NCF1_BOVIN
ID NCF1_BOVIN Reviewed; 392 AA.
AC O77774; Q5E9R8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Neutrophil cytosol factor 1;
DE Short=NCF-1;
DE AltName: Full=47 kDa neutrophil oxidase factor;
DE AltName: Full=NCF-47K;
DE AltName: Full=Neutrophil NADPH oxidase factor 1;
DE AltName: Full=p47-phox;
GN Name=NCF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10647999; DOI=10.1002/jlb.67.1.63;
RA Bunger P.L., Swain S.D., Clements M.K., Siemsen D.W., Davis A.R.,
RA Gauss K.A., Quinn M.T.;
RT "Cloning and expression of bovine p47-phox and p67-phox: comparison with
RT the human and murine homologs.";
RL J. Leukoc. Biol. 67:63-72(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required
CC for activation of the latent NADPH oxidase (necessary for superoxide
CC production). {ECO:0000269|PubMed:10647999}.
CC -!- SUBUNIT: Component of an NADPH oxidase complex composed of a
CC heterodimer formed by the membrane proteins CYBA and CYBB and the
CC cytosolic subunits NCF1, NCF2 and NCF4. Interacts (via C-terminus) with
CC NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts
CC with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts
CC with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with
CC FASLG (By similarity). Interacts with PARK7 (via C-terminus); the
CC interaction is enhanced by LPS and modulates NCF1 phosphorylation and
CC membrane translocation (By similarity). {ECO:0000250|UniProtKB:P14598,
CC ECO:0000250|UniProtKB:Q09014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10647999}.
CC Membrane {ECO:0000250|UniProtKB:P14598}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14598}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P14598}.
CC -!- DOMAIN: The PX domain mediates interaction with phosphatidylinositol
CC 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited,
CC unphosphorylated state an intramolecular interaction with the C-
CC terminal SH3 domain precludes phospholipid binding and interaction with
CC CYBA. Phosphorylation disrupts the autoinhibited state (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by PRKCD; phosphorylation induces activation of
CC NCF1 and NADPH oxidase activity. {ECO:0000250}.
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DR EMBL; AF079302; AAC82462.1; -; mRNA.
DR EMBL; BT020852; AAX08869.1; -; mRNA.
DR EMBL; BT021181; AAX31363.1; -; mRNA.
DR EMBL; BC103145; AAI03146.1; -; mRNA.
DR RefSeq; NP_776544.1; NM_174119.4.
DR AlphaFoldDB; O77774; -.
DR SMR; O77774; -.
DR STRING; 9913.ENSBTAP00000004279; -.
DR PaxDb; O77774; -.
DR PRIDE; O77774; -.
DR GeneID; 281345; -.
DR KEGG; bta:281345; -.
DR CTD; 653361; -.
DR eggNOG; KOG4773; Eukaryota.
DR HOGENOM; CLU_030529_0_0_1; -.
DR InParanoid; O77774; -.
DR OrthoDB; 1183210at2759; -.
DR TreeFam; TF329347; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0045730; P:respiratory burst; IBA:GO_Central.
DR GO; GO:0042554; P:superoxide anion generation; ISS:UniProtKB.
DR CDD; cd06887; PX_p47phox; 1.
DR CDD; cd12021; SH3_p47phox_1; 1.
DR CDD; cd12022; SH3_p47phox_2; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR015039; NADPH_oxidase_p47Phox_C.
DR InterPro; IPR035756; NCF1_SH3_1.
DR InterPro; IPR035757; NCF1_SH3_2.
DR InterPro; IPR032136; NECFESHC.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034909; PX_p47phox.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15706:SF6; PTHR15706:SF6; 1.
DR Pfam; PF16621; NECFESHC; 1.
DR Pfam; PF08944; p47_phox_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00498; P47PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..392
FT /note="Neutrophil cytosol factor 1"
FT /id="PRO_0000096761"
FT DOMAIN 4..125
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 156..215
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 226..285
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 290..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14598"
SQ SEQUENCE 392 AA; 45346 MW; 79199BD86AE80DB7 CRC64;
MGDHFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKILKEMFPI
EAGDINPENR IIPHLPAPRW YDGQRVAESR QGTLTEYCST LMSLPVKISR CPHLLNFFKV
RPDDLKLPTD SQVKKPETYL MPKDGKNNAA DITGPIILQT YRAIADYEKG SSSQMALATG
DVVDVVEKNE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPEPNYAGEP YITIKAYTAV
LEDEISLEEG EAIEVIHKLL DGWWVIRKED VTGYFPSMYL QKAGQDVAQA KSQIKSRGAP
PRRSSIRNAH SIHQRSRKRL SQDTYRRNSV RFMQQRRHQR PEPQRSRSAL REQQQPKTER
PKPQPAVPPR PSADLILHRC SESTKRKLAS AV
