ID   ABCGG_DICDI             Reviewed;        1528 AA.
AC   Q54HM0; Q8T677;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=ABC transporter G family member 16;
DE   AltName: Full=ABC transporter ABCG.16;
GN   Name=abcG16; ORFNames=DDB_G0289331;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC   STRAIN=AX4;
RX   PubMed=12456012; DOI=10.1128/ec.1.4.643-652.2002;
RA   Anjard C., Loomis W.F.;
RT   "Evolutionary analyses of ABC transporters of Dictyostelium discoideum.";
RL   Eukaryot. Cell 1:643-652(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR   EMBL; AF482394; AAL91501.1; -; Genomic_DNA.
DR   EMBL; AAFI02000139; EAL62752.1; -; Genomic_DNA.
DR   RefSeq; XP_636281.1; XM_631189.1.
DR   AlphaFoldDB; Q54HM0; -.
DR   SMR; Q54HM0; -.
DR   PaxDb; Q54HM0; -.
DR   PRIDE; Q54HM0; -.
DR   EnsemblProtists; EAL62752; EAL62752; DDB_G0289331.
DR   GeneID; 8627099; -.
DR   KEGG; ddi:DDB_G0289331; -.
DR   dictyBase; DDB_G0289331; abcG16.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; Q54HM0; -.
DR   OMA; YASTFTH; -.
DR   PhylomeDB; Q54HM0; -.
DR   PRO; PR:Q54HM0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IBA:GO_Central.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IBA:GO_Central.
DR   CDD; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR034001; ABCG_PDR_1.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1528
FT                   /note="ABC transporter G family member 16"
FT                   /id="PRO_0000330365"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        545..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        655..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        763..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1225..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1255..1272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1285..1305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1334..1354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1361..1381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1391..1411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1504..1524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          167..412
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          509..738
FT                   /note="ABC transmembrane type-2 1"
FT   DOMAIN          837..1085
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          1249..1479
FT                   /note="ABC transmembrane type-2 2"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1159..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         878..885
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        378
FT                   /note="L -> I (in Ref. 1; AAL91501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1528 AA;  172667 MW;  A9FB1710B0281B33 CRC64;
     MKLTNSISPT NLDGEINKNS QPSNDNQQQQ QPKINKIINK FSESINSVSK TIGKGIGDLT
     SSNALDEHIK NHNSNFIDPF YNEEAVVVVD DENIRSLIGD NCSSIGNIGV NGIEAFYGEH
     NNKKSELIKQ FLKINSTNNK SNQTIVVDHM DYSVMERQSS SSSSSSSRST GVSKLIPFLK
     RKEKIEILKD LSFYLKPGMM VLLLSEAGSG VSTLFKCLTN RIPKRGSING DILFDNEPID
     GESHHSQYLF VQQSDHHIST LTVKETLEFS IECQSNLSRE AKKQLSSNIL SILGISHVAD
     TYIGNQSIRG ISGGQKKRMT VAVELVKGAK AIMIDQATNG LDSTSAFELL NSIQMISKVS
     NVPALVSLLQ PSPEIFSLFS HILMMKDGEI TFFGEKHQIF DHFSDYGLEC KDKQNPAEFL
     SSIYHQAQLD PDCQLKSSSD FIVAYKQSQY YKDCLIKISQ ERLSNHKFSG DKSIKIIENE
     KEQQQQEIYQ LSLIKQIQLN LKRAFLTTIR DRASILSRVI KSSLLGLLIG TLFFQLDSSQ
     KSANLLPSLS FFLLTFVVFG SLAGVGQVFS ERPVFYDQKI GKYYKSIAYF FAGLVSDLIW
     NFIDVIIFCS ISYWLIGLNH SADRFFFFLL AIYLLDCLVN RVSKMVSIYS PNAAIASTIA
     PLYFSLFLLM AGYLIHRNSI PIYWRWMHYI SPFKWVFEAI LSNQLHGQTF TCKSDELLPP
     IGYPLLNVSF PDGYSGSQVC PIIDGIEILK SKDINSDYSY KYYSVWIILS MYLLFSILSI
     IGLSNITFDN IISNKEKNNG NGNNNYNGKE SINEESIKLS IKQHQQKQFE SNEKCYLTFK
     NLTYKVLIKK KNHQKVSRTL LHDINGYVKP GSMVALIGSS GAGKSTLLDI LANRKDQGII
     SGEILLNGKA RDKCFNRYVA YVEQEDTLPD FQTVREAITF SALLRLPNDT MTHQDKLDTV
     DYILDVLELN SIANTLIGKV DHGITQEQRK RVNIAIEMAS LPDILFLDEP TTGLTSVAAE
     LIMQLIKRVA LDGRSVICTI HQPSETIFKK FDSILLLTQG GFVAYFGELG PNCRTVLNYC
     SDLGFNCPQG KNPADFLLDF SASFNSASRL ASNDKMIPSI RSRIKNVGNY CFDGSSNLNN
     KNEIKQQQTT TQNVNLGNED KQQQQQEEAN DDNNIQEATS SNSNNNNNND IIDNYQFSNL
     NRDTIEIIDS GLPIGFISKT FKEKNATSFL FQFFMLLFRF FVCAIRRRNL IMTRIIRSIL
     LSVVTGTLYL QLKNDQDGVM DRISFIFFTS TFASISCLSN IPTVFEDRFL FYHELNSNTY
     RHLSYILAMI LADLPFTIMY SLLFSAPIYW IVGLQNDVDK FLFFIFVYYL YLQVLVSFSQ
     LLGMVSPTLA TANEITGISF SVFSLFAGFI IKKDDIPSYY KWLNYVSITR YLVEPLTVNE
     MTGSVSFHCE PHQLIPVPIH YTPTNATASE PTKLVFKSFC PITQGNQVLY QFDINDTDKF
     EDTFVLIGLF IGFLLLILIF SKILKFKK