MPEG1_BOVIN
ID MPEG1_BOVIN Reviewed; 717 AA.
AC Q2KJC3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Macrophage-expressed gene 1 protein;
DE Short=Macrophage gene 1 protein;
DE Short=Mpg-1;
DE AltName: Full=Perforin-2 {ECO:0000250|UniProtKB:Q2M385};
DE Short=P-2 {ECO:0000250|UniProtKB:Q2M385};
DE Flags: Precursor;
GN Name=MPEG1;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a key role in the innate immune response following
CC bacterial infection by polymerizing and inserting into the bacterial
CC surface to form pores (By similarity). By breaching the surface of
CC phagocytosed bacteria, allows antimicrobial effectors to enter the
CC bacterial periplasmic space and degrade bacterial proteins such as
CC superoxide dismutase sodC which contributes to bacterial virulence (By
CC similarity). Shows antibacterial activity against a wide spectrum of
CC Gram-positive, Gram-negative and acid-fast bacteria (By similarity).
CC Reduces the viability of the intracytosolic pathogen L.monocytogenes by
CC inhibiting acidification of the phagocytic vacuole of host cells which
CC restricts bacterial translocation from the vacuole to the cytosol (By
CC similarity). Required for the antibacterial activity of reactive oxygen
CC species and nitric oxide (By similarity).
CC {ECO:0000250|UniProtKB:A1L314}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:A1L314}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Bacterial infection induces translocation of the
CC cytoplasmic vesicles to bacterium-containing phagocytic vesicles and
CC fusing of the vesicles. {ECO:0000250|UniProtKB:A1L314}.
CC -!- PTM: Monoubiquitinated in response to bacterial infection;
CC ubiquitination is required for vesicular localization and antibacterial
CC activity and can be blocked by bacterial cell cycle inhibiting factor
CC (cif) (By similarity). {ECO:0000250|UniProtKB:A1L314}.
CC -!- SIMILARITY: Belongs to the MPEG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05416.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC105415; AAI05416.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001039929.1; NM_001046464.1.
DR AlphaFoldDB; Q2KJC3; -.
DR SMR; Q2KJC3; -.
DR PRIDE; Q2KJC3; -.
DR GeneID; 539997; -.
DR KEGG; bta:539997; -.
DR CTD; 219972; -.
DR InParanoid; Q2KJC3; -.
DR OrthoDB; 235876at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035915; P:pore formation in membrane of another organism; ISS:UniProtKB.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR039707; MPEG1.
DR PANTHER; PTHR31463; PTHR31463; 1.
DR Pfam; PF01823; MACPF; 1.
DR SMART; SM00457; MACPF; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Cytoplasmic vesicle; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..717
FT /note="Macrophage-expressed gene 1 protein"
FT /id="PRO_0000324142"
FT TOPO_DOM 18..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..345
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 717 AA; 78413 MW; 9AF152AC3C6F2B87 CRC64;
MNSFRGAFLI WAVATWAETD TSWGATDEPG FQNCKNALKL PVLPVLPGGG WDNLRNVDTG
RVMELAYSHC RTTEDGQYIV PDEIFTIPQK QSNLEMNSKI LESWVNYQSS TSNSINMELS
LFSKVNGKFS LEFQRIKTLQ VKDQAVTTQV QVRNLVYTVK INPDAELSLG FKKALMDISE
QLENNQTRMA TYLAELLVLN YGTHVITSVD AGAALIQEDH IRSSFLQDSQ SSRSAVTASA
GITFLNIVNF KFEENYTSQN TFTKSYLSNR TNSRVQSFGG LPFYPGITLQ AWQQGVSNHL
VAMDRAGLPL YFFINPERLP DLPGPLVRKL SKTVEAAVRR YYAVNTYPGC TDLSSPNFNF
QANTDDGSCE GKMTNFSFGG VYQECTQFSG NEVVQLCQNL EQKNPLTGSV SCPSGYSPVQ
LLTQTHEEGY NHLECSRKCT LYIFCKTVCE DVFRVARAEF RAFWCAASGQ VSENSGLLFG
GLFSGKSINP LTNAQSCPAG YFQLKLFENL KVCASLDYEL GYRFSIPFGG FFSCAAGNPL
VDSATSKDLG APSLRKCPGG FSQHLALISD GCQVSYCVKA GLFTGGSLPP VRLPPYTRPP
LMSQVATNTV LVTNHETASS WIKDPQTHQW RLGEPLELRR AMRVVHGDGE GLSGGAAAGL
TLGVTIALAG VVALAIYGAR KSRKKGYQAL QDEKQSLAAG AAVNGDALDQ EQAQNPA
