ABCF3_HUMAN
ID ABCF3_HUMAN Reviewed; 709 AA.
AC Q9NUQ8; A8K241; Q86UA2; Q8NAN1; Q96GS8; Q9H7A8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=ATP-binding cassette sub-family F member 3;
GN Name=ABCF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-503.
RC TISSUE=Placenta, Subthalamic nucleus, and Vascular smooth muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Muscle, and Skin;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-155; SER-157; SER-161
RP AND SER-283, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Displays an antiviral effect against flaviviruses such as
CC west Nile virus (WNV) in the presence of OAS1B. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NUQ8; O94868: FCHSD2; NbExp=4; IntAct=EBI-717672, EBI-1215612;
CC Q9NUQ8; P14373: TRIM27; NbExp=7; IntAct=EBI-717672, EBI-719493;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUQ8-2; Sequence=VSP_020142;
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=BAB14989.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK002060; BAA92063.1; -; mRNA.
DR EMBL; AK024758; BAB14989.1; ALT_INIT; mRNA.
DR EMBL; AK092415; BAC03881.1; -; mRNA.
DR EMBL; AK290106; BAF82795.1; -; mRNA.
DR EMBL; BC009253; AAH09253.1; -; mRNA.
DR EMBL; BC051754; AAH51754.1; -; mRNA.
DR EMBL; BC051884; AAH51884.2; -; mRNA.
DR CCDS; CCDS3254.1; -. [Q9NUQ8-1]
DR CCDS; CCDS87173.1; -. [Q9NUQ8-2]
DR RefSeq; NP_060828.2; NM_018358.2. [Q9NUQ8-1]
DR AlphaFoldDB; Q9NUQ8; -.
DR SMR; Q9NUQ8; -.
DR BioGRID; 120605; 132.
DR IntAct; Q9NUQ8; 24.
DR MINT; Q9NUQ8; -.
DR STRING; 9606.ENSP00000411471; -.
DR TCDB; 3.A.1.121.9; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q9NUQ8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUQ8; -.
DR PhosphoSitePlus; Q9NUQ8; -.
DR BioMuta; ABCF3; -.
DR DMDM; 114149223; -.
DR EPD; Q9NUQ8; -.
DR jPOST; Q9NUQ8; -.
DR MassIVE; Q9NUQ8; -.
DR MaxQB; Q9NUQ8; -.
DR PaxDb; Q9NUQ8; -.
DR PeptideAtlas; Q9NUQ8; -.
DR PRIDE; Q9NUQ8; -.
DR ProteomicsDB; 82712; -. [Q9NUQ8-1]
DR ProteomicsDB; 82713; -. [Q9NUQ8-2]
DR Antibodypedia; 33796; 204 antibodies from 29 providers.
DR DNASU; 55324; -.
DR Ensembl; ENST00000292808.5; ENSP00000292808.4; ENSG00000161204.12. [Q9NUQ8-2]
DR Ensembl; ENST00000429586.7; ENSP00000411471.2; ENSG00000161204.12. [Q9NUQ8-1]
DR GeneID; 55324; -.
DR KEGG; hsa:55324; -.
DR MANE-Select; ENST00000429586.7; ENSP00000411471.2; NM_018358.3; NP_060828.2.
DR UCSC; uc003fmz.3; human. [Q9NUQ8-1]
DR CTD; 55324; -.
DR DisGeNET; 55324; -.
DR GeneCards; ABCF3; -.
DR HGNC; HGNC:72; ABCF3.
DR HPA; ENSG00000161204; Low tissue specificity.
DR MIM; 618967; gene.
DR neXtProt; NX_Q9NUQ8; -.
DR OpenTargets; ENSG00000161204; -.
DR PharmGKB; PA24407; -.
DR VEuPathDB; HostDB:ENSG00000161204; -.
DR eggNOG; KOG0062; Eukaryota.
DR GeneTree; ENSGT00940000155604; -.
DR HOGENOM; CLU_000604_36_6_1; -.
DR InParanoid; Q9NUQ8; -.
DR OMA; CTHIADI; -.
DR PhylomeDB; Q9NUQ8; -.
DR TreeFam; TF105209; -.
DR PathwayCommons; Q9NUQ8; -.
DR SignaLink; Q9NUQ8; -.
DR BioGRID-ORCS; 55324; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; ABCF3; human.
DR GenomeRNAi; 55324; -.
DR Pharos; Q9NUQ8; Tdark.
DR PRO; PR:Q9NUQ8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NUQ8; protein.
DR Bgee; ENSG00000161204; Expressed in right adrenal gland cortex and 168 other tissues.
DR ExpressionAtlas; Q9NUQ8; baseline and differential.
DR Genevisible; Q9NUQ8; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
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; Alternative splicing; Antiviral defense; ATP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..709
FT /note="ATP-binding cassette sub-family F member 3"
FT /id="PRO_0000248042"
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:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 69..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020142"
FT VARIANT 503
FT /note="P -> L (in dbSNP:rs11706273)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_027247"
FT VARIANT 510
FT /note="R -> H (in dbSNP:rs9811715)"
FT /id="VAR_027248"
FT CONFLICT 231
FT /note="P -> S (in Ref. 1; BAC03881)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="A -> G (in Ref. 1; BAB14989)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="K -> R (in Ref. 1; BAA92063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 79745 MW; E7E0FDB6426F3F60 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
QEVAGDDTPA LQSVLESDSV REDLLRRERE LTAQIAAGRA EGSEAAELAE IYAKLEEIEA
DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV
RAILWLENYL QTWPSTILVV SHDRNFLNAI ATDIIHLHSQ RLDGYRGDFE TFIKSKQERL
LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVMKF
PDGFEKFSPP ILQLDEVDFY YDPKHVIFSR LSVSADLESR ICVVGENGAG KSTMLKLLLG
DLAPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGRPEEEY RHQLGRYGIS
GELAMRPLAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG RALNNFRGGV
ILVSHDERFI RLVCRELWVC EGGGVTRVEG GFDQYRALLQ EQFRREGFL
