NCF2_BOVIN
ID NCF2_BOVIN Reviewed; 527 AA.
AC O77775;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Neutrophil cytosol factor 2;
DE Short=NCF-2;
DE AltName: Full=67 kDa neutrophil oxidase factor;
DE AltName: Full=Neutrophil NADPH oxidase factor 2;
DE AltName: Full=p67-phox;
GN Name=NCF2;
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].
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).
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).
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 with NCF4. Interacts
CC (via the C-terminal SH3 domain) with NCF1 (via C-terminus). Interacts
CC with SYTL1 and RAC1. May interact with NOXO1. Interacts with S100A8 and
CC calprotectin (S100A8/9) (By similarity). Interacts with GBP7 (via
CC GB1/RHD3-type G domain) (By similarity). Interacts with CYBB; the
CC interaction is enhanced in the presence of GBP7 (By similarity).
CC {ECO:0000250|UniProtKB:O70145, ECO:0000250|UniProtKB:P19878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The OPR/PB1 domain mediates the association with NCF4/p40-PHOX.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NCF2/NOXA1 family. {ECO:0000305}.
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DR EMBL; AF079303; AAC82463.1; -; mRNA.
DR RefSeq; NP_776545.1; NM_174120.2.
DR AlphaFoldDB; O77775; -.
DR SMR; O77775; -.
DR IntAct; O77775; 2.
DR STRING; 9913.ENSBTAP00000010525; -.
DR PaxDb; O77775; -.
DR PeptideAtlas; O77775; -.
DR PRIDE; O77775; -.
DR GeneID; 281346; -.
DR KEGG; bta:281346; -.
DR CTD; 4688; -.
DR eggNOG; KOG4225; Eukaryota.
DR InParanoid; O77775; -.
DR OrthoDB; 431898at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043020; C:NADPH oxidase complex; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IEA:InterPro.
DR GO; GO:0045730; P:respiratory burst; IEA:InterPro.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR CDD; cd06406; PB1_P67; 1.
DR CDD; cd11871; SH3_p67phox_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034889; P67-PHOX.
DR InterPro; IPR035546; p67phox_SH3_1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034885; PB1_P67.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR15175:SF3; PTHR15175:SF3; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW TPR repeat.
FT CHAIN 1..527
FT /note="Neutrophil cytosol factor 2"
FT /id="PRO_0000106360"
FT REPEAT 37..70
FT /note="TPR 1"
FT REPEAT 71..104
FT /note="TPR 2"
FT REPEAT 121..154
FT /note="TPR 3"
FT DOMAIN 240..299
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 352..430
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 458..517
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 304..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70145"
SQ SEQUENCE 527 AA; 59663 MW; 430D33FE1DF68BD1 CRC64;
MSLAEAISLW NEGVLAADKK DWKGALDAFT GVQDPHSRIC FNVGCIYTIL GNLPEAEKAF
TKSINRDKHL AVSYFQRGML YYQMEKYDSA IKDLKEALTQ LRGNQLIDYK ILGLQFKLFA
CEVLYNIAFM YAKREEWKKA EEHLALAVSM KSEPRHSKID RAMESVWKQK LYEPVVIPVG
RLFRPNEKQV AQLVKKDYLG KATVVASVVD QDSFSGFAPL QPQAAEPPPR PKTPEIFRAL
EGEAHRVLFG FVPETPEELQ VMPGNIVFVL KKGNDNWATV MFNGQKGLVP CNYLEPVELR
IHPQQQPQEE TSLESDIPAP PSSSAPGRPQ LSPGQKGKEE PKQEIKLSVP KSYTLKVHYK
YTVVMETQFR LPYSQVRDMV AKKLDLLPEH TKLSYRRQDS NELVPLSEFS MKDAWAQVKN
YCLTLWCENT VGDQGFPDEP EESKKSDANN QTTEPELKEG SKVVALFSYE ATQPEDLEFL
EGDVILVIST VNEQWLEGEC KGKVGIFPKA FVEQHPTTDL ESTPGRV
