AIF1_MACMU
ID AIF1_MACMU Reviewed; 147 AA.
AC Q5TM25;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Allograft inflammatory factor 1;
DE Short=AIF-1;
GN Name=AIF1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
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). {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 -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
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DR EMBL; AB128049; BAD69720.1; -; Genomic_DNA.
DR RefSeq; NP_001040583.1; NM_001047118.1.
DR AlphaFoldDB; Q5TM25; -.
DR BMRB; Q5TM25; -.
DR SMR; Q5TM25; -.
DR STRING; 9544.ENSMMUP00000007001; -.
DR Ensembl; ENSMMUT00000088853; ENSMMUP00000074541; ENSMMUG00000049735.
DR GeneID; 574115; -.
DR KEGG; mcc:574115; -.
DR CTD; 199; -.
DR VEuPathDB; HostDB:ENSMMUG00000049735; -.
DR VGNC; VGNC:81011; AIF1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013846; -.
DR HOGENOM; CLU_134149_0_0_1; -.
DR InParanoid; Q5TM25; -.
DR OMA; NKYMEFD; -.
DR TreeFam; TF320736; -.
DR Proteomes; UP000006718; Chromosome 4.
DR Bgee; ENSMMUG00000049735; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; Q5TM25; baseline.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0051764; P:actin crosslink formation; IEA:Ensembl.
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:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
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 3: Inferred from homology;
KW Acetylation; Actin-binding; Calcium; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P81076"
FT CHAIN 2..147
FT /note="Allograft inflammatory factor 1"
FT /id="PRO_0000073866"
FT DOMAIN 45..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..115
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P81076"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55008"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55008"
SQ SEQUENCE 147 AA; 16719 MW; 70B2179D24C6E29E CRC64;
MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLLSKLEGF KEKYMEFDLN
GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM
ILMYEEKARE KEKPTGPPAK KAISELP
