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ABCC9_DICDI
ID   ABCC9_DICDI             Reviewed;        1345 AA.
AC   Q54NL1; Q8T6H0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ABC transporter C family member 9;
DE   AltName: Full=ABC transporter ABCC.9;
GN   Name=abcC9; ORFNames=DDB_G0285165;
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: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; AF474341; AAL85712.1; -; Genomic_DNA.
DR   EMBL; AAFI02000075; EAL64839.1; -; Genomic_DNA.
DR   RefSeq; XP_638351.1; XM_633259.1.
DR   AlphaFoldDB; Q54NL1; -.
DR   SMR; Q54NL1; -.
DR   STRING; 44689.DDB0216237; -.
DR   PaxDb; Q54NL1; -.
DR   PRIDE; Q54NL1; -.
DR   EnsemblProtists; EAL64839; EAL64839; DDB_G0285165.
DR   GeneID; 8624976; -.
DR   KEGG; ddi:DDB_G0285165; -.
DR   dictyBase; DDB_G0285165; abcC9.
DR   eggNOG; KOG0054; Eukaryota.
DR   HOGENOM; CLU_000604_27_3_1; -.
DR   InParanoid; Q54NL1; -.
DR   OMA; WISIRLE; -.
DR   PhylomeDB; Q54NL1; -.
DR   Reactome; R-DDI-159418; Recycling of bile acids and salts.
DR   Reactome; R-DDI-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DDI-9749641; Aspirin ADME.
DR   Reactome; R-DDI-9753281; Paracetamol ADME.
DR   PRO; PR:Q54NL1; -.
DR   Proteomes; UP000002195; Chromosome 4.
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:0031153; P:slug development involved in sorocarp development; HMP:dictyBase.
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; IPR017871; ABC_transporter-like_CS.
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; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Membrane; Nucleotide-binding; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1345
FT                   /note="ABC transporter C family member 9"
FT                   /id="PRO_0000363854"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        776..796
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        817..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        906..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1008..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          135..419
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          481..703
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          775..1060
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1103..1338
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          460..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..55
FT                   /evidence="ECO:0000255"
FT   COILED          709..739
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        463..484
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1137..1144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        273
FT                   /note="S -> P (in Ref. 1; AAL85712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1345 AA;  154402 MW;  54E539F9382C372E CRC64;
     MIRNKIKNKK SKSDYYSEIS LEEEEDKEEE IKDKKVLSKE EIKENENKNE KIKQTQCPED
     NASLFSKITF GWITKLIVKA YIKKSLDIKD IFDVPNYLKS NYTSKFLTTE KQTFKRNTKY
     SLILNIYINF ILLKNKKLIL IQFLRVLFTL LSPLILKLFI EFTQRIDSEK SIIEGIIYCG
     LLFFSSFCSS LVDEYLVWFG MITSSQVKSC LTCLIFEKSL KLSNSAKVKY NAAKITNLIS
     IDVDNFSNFF WSNSVEIFFQ PFQLIFLLIL LISEVGWSGF VGTAVILISF PINSYFGKKT
     SDYYEKLLKY TDKRVSTTSE FINGIRFIKM YAWESLFLKK IEKQRKQELK ILLERGLFWL
     GQIIIINTNS TFVFVATMVT YSLSGNKMKL ETAFTAMNIL DSIRILLIVM PYCYYSIMEL
     IPSNKRIEKF LSTLEIQQNL QTTKNSNTIS INNGTFKWKD ENFEETDDDD DHDDDDDEGE
     KEIEGKEEKE EINNFIFENI NFKAPIGKLT MICSPVGSGK TSLINALIGE IEKVNGEING
     VPENISFTSQ QPFLLSTSLR ENILFGKELD IEYYKQVLDA CCLVSDLTQL SALDLTEIGE
     GGINLSGGQK QRVSLARALY SNSDFILMDE PLSAVDPEVA NHLFEKCIQG MMKNKTRILV
     THQIQFIPYA DHIVIIKDGK IIQGTYKELK DENGIDFESI IKTKNSNLNL NKTIKDEEEK
     EDKEGEEKEE DKKEMILKLI KINYSDELKE KAKLLVEEDR NEGEVSFKTY KEYFYYGSSN
     LFLFITLLVF LIGLIVNRLS DFWLTIWTEQ SFKEKSQTFY IICFVSIFIV SLILIFIRYS
     LVAKIGFKSS KKLHDLLINS ISKSPIQFFD SNPSGRILNR FSNDISDIDT SMIDMFSDTL
     EYIFAIVVGI FSIIYINPMT IVPFLILSMF YYQIFNIYRV SVRELNRCKS ISQSPIISFL
     SECCNGLSTI RAFKQQSRFI GIMNDNIDKN LKCEFASFAV EMWISIRLEL LSSIIVFIVS
     LFSLFNGYSN SALSILSVST ARSITSYLKS ACRQMVDLER KMNSFERVNN YIKLPSEGSG
     SGVKSMEFIS EKDLLNWPEK GNIQFNNVQV NYNSNSVPSL KDITFSVESN EKIGIVGRTG
     AGKSTIANCL FRLVECSKGS ILIDGIDIKT IDLNKLRGSL GIVPQEPWLF SGTIRSNIDP
     LNQYDDEMIW NYLEMVKLKK LIIEMPLKLN SKIHENGNTT LSYGQKQLLC LCRCLIKNPK
     LIIMDEATSS VDFQTAETIK SVINENLVNN TILTIAHRLD IIIDSDKIAV IDNSKLIEFE
     NPKNLINSNS KFRKIVNFQT KIQTN
 
 
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