ABCF3_MOUSE
ID ABCF3_MOUSE Reviewed; 709 AA.
AC Q8K268; Q9JL49;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP-binding cassette sub-family F member 3;
GN Name=Abcf3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 589-709.
RC STRAIN=CD-1;
RX PubMed=10708515; DOI=10.1006/geno.1999.6102;
RA Schriml L.M., Dean M.;
RT "Identification of 18 mouse ABC genes and characterization of the ABC
RT superfamily in Mus musculus.";
RL Genomics 64:24-31(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [4]
RP FUNCTION, AND INTERACTION WITH OAS1B.
RX PubMed=22623793; DOI=10.1128/jvi.00333-12;
RA Courtney S.C., Di H., Stockman B.M., Liu H., Scherbik S.V., Brinton M.A.;
RT "Identification of novel host cell binding partners of Oas1b, the protein
RT conferring resistance to flavivirus-induced disease in mice.";
RL J. Virol. 86:7953-7963(2012).
CC -!- FUNCTION: Displays an antiviral effect against flaviviruses such as
CC west Nile virus (WNV) in the presence of OAS1B.
CC {ECO:0000269|PubMed:22623793}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks transmembrane domains and is probably not involved in
CC transport. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31421.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC032923; AAH32923.1; -; mRNA.
DR EMBL; AF213381; AAF31421.1; ALT_FRAME; mRNA.
DR CCDS; CCDS28049.1; -.
DR RefSeq; NP_038880.1; NM_013852.2.
DR AlphaFoldDB; Q8K268; -.
DR SMR; Q8K268; -.
DR BioGRID; 205213; 2.
DR IntAct; Q8K268; 2.
DR MINT; Q8K268; -.
DR STRING; 10090.ENSMUSP00000003319; -.
DR iPTMnet; Q8K268; -.
DR PhosphoSitePlus; Q8K268; -.
DR EPD; Q8K268; -.
DR MaxQB; Q8K268; -.
DR PaxDb; Q8K268; -.
DR PeptideAtlas; Q8K268; -.
DR PRIDE; Q8K268; -.
DR ProteomicsDB; 285817; -.
DR Antibodypedia; 33796; 204 antibodies from 29 providers.
DR DNASU; 27406; -.
DR Ensembl; ENSMUST00000003319; ENSMUSP00000003319; ENSMUSG00000003234.
DR GeneID; 27406; -.
DR KEGG; mmu:27406; -.
DR UCSC; uc007ypz.1; mouse.
DR CTD; 55324; -.
DR MGI; MGI:1351656; Abcf3.
DR VEuPathDB; HostDB:ENSMUSG00000003234; -.
DR eggNOG; KOG0062; Eukaryota.
DR GeneTree; ENSGT00940000155604; -.
DR HOGENOM; CLU_000604_36_6_1; -.
DR InParanoid; Q8K268; -.
DR OMA; CTHIADI; -.
DR OrthoDB; 580544at2759; -.
DR PhylomeDB; Q8K268; -.
DR TreeFam; TF105209; -.
DR BioGRID-ORCS; 27406; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8K268; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K268; protein.
DR Bgee; ENSMUSG00000003234; Expressed in mesenchyme of tongue and 256 other tissues.
DR ExpressionAtlas; Q8K268; baseline and differential.
DR Genevisible; Q8K268; MM.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Antiviral defense; ATP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT CHAIN 2..709
FT /note="ATP-binding cassette sub-family F member 3"
FT /id="PRO_0000248043"
FT DOMAIN 178..424
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 492..707
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 129..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 525..532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ8"
FT CONFLICT 705..706
FT /note="RE -> SG (in Ref. 2; AAF31421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 79865 MW; 03CBD4E7FD967B79 CRC64;
MATCADILRS EFPEIDGQVF DYVTGVLHSG SADFESVDDL VEAVGELLQE VSGDSKDDAG
IRAVCQRMYN TLRLAEPQNQ GNSQVLLDAP IQLSKIMENY DCDTKLPGLL KREQSSTVNA
KKLEKAEARL KAKQEKRSEK ETLKTSNPLV LEEASASQAG SRKESRLESS GKNKSYDVRI
ENFDVSFGDR VLLAGADVNL AWGRRYGLVG RNGLGKTTLL KMLATRSLRV PAHISLLHVE
QEVAGDDTPA LQSVLESDTV REDLLRQERE LSLRIAAGRA EGSEAAQLAE IYGKLEEIEA
DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV
RAILWLENYL QTWPSTILVV SHDRNFLNAI ATDIIHLHSQ RLDGYRGDFE TFIKSKQERL
LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVLKF
PDGFEKFSPP ILQLDEVDFY YDPKHSIFSR LSVSADLESR ICVVGENGAG KSTMLKLLMG
DLSPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGLPEEEY RHQLGRYGIS
GELAMRPVAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG QALNNFRGGV
ILVSHDERFI RLVCKELWVC ENGSVTRVEG GFDQYRALLQ EQFRREGFL
