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ABCG6_DICDI
ID   ABCG6_DICDI             Reviewed;        1534 AA.
AC   Q54TV1; Q8T687;
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 6;
DE   AltName: Full=ABC transporter ABCG.6;
GN   Name=abcG6; ORFNames=DDB_G0281389;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-1534, 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).
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; AAFI02000041; EAL66676.1; -; Genomic_DNA.
DR   EMBL; AF482385; AAL91491.1; -; Genomic_DNA.
DR   RefSeq; XP_640710.1; XM_635618.1.
DR   AlphaFoldDB; Q54TV1; -.
DR   SMR; Q54TV1; -.
DR   STRING; 44689.DDB0215376; -.
DR   PaxDb; Q54TV1; -.
DR   PRIDE; Q54TV1; -.
DR   EnsemblProtists; EAL66676; EAL66676; DDB_G0281389.
DR   GeneID; 8623097; -.
DR   KEGG; ddi:DDB_G0281389; -.
DR   dictyBase; DDB_G0281389; abcG6.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_3_1; -.
DR   InParanoid; Q54TV1; -.
DR   OMA; YAKLILC; -.
DR   PhylomeDB; Q54TV1; -.
DR   PRO; PR:Q54TV1; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IGC:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IBA:GO_Central.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
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; IPR043926; ABCG_dom.
DR   InterPro; IPR034003; ABCG_PDR_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013581; PDR_assoc.
DR   Pfam; PF01061; ABC2_membrane; 2.
DR   Pfam; PF19055; ABC2_membrane_7; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF08370; PDR_assoc; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 3.
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..1534
FT                   /note="ABC transporter G family member 6"
FT                   /id="PRO_0000330364"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        592..612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        652..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        734..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1261..1281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1296..1316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1345..1365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1377..1397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1404..1424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1506..1526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          138..385
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          481..757
FT                   /note="ABC transmembrane type-2 1"
FT   DOMAIN          924..1166
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          1256..1529
FT                   /note="ABC transmembrane type-2 2"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         177..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         960..967
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        18
FT                   /note="I -> L (in Ref. 2; AAL91491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51..52
FT                   /note="NN -> II (in Ref. 2; AAL91491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        824
FT                   /note="T -> P (in Ref. 2; AAL91491)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1534 AA;  173651 MW;  AB3DE3CA581517DE CRC64;
     MAKQDPKDKN SDSPNLSIPI NNNNNENLDN DQELLNNNNN NNNNNNNNNN NNNNNNNNNN
     NNNNLISSSR KHKDEESNYD SDDEKSVYQI AKEHEGEDDG DDEYFPIPLD ELMPNHENDE
     LTKKIKQTRP EDKTGLYVYC RNATYTVKHR ENKKVKIKLI DDISFYLKPK EMTLILGTPG
     CGKSTIFQML AGQLKDKHFK GELLFNGHPI NHKNHHRDIS YVTQDDIHVP TLTVKETFRF
     ALDCLGRKEL TNEEKKETVD NCMNLLGLKE SENTVVGDNF VRGISGGQKK RVTIGVGVIK
     GSNLLLMDEP TSGLDSSTSF EILSDVKKFV TYGYSPALIT LLQPSVQLTS LFDNLMILNK
     GRICYFGPMN KALGYFKKLG FACPSHNNPA EFFQEVVDAP ERYSFIHPPK CKTSKDFVRA
     YRESEFYKDL MEKMDANKDG IVDDNKPKVL VDSTAKELGM YPHGIGYQTK ICMKRGFTMI
     RRNYYNFLTR VAKGIFFGLL LGTLYWRIGH NQSGGMERFG LLFFIMVTII FSSFAAVNSF
     FGERKVFYSQ KALYYYKTGA YFISSIICDI PAGILEVAFF GPIVYWLANL RPVFIRFVYF
     MLLLIMTDNL SLSFAKMCAA ISPTIEIANV IASVILSIWL LFSGFTAPKN DIGGWWIWLY
     YISPYTWIFQ GLSINEFTYQ EYGCKTSELI PPRTPQNLLP YPEGFGGNQV CQFTSGEQIM
     DAFGITNPNY FKWVVFGILS AYIVFFYVVC FFALKYFNFE DKKSKLAVKK LKKKKKVKTT
     KQDEESAAIS SEALERIDDD NDDDADYETE IKKKKSHKKQ KEDTVIDVKS PSSLTTGSPY
     YNINNNNNNL SGSGNNIKKR KVKTPSNLSP SVNSPITINS PMPTSPSNNN NNNNSNEKSK
     NGKDIGSETG SYLQFKKLCY AVDVKVDDPD NPKKKKSQRL QLLTDIDGYV KPGQMLALMG
     PSGAGKSTLL DVLAQRKTGG HITGEILING KPPSEFTNRI RAYVEQMDVL PPTQTVREAI
     AFSARCRLPP EVTKEERESY VDKIVEVLSL SSIKDLKIGV LGDGLSVSQR KRVNIGVELA
     SNPEILFLDE PTSGLDSGDA FKVIDVVNKI AKVMNRTVIC TVHQPSAAIF EFFDQLLLLK
     QGGETIYFGP LGNQSSVILD YCDKLGMHIK PHINPADFVM TLADQGKMVE GPNGEQVPLD
     AKKAYFESDI CKKEYEIMEG QLIPDDFVIK TYDSRFASSW MTQFRALCMR SWLSRLRRPA
     IFVSNCIRSI LLAVLLGTLF VRMDYEQKDA RSRVSLLFFS FLFAGMVAIG NIPTTVLERG
     VFYREVTAGF YHSTAYMTSY VLTSYPFTLS TGILYIIPTF WIAGLDSGRH SSKFWYCLFI
     FIITYVMYDA FGLCLAVCLP NEVMASTICG IGLSLSTLFG GFVIARPNYP SAYYWCHYLD
     WLRYPLEASC TNEFTGLTFV CTNNKGAVPI PIIENGVQIA IKYYCPITNG DDFMLTYGFH
     KFMRYIDIAA IFGYIFIFVG LSFWGFKKIR WFNR
 
 
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