ID F6HE44_VITVI Unreviewed; 1294 AA.
AC F6HE44;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=ABC transporter B family member 11 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_05s0020g00890 {ECO:0000313|EMBL:CCB50296.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB50296.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FN595749; CCB50296.1; -; Genomic_DNA.
DR RefSeq; XP_002275143.2; XM_002275107.4.
DR RefSeq; XP_010649698.1; XM_010651396.2.
DR RefSeq; XP_010649699.1; XM_010651397.2.
DR SMR; F6HE44; -.
DR PaxDb; 29760-VIT_05s0020g00890-t01; -.
DR EnsemblPlants; Vitvi05g00261_t001; Vitvi05g00261_P001; Vitvi05g00261.
DR GeneID; 100244232; -.
DR Gramene; Vitvi05g00261_t001; Vitvi05g00261_P001; Vitvi05g00261.
DR KEGG; vvi:100244232; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; F6HE44; -.
DR OrthoDB; 5487044at2759; -.
DR Proteomes; UP000009183; Chromosome 5.
DR ExpressionAtlas; F6HE44; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..975
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..359
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 394..630
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 729..1015
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1050..1287
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1294 AA; 140128 MW; 4030927B64989549 CRC64;
MAGENGWRGG KYTEQATAST SHSSVMEIEK VPNDTDSKQE TDTNREKEES TRTVPFCKLF
SFADSWDYLF MFVGAVAAAA NGVSTPLMTI LFGDVINSFG KDSNSKDMVH EVSKVSLKFV
YLAIGTGVAS FLQVTCWMLT GERQAARIRS LYLKTILRQD VGFFDKFTNA GEVVGRMSGD
TVFIQDAMGE KVGKFIQLMA TFLGGFIVAF CKGWLLTLVM LSCFPPLVIV GAFTTMFITK
MASRGQAAYS VAAVVVEQTI GSIRTVASFT GEKQAIAKYN QSLSKAYTSG VQESVLSGLG
FGLFMFVLFA SYALAMWFGS KMIIDKGYTG GAVMNIIFSV VAGSMSLGQA SPCLSAFGSG
QAAAFKMFET IERKPEIDAY SSDGQKLDDI QGDVELRDVY FSYPTRPDEQ VFKGFSLSIP
SGTTAALVGE SGSGKSTVIS LIERFYDPQA GEVLIDGINL KEFQLRWIRG KIGLVSQEPV
LFTSSIRDNI AYGKDGATIE EIRAAAELAN ASKFIDKLPQ GLDTLVGEHG TQLSGGQKQR
VAIARAILKD PRILLLDEAT SALDAESERV VQEALDRVMI NRTTIIVAHR LSTVRNADMI
AVIHRGKIVE KGAHSELIKD PDGAYSLLIR LQEISSEQNA SHDQEKPEIS VDSGRHSSKR
MSLLRSISRS SSIGQSSRHS FSMSFGVPPD INIIETAPDG QDPAPLEHPP KVPLGRLAYL
NKPEIPFLLL GTIAAVVNGA VFPVFGILIS SIIKSFFKPP HELRKDARFW ALMFVVLGLV
SFSSLSLRSY LFSTAGFKLI KRIRAMCFEK VVYMEVSWFD EADHSSGSIG ARLSADAAMV
RSLVGDALSