIALEWLPGG TLADYFQFKV
REKDDSERSP IQLKDMLSIL YQVSQALKYI HSQLDEFGQE LTHGRIFTRN VLVTEPDLRK
CEVKLGDFGD APMGLEYSTP IIAYMPPEIL CCAERIPPHR PENDVWMFGV FIWECLTLGA
QPHFRKSVEE IKKSFRLPDR GLSCPPTCPL DVWTLVSDCL SEPHMRPRFA STTNASITSR
LSELHHIVSP ALFLYAIPNQ SVCTCIEHHC QSVIHY
