ABCCF_DICDI
ID ABCCF_DICDI Reviewed; 1436 AA.
AC Q54VC1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ABC transporter C family member 15;
DE AltName: Full=ABC transporter ABCC.15;
GN Name=abcC15; ORFNames=DDB_G0280459;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000036; EAL67208.1; -; Genomic_DNA.
DR RefSeq; XP_641188.1; XM_636096.1.
DR AlphaFoldDB; Q54VC1; -.
DR SMR; Q54VC1; -.
DR STRING; 44689.DDB0216384; -.
DR PaxDb; Q54VC1; -.
DR EnsemblProtists; EAL67208; EAL67208; DDB_G0280459.
DR GeneID; 8622569; -.
DR KEGG; ddi:DDB_G0280459; -.
DR dictyBase; DDB_G0280459; abcC15.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q54VC1; -.
DR OMA; VIHTHYL; -.
DR PhylomeDB; Q54VC1; -.
DR PRO; PR:Q54VC1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
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..1436
FT /note="ABC transporter C family member 15"
FT /id="PRO_0000363859"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1017..1039
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1127..1147
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 128..412
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 543..766
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 865..1155
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1193..1426
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1227..1234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1436 AA; 164683 MW; 9CC96CFA69AD9325 CRC64;
MIKKIKNIIN KIINFFSTIY ILCKIYLYYN IKNRYEAYNI LSVYGDDDFF NKPCPEDSSN
WKDKLTFKWV ERIIFVGFFR APLNLNDISD LPSSLKVENT APLLKDIIFN DSTIPLIKHI
YSKFLPRNYI ATGLFVFVSV FSFITPLILK NFLSYVEKID EQKHIYIGII QCFLLFLSSF
INMASQQYSY WFGFKTSLEV KGALETIIFE KMTKLSNLSK KNYNIGSMLN LMSVDTDFFQ
YFFCHYYIEI FLFPIQILSL LGFLIYVIGI AGFVGFLVML ITIPLSSFLG TQISKNLSTS
MGYADTRISL TGELINGIKF LKQYAWEKMF CERIEEQRKL QLKYLYIRII YWVLVQIVTQ
ASSGLVLVST FTTYTLLGYE VSLEIAFTSI TILQNLRRPI ESLPDCLHKF ISLIASAKRI
ETFLQSSELQ NQPFIHNQSG LNDILIRNIN FNWNEHNLKL KNNKNNQNNN QNKRSIILSS
GEQFEITNDF TFDGIDIQDD NYDYEKEYKI NYNNNEEEEN FMTDCLLKIK PLIKDRRLQQ
QQADYQDLLS INLPPPPSEN VDFKAPKGLL TIISGGVRSG KTSLASGLLG EICKAVDKSS
PDSVNSILST IQQPFLQSTS FRENILFGKP MNMERYIKVI EACCLAPDLL AMGEGKDLTE
IGERGINLSN GLKHRIQLAR ALYADSDCYI LDEILSSVDP EIANYIFQHC IKGMMKGKTV
ILVTHQIQFI SSADHVVVVD NGVLIQGTYL ELLRMGIDFE MILKEKENRI EKQIVQLQED
EDYYEEVEIL DFTMNNNNNN NNNNNNNNSN FNGNNKLKRS SISLPKGISI ESIISKDFDQ
TTIEKAKLFV QEDRNKGDPG WIIYKKYIRM GSSISFFIFT CIIYLTSQII LLLSDYWLQS
WASHDRLNVS EPTDVHYLLI YLAYIGGFVF TLGVRYLLIA KITFGSAETL HRSLLKSIIR
APLTFFEQNP VGRILNRFGK DISDIDILLL DCFSDVLYCG ACLVTSIGII IYISPYIAIP
FVILIAINYI FQLFYNYSVL ELKRIQSISR SPVYSLLSEV YNGLTTIRSF GQQERFFNMM
KDNININLRV FFYNFAVSRW IGIRVEFLSA IVVLMSALFS IFNDNPGLSA LGVTTALGIT
FNLNWFMRQF GELESRINSV ERVQSYISIP KEKETNEDEF IQTGFIWPSR GEIEFKNVEI
RYRPNSIATL RNFSMKINAQ ERIGIIGRSG SGKSTIGMSL FRMIECSSGS ILIDGDDISQ
IDLKRLRSSI GIVPQDPFIF SGSIRLNLDP FDQFTDNEIW EALSKVKLKK MVSTMPMKLE
SLVQGGDGLT IGNKQLLCLC RAILRNSKIV LFDEATNSID FQTTRLIKQT IEENFKDCTI
LTIAHNIDTI LDSDKIAIID EGELIEFDTP LNLIKDSTSR FSKLIKLNNN QKNKLN
