ID   ABCF2_HUMAN             Reviewed;         623 AA.
AC   Q9UG63; O60864; Q75MJ0; Q75MJ1; Q96TE8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=ATP-binding cassette sub-family F member 2;
DE   AltName: Full=Iron-inhibited ABC transporter 2;
GN   Name=ABCF2; ORFNames=HUSSY-18;
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 [MRNA] (ISOFORM 1).
RX   PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
RA   Ye Z., Connor J.R.;
RT   "cDNA cloning by amplification of circularized first strand cDNAs reveals
RT   non-IRE-regulated iron-responsive mRNAs.";
RL   Biochem. Biophys. Res. Commun. 275:223-227(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 74-623.
RC   TISSUE=Lung;
RX   PubMed=11124703;
RX   DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA   Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA   Zimbello R., Lanfranchi G., Valle G.;
RT   "Characterization of 16 novel human genes showing high similarity to yeast
RT   sequences.";
RL   Yeast 18:69-80(2001).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-218 AND SER-512, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UG63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UG63-2; Sequence=VSP_054715;
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   -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC       URL="http://abcm2.hegelab.org/search";
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DR   EMBL; AF261091; AAG13902.1; -; mRNA.
DR   EMBL; AF261092; AAG13903.1; -; mRNA.
DR   EMBL; BT007451; AAP36119.1; -; mRNA.
DR   EMBL; AL050291; CAB43392.1; -; mRNA.
DR   EMBL; AC021097; AAS00378.1; -; Genomic_DNA.
DR   EMBL; AC021097; AAS00379.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54014.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54016.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54017.1; -; Genomic_DNA.
DR   EMBL; BC001661; AAH01661.1; -; mRNA.
DR   EMBL; AJ005016; CAA06290.1; -; mRNA.
DR   CCDS; CCDS5923.1; -. [Q9UG63-1]
DR   PIR; T08810; T08810.
DR   RefSeq; NP_005683.2; NM_005692.4. [Q9UG63-2]
DR   RefSeq; NP_009120.1; NM_007189.2. [Q9UG63-1]
DR   RefSeq; XP_016867128.1; XM_017011639.1.
DR   RefSeq; XP_016867129.1; XM_017011640.1.
DR   AlphaFoldDB; Q9UG63; -.
DR   SMR; Q9UG63; -.
DR   BioGRID; 115372; 163.
DR   CORUM; Q9UG63; -.
DR   IntAct; Q9UG63; 47.
DR   MINT; Q9UG63; -.
DR   STRING; 9606.ENSP00000222388; -.
DR   TCDB; 3.A.1.121.11; the atp-binding cassette (abc) superfamily.
DR   GlyGen; Q9UG63; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UG63; -.
DR   MetOSite; Q9UG63; -.
DR   PhosphoSitePlus; Q9UG63; -.
DR   SwissPalm; Q9UG63; -.
DR   BioMuta; ABCF2; -.
DR   DMDM; 12643306; -.
DR   EPD; Q9UG63; -.
DR   jPOST; Q9UG63; -.
DR   MassIVE; Q9UG63; -.
DR   MaxQB; Q9UG63; -.
DR   PaxDb; 9606-ENSP00000222388; -.
DR   PeptideAtlas; Q9UG63; -.
DR   ProteomicsDB; 84202; -. [Q9UG63-1]
DR   Pumba; Q9UG63; -.
DR   Antibodypedia; 18732; 412 antibodies from 30 providers.
DR   DNASU; 10061; -.
DR   Ensembl; ENST00000287844.7; ENSP00000287844.2; ENSG00000033050.9. [Q9UG63-1]
DR   GeneID; 10061; -.
DR   GeneID; 114483834; -.
DR   KEGG; hsa:10061; -.
DR   KEGG; hsa:114483834; -.
DR   MANE-Select; ENST00000287844.7; ENSP00000287844.2; NM_007189.3; NP_009120.1.
DR   UCSC; uc003wjo.3; human. [Q9UG63-1]
DR   AGR; HGNC:54751; -.
