ID   ABCF3_RAT               Reviewed;         709 AA.
AC   Q66H39;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=ATP-binding cassette sub-family F member 3;
GN   Name=Abcf3;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Displays an antiviral effect against flaviviruses such as
CC       west Nile virus (WNV) in the presence of OAS1B. {ECO:0000250}.
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}.
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DR   EMBL; BC082042; AAH82042.1; -; mRNA.
DR   RefSeq; NP_001011896.1; NM_001011896.1.
DR   AlphaFoldDB; Q66H39; -.
DR   SMR; Q66H39; -.
DR   STRING; 10116.ENSRNOP00000002327; -.
DR   jPOST; Q66H39; -.
DR   PaxDb; Q66H39; -.
DR   PRIDE; Q66H39; -.
DR   GeneID; 287982; -.
DR   KEGG; rno:287982; -.
DR   CTD; 55324; -.
DR   RGD; 1310468; Abcf3.
DR   VEuPathDB; HostDB:ENSRNOG00000001710; -.
DR   eggNOG; KOG0062; Eukaryota.
DR   HOGENOM; CLU_000604_36_6_1; -.
DR   InParanoid; Q66H39; -.
DR   OMA; CTHIADI; -.
DR   OrthoDB; 580544at2759; -.
DR   PhylomeDB; Q66H39; -.
DR   TreeFam; TF105209; -.
DR   PRO; PR:Q66H39; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001710; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q66H39; RN.
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   2: Evidence at transcript 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_0000248045"
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         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"
SQ   SEQUENCE   709 AA;  79856 MW;  57014DCB3311D219 CRC64;
     MATCADILRS EFPEIDGQVF DYVTGVLHSG SADFESVDDL VEAVGELLQE VSGDSKDDAG
     IRAVCQRMYN TLRLAEPQNQ GNNQVLLDAP IQLSKIMENY DCDTKLPGLL KREQSSTVNA
     KKLEKAEARL KAKQEKRSEK ETLKTSSPLV LEEASASQAG SRKESRLESS GKNKSYDVRI
     ENFDVSFGDR VLLAGADVNL AWGRRYGLVG RNGLGKTTLL KMLATRSLRV PAHISLLHVE
     QEVAGDDTPA LQSVLESDTI REDLLRQERG LSLKIAAGRA EGSEAALLAE VYTKLEEIEA
     DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV
     RAILWLENYL QTWPSTILVV SHDRNFLNAI ATDIIHLHSQ RLDGYRGDFE TFIKSKQERL
     LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVLKF
     PDGFEKFSPP ILQLDEVDFY YDPKHIIFSR LSVSADLESR ICVVGENGAG KSTMLKLLMG
     DLAPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGRPEEEY RHQLGRYGIS
     GELAMRPVAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG HALNNFRGGV
     VLVSHDERFI RLVCKELWVC EKGSVTRVEG GFDQYRALLQ EQFRREGFL