ABCA2_DICDI
ID ABCA2_DICDI Reviewed; 1621 AA.
AC Q8T6J5; Q55GB0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ABC transporter A family member 2;
DE AltName: Full=ABC transporter ABCA.2;
GN Name=abcA2; ORFNames=DDB_G0267438;
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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AF465304; AAL85295.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73171.1; -; Genomic_DNA.
DR RefSeq; XP_647274.1; XM_642182.1.
DR AlphaFoldDB; Q8T6J5; -.
DR SMR; Q8T6J5; -.
DR STRING; 44689.DDB0191223; -.
DR TCDB; 3.A.1.211.19; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8T6J5; -.
DR EnsemblProtists; EAL73171; EAL73171; DDB_G0267438.
DR GeneID; 8616081; -.
DR KEGG; ddi:DDB_G0267438; -.
DR dictyBase; DDB_G0267438; abcA2.
DR eggNOG; KOG0059; Eukaryota.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8T6J5; -.
DR OMA; DPVYSYD; -.
DR PhylomeDB; Q8T6J5; -.
DR Reactome; R-DDI-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-DDI-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8963896; HDL assembly.
DR PRO; PR:Q8T6J5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0031288; P:sorocarp morphogenesis; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
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..1621
FT /note="ABC transporter A family member 2"
FT /id="PRO_0000363834"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1227..1247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 484..717
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1293..1528
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 520..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1331..1338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1621 AA; 181214 MW; E1CA0A8FA25358A2 CRC64;
MGEFKSQLRT LLKKNLLLKG KSKCAICCEI LFPIIVILVI FAILVLVMAF KANYDPYNAS
NFVNRFENTV LLYGNADGAL NVEQLGVMNI LKNEVATAKN LNSTQIDQLF IEINDQTAME
AFFQNKSDFV FSAVWFNNSA LSSGTNPFQY NIRVDSDDVM DTEELIKEDD TSDSEVYVKK
RFVATQVAMD QAIFSYFGLN KTLNVKGQRY PDPWTELWQK WIQGRDGIFK DAGSVFITAA
LMIFGFRLIT DLVIEKETKI RESMKMMGLN DLAYFISWMI TSLVTALPVN LIISIILKGS
SVIHHTNWGV VIFTLILYLL TLLLLAFILS MFFDKSKFCG LLSFVIIIAI NIGGIFVAKY
DFAPGAKLFL CLISPIAIAC SIFAMSARDL EEINTYNWDM MVTENQVIGM LVLDIFFYIF
LVWYLDNVVT TEFGTKQKWY FLFTKKYWFP KKCNENGDEQ DIESTYQNED VEMTPVGVGQ
KVTISIRNLR KEYNTGDGLR VAVNDLYLDM YENQIHALLG PNGSGKSTTI GMMTGLTPPT
NGNAFVHGYG ILNQMSSVRK HLGVCPQTDI IWQQLTVLDH LKIYASLKGV SPSEIQREAE
KMAVEVDLGE KIHSQAGSLS GGQKRKLCLG IAFIGRSDVI FLDEVSSGMD PLSRRVVWDF
LLKYKKGRTI ILTTHYLEEA DYLGDRIAII SHGKLRCDGS SLYLKNKFGC GYLLTCSKIL
SSMNNFNAQQ VTEFIHNYIP EATILSNAGT ELSYRLPTAS LPHFAQFFRE FDDRLQSFGL
LTYGISVTTL EEVFLSLGRE AALEKGGFNI DQNENQDLEQ LRKSIAISST GVKAGQQFKG
LLIKRIKTSI KDAKSFFLTL VIPLVFIIGS IIMYKAMDKP QIFYNNATVP LTMNLGIYSG
LENNFVPMQS SNELNWENSL NSSPYFNKFR FIPQTENFED YLIEGKTNGS FAYKSSAGAI
NFTLPIDVSS TTIDYTAFYN KDYIHSLPVH INLVNDAVLR KHNNIGIQVT NMPFKHVLSN
FDLASEGMNI SSIVYFIIIM MAGYALMAGS FAGNVAQERT NRVKRLLYIS GCKKYVYWLS
NLVWDYFFSF ILILLTTCIL AGIRENYKSQ FGLMFLCLIL FCVSVVPLSY LLSYRFASFG
KATGAITAIH FAIGIIFVII SLNLRIQVLI DQDVDFQKAA DAVDIVFCIL SPLFAYSRIL
FLVSEFPGSV RVGTLKVDNY WSMDYGGSPM IILAAHCIVW VSWIMILDYT PELIGKIRNP
KNIEAPPPPD DEDSDVTAER TRLLSVGPND EPLQFRNLHK LFPAVGKAAP KAAVYNSTLS
IPKGQTFGLL GLNGAGKTTT IAMLCGDIVP SSGEVTINGH DLITDRGQAL RSNGLCPQFD
ALITLLSARE QLTLYCAIKG VPEDKVKEVV EAFIKMMDLG AIANSNTGGY SGGNKRKTSL
SIAMLGNPSI VSLDEPSTGC DAVVRKYIWN VVSELAKDKV IILTSHSMAE VEALCYRMTI
MRDGKMKCLG SIQHIKSKFG AGYTFDVKFK KEYLDSGIQT VLKAIPNSIV LDEHDVMASF
EIPNPPDNPV KISTLFESLS HLTILDDYNV SQTSLESVFL KLTGASYEDR LNLNNQKHTS
D