AIF1_PIG
ID AIF1_PIG Reviewed; 146 AA.
AC P81076;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Allograft inflammatory factor 1;
DE Short=AIF-1;
DE AltName: Full=Daintain;
GN Name=AIF1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC TISSUE=Intestine;
RX PubMed=9391121; DOI=10.1073/pnas.94.25.13879;
RA Chen Z.-W., Ahren B., Oestenson C.-G., Cintra A., Bergman T., Moeller C.,
RA Fuxe K., Mutt V., Joernvall H., Efendic S.;
RT "Identification, isolation, and characterization of daintain (allograft
RT inflammatory factor 1), a macrophage polypeptide with effects on insulin
RT secretion and abundantly present in the pancreas of prediabetic BB rats.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13879-13884(1997).
CC -!- FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC
CC activation. Enhances the actin-bundling activity of LCP1. Binds
CC calcium. Plays a role in RAC signaling and in phagocytosis. May play a
CC role in macrophage activation and function. Promotes the proliferation
CC of vascular smooth muscle cells and of T-lymphocytes. Enhances
CC lymphocyte migration. Plays a role in vascular inflammation (By
CC similarity). Has a dual influence on glucose-induced insulin secretion:
CC inhibition at low concentration and stimulation at high concentrations.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Potential). Monomer. Interacts with LCP1 (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O70200}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:O70200}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O70200}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O70200}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:O70200}. Note=Associated with the actin
CC cytoskeleton at membrane ruffles and at sites of phagocytosis.
CC {ECO:0000250|UniProtKB:O70200}.
CC -!- TISSUE SPECIFICITY: Microglial cells in the central nervous system and
CC dendritic cells and macrophages in several organs.
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DR AlphaFoldDB; P81076; -.
DR SMR; P81076; -.
DR STRING; 9823.ENSSSCP00000001497; -.
DR iPTMnet; P81076; -.
DR PaxDb; P81076; -.
DR PeptideAtlas; P81076; -.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; P81076; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB.
DR InterPro; IPR042433; AIF1/AIF1L.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10356; PTHR10356; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calcium; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..146
FT /note="Allograft inflammatory factor 1"
FT /id="PRO_0000073868"
FT DOMAIN 44..79
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..115
FT /note="EF-hand 2; degenerate"
FT /evidence="ECO:0000305"
FT REGION 127..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9391121"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55008"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55008"
SQ SEQUENCE 146 AA; 16560 MW; 018FD1D8698E86EF CRC64;
SETIDLQGGK AFGLLKAQQE GRLNEINKQF LDDPKYSSDE DLSRKLEAFK QKYMEFDLNG
NGDIDIMSLK RMLEKLGVPK THLELKKLIK EVSSGSGETF SYSIFLKMML GKRSAILKMI
LMYEEKAREQ EKPTGPPAKK AISELP
