AIF1L_MOUSE
ID AIF1L_MOUSE Reviewed; 150 AA.
AC Q9EQX4; Q8C150;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Allograft inflammatory factor 1-like;
DE AltName: Full=Ionized calcium-binding adapter molecule 2;
GN Name=Aif1l; Synonyms=Iba2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Imai Y., Kohsaka S.;
RT "Molecular cloning of mouse iba2 cDNA encoding a novel EF-hand calcium-
RT binding protein.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Imai Y., Kohsaka S.;
RT "Complete sequence of mouse iba2 gene.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Actin-binding protein that promotes actin bundling. May
CC neither bind calcium nor depend on calcium for function (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Potential). Monomer (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with F-
CC actin. Partially relocates to membrane ruffles in response to invading
CC bacteria (By similarity). {ECO:0000250}.
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DR EMBL; AB035322; BAB20749.1; -; mRNA.
DR EMBL; AB094629; BAC55012.1; -; Genomic_DNA.
DR EMBL; AK028955; BAC26211.1; -; mRNA.
DR EMBL; AK045539; BAC32410.1; -; mRNA.
DR EMBL; BC024599; AAH24599.1; -; mRNA.
DR CCDS; CCDS15904.1; -.
DR RefSeq; NP_660126.1; NM_145144.1.
DR AlphaFoldDB; Q9EQX4; -.
DR SMR; Q9EQX4; -.
DR BioGRID; 224458; 7.
DR IntAct; Q9EQX4; 6.
DR STRING; 10090.ENSMUSP00000001920; -.
DR iPTMnet; Q9EQX4; -.
DR PhosphoSitePlus; Q9EQX4; -.
DR EPD; Q9EQX4; -.
DR jPOST; Q9EQX4; -.
DR MaxQB; Q9EQX4; -.
DR PaxDb; Q9EQX4; -.
DR PeptideAtlas; Q9EQX4; -.
DR PRIDE; Q9EQX4; -.
DR ProteomicsDB; 296342; -.
DR Antibodypedia; 31561; 22 antibodies from 9 providers.
DR DNASU; 108897; -.
DR Ensembl; ENSMUST00000001920; ENSMUSP00000001920; ENSMUSG00000001864.
DR GeneID; 108897; -.
DR KEGG; mmu:108897; -.
DR UCSC; uc008jeg.1; mouse.
DR CTD; 83543; -.
DR MGI; MGI:1919598; Aif1l.
DR VEuPathDB; HostDB:ENSMUSG00000001864; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013846; -.
DR HOGENOM; CLU_134149_0_0_1; -.
DR InParanoid; Q9EQX4; -.
DR OMA; KILMFEE; -.
DR OrthoDB; 1557466at2759; -.
DR PhylomeDB; Q9EQX4; -.
DR TreeFam; TF320736; -.
DR BioGRID-ORCS; 108897; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9EQX4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQX4; protein.
DR Bgee; ENSMUSG00000001864; Expressed in decidua and 250 other tissues.
DR ExpressionAtlas; Q9EQX4; baseline and differential.
DR Genevisible; Q9EQX4; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IBA:GO_Central.
DR InterPro; IPR028453; Aif1-like.
DR InterPro; IPR042433; AIF1/AIF1L.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10356; PTHR10356; 1.
DR PANTHER; PTHR10356:SF5; PTHR10356:SF5; 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; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI0"
FT CHAIN 2..150
FT /note="Allograft inflammatory factor 1-like"
FT /id="PRO_0000073871"
FT DOMAIN 47..82
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 83..117
FT /note="EF-hand 2; degenerate"
FT /evidence="ECO:0000305"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI0"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI0"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI0"
FT CONFLICT 111
FT /note="M -> K (in Ref. 3; BAC26211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17024 MW; C707C3059FCA7A00 CRC64;
MSVALSNRFQ GGKAFGLLKA RQEKRLEEIN REFLCDQKYS DEENLPEKLA AFKEKYMEFD
LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL
KLVMMFEGKA NESSPKPAGP PPERDIASLP
