ID   ABCF3_PONAB             Reviewed;         709 AA.
AC   Q5R9Z5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-binding cassette sub-family F member 3;
GN   Name=ABCF3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Displays an antiviral effect against flaviviruses in the
CC       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; CR859235; CAH91415.1; -; mRNA.
DR   RefSeq; NP_001125831.1; NM_001132359.1.
DR   AlphaFoldDB; Q5R9Z5; -.
DR   SMR; Q5R9Z5; -.
DR   STRING; 9601.ENSPPYP00000016045; -.
DR   GeneID; 100172759; -.
DR   KEGG; pon:100172759; -.
DR   CTD; 55324; -.
DR   eggNOG; KOG0062; Eukaryota.
DR   InParanoid; Q5R9Z5; -.
DR   OrthoDB; 580544at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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_0000248044"
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"
SQ   SEQUENCE   709 AA;  79796 MW;  F6A5A0D0BC9DFD29 CRC64;
     MATCAEILRS EFPEIDGQVF DYVTGVLHSG SADFESVDDL VEAVGELLQE VSGDSKDDAG
     IRAVCQRMYN TLRLAEPQSQ GNSQVLLDAP IQLSKITENY DCGTKLPGLL KREQSSTVNA
     KKLEKAEARL KAKQEKRSEK DTLKTSNPLV LEEASASQAG SRKESRLESS GKNKSYDVRI
     ENFDVSFGDR VLLAGADVNL AWGRRYGLVG RNGLGKTTLL KMLATRSLRV PAHISLLHVE
     QEVAEDDTPA LQSVLESDSV REDLLRRERE LSAHIAAGRV EGSEAAELAE IYAKLEEIEA
     DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV
     RAILWLENYL QTWPSTILVV SHDRNFLNAI AADIIHLHSQ RLDGYRGDFE TFIKSKQERL
     LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVMKF
     PDGFEKFSPP ILQLDEVDFY YDPKHVIFSR LSVSADLESR ICVVGENGAG KSTMLKLLLG
     DLAPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGRPEEEY RHQLGRYGIS
     GELAMRPVAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG RALNNFRGGV
     ILVSHDERFI RLVCRELWVC EGGGVTRVEG GFDQYRALLQ EQFRREGFL