DR   AGR; HGNC:71; -.
DR   CTD; 10061; -.
DR   CTD; 114483834; -.
DR   DisGeNET; 10061; -.
DR   DisGeNET; 114483834; -.
DR   GeneCards; ABCF2; -.
DR   HGNC; HGNC:71; ABCF2.
DR   HPA; ENSG00000033050; Low tissue specificity.
DR   MIM; 612510; gene.
DR   neXtProt; NX_Q9UG63; -.
DR   OpenTargets; ENSG00000033050; -.
DR   PharmGKB; PA24406; -.
DR   VEuPathDB; HostDB:ENSG00000033050; -.
DR   VEuPathDB; HostDB:ENSG00000285292; -.
DR   eggNOG; KOG0927; Eukaryota.
DR   GeneTree; ENSGT00630000089910; -.
DR   HOGENOM; CLU_000604_36_6_1; -.
DR   InParanoid; Q9UG63; -.
DR   OMA; QYEGTML; -.
DR   OrthoDB; 25181at2759; -.
DR   PhylomeDB; Q9UG63; -.
DR   TreeFam; TF105208; -.
DR   PathwayCommons; Q9UG63; -.
DR   Reactome; R-HSA-9818032; NFE2L2 regulating MDR associated enzymes.
DR   SignaLink; Q9UG63; -.
DR   BioGRID-ORCS; 10061; 30 hits in 1161 CRISPR screens.
DR   ChiTaRS; ABCF2; human.
DR   GeneWiki; ABCF2; -.
DR   GenomeRNAi; 10061; -.
DR   Pharos; Q9UG63; Tbio.
DR   PRO; PR:Q9UG63; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9UG63; Protein.
DR   Bgee; ENSG00000033050; Expressed in sural nerve and 178 other cell types or tissues.
DR   ExpressionAtlas; Q9UG63; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR19211:SF15; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 2; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; Q9UG63; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..623
FT                   /note="ATP-binding cassette sub-family F member 2"
FT                   /id="PRO_0000093323"
FT   DOMAIN          86..325
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          396..613
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         430..437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         218
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         304
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         623
FT                   /note="V -> VCTLTLASLPRP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_054715"
FT   CONFLICT        39
FT                   /note="V -> A (in Ref. 1; AAG13902/AAG13903)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="T -> A (in Ref. 7; CAA06290)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   623 AA;  71290 MW;  702A968BCF8061AE CRC64;
     MPSDLAKKKA AKKKEAAKAR QRPRKGHEEN GDVVTEPQVA EKNEANGRET TEVDLLTKEL
     EDFEMKKAAA RAVTGVLASH PNSTDVHIIN LSLTFHGQEL LSDTKLELNS GRRYGLIGLN
     GIGKSMLLSA IGKREVPIPE HIDIYHLTRE MPPSDKTPLH CVMEVDTERA MLEKEAERLA
     HEDAECEKLM ELYERLEELD ADKAEMRASR ILHGLGFTPA MQRKKLKDFS GGWRMRVALA
     RALFIRPFML LLDEPTNHLD LDACVWLEEE LKTFKRILVL VSHSQDFLNG VCTNIIHMHN
     KKLKYYTGNY DQYVKTRLEL EENQMKRFHW EQDQIAHMKN YIARFGHGSA KLARQAQSKE
     KTLQKMMASG LTERVVSDKT LSFYFPPCGK IPPPVIMVQN VSFKYTKDGP CIYNNLEFGI
     DLDTRVALVG PNGAGKSTLL KLLTGELLPT DGMIRKHSHV KIGRYHQHLQ EQLDLDLSPL
     EYMMKCYPEI KEKEEMRKII GRYGLTGKQQ VSPIRNLSDG QKCRVCLAWL AWQNPHMLFL
     DEPTNHLDIE TIDALADAIN EFEGGMMLVS HDFRLIQQVA QEIWVCEKQT ITKWPGDILA
     YKEHLKSKLV DEEPQLTKRT HNV
//