AIF1_RAT
ID AIF1_RAT Reviewed; 147 AA.
AC P55009; P55007; P70491;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Allograft inflammatory factor 1;
DE Short=AIF-1;
DE AltName: Full=Ionized calcium-binding adapter molecule 1;
DE AltName: Full=MRF-1;
DE AltName: Full=Microglia response factor;
GN Name=Aif1; Synonyms=Iba1, Mrf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Lewis; TISSUE=Heart;
RX PubMed=7769138; DOI=10.1172/jci118003;
RA Utans U., Arceci R.J., Yamashita Y., Russell M.E.;
RT "Cloning and characterization of allograft inflammatory factor-1: a novel
RT macrophage factor identified in rat cardiac allografts with chronic
RT rejection.";
RL J. Clin. Invest. 95:2954-2962(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=7783423;
RA Autieri M.V., Feuerstein G.Z., Yue T.-L., Ohlstein E.H., Douglas S.A.;
RT "Use of differential display to identify differentially expressed mRNAs
RT induced by rat carotid artery balloon angioplasty.";
RL Lab. Invest. 72:656-661(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=8713135; DOI=10.1006/bbrc.1996.1112;
RA Imai Y., Ibata I., Ito D., Ohsawa K., Kohsaka S.;
RT "A novel gene iba1 in the major histocompatibility complex class III region
RT encoding an EF hand protein expressed in a monocytic lineage.";
RL Biochem. Biophys. Res. Commun. 224:855-862(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9698327; DOI=10.1523/jneurosci.18-16-06358.1998;
RA Tanaka S., Suzuki K., Watanabe M., Matsuda A., Tone S., Koike T.;
RT "Upregulation of a new microglial gene, mrf-1, in response to programmed
RT neuronal cell death and degeneration.";
RL J. Neurosci. 18:6358-6369(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(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 an
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 -!- TISSUE SPECIFICITY: Cardiac allograft, spleen and testis. Expressed by
CC inflammatory cells (macrophages and neutrophils).
CC -!- DEVELOPMENTAL STAGE: Expressed early and persistently in chronically
CC rejecting cardiac allografts but is absent in cardiac syngrafts and
CC host hearts. In the embryonic cerebellum, expression peaks at day 7.
CC -!- INDUCTION: By interferon gamma.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB06590.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB06590.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; U17919; AAA80105.1; -; mRNA.
DR EMBL; U33471; AAB06590.1; ALT_SEQ; mRNA.
DR EMBL; D82069; BAA11533.1; -; mRNA.
DR EMBL; AB000818; BAA19189.1; -; mRNA.
DR EMBL; BX883046; CAE83999.1; -; Genomic_DNA.
DR PIR; I55617; I55617.
DR PIR; JC4902; JC4902.
DR RefSeq; NP_058892.1; NM_017196.3.
DR RefSeq; XP_006256127.1; XM_006256065.2.
DR AlphaFoldDB; P55009; -.
DR SMR; P55009; -.
DR STRING; 10116.ENSRNOP00000001135; -.
DR iPTMnet; P55009; -.
DR PhosphoSitePlus; P55009; -.
DR PaxDb; P55009; -.
DR GeneID; 29427; -.
DR KEGG; rno:29427; -.
DR CTD; 199; -.
DR RGD; 61924; Aif1.
DR VEuPathDB; HostDB:ENSRNOG00000000853; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_134149_0_0_1; -.
DR InParanoid; P55009; -.
DR OMA; NKYMEFD; -.
DR OrthoDB; 1557466at2759; -.
DR PRO; PR:P55009; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000853; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; P55009; baseline and differential.
DR Genevisible; P55009; RN.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0051764; P:actin crosslink formation; ISO:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEP:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
DR GO; GO:0071315; P:cellular response to morphine; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
DR GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; ISO:RGD.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:RGD.
DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:RGD.
DR GO; GO:0014739; P:positive regulation of muscle hyperplasia; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
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; IMP:RGD.
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:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
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 2: Evidence at transcript level;
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_0000073869"
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; degenerate"
FT /evidence="ECO:0000305"
FT REGION 127..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 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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"
FT CONFLICT 2..9
FT /note="SQSKDLQG -> MKPEEISR (in Ref. 3; BAA11533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16827 MW; 76EA1DAC977A71DA CRC64;
MSQSKDLQGG KAFGLLKAQQ EERLDGINKH FLDDPKYSSD EDLQSKLEAF KTKYMEFDLN
GNGDIDIMSL KRMLEKLGVP KTHLELKKLI REVSSGSEET FSYSDFLRMM LGKRSAILRM
ILMYEEKNKE HQKPTGPPAK KAISELP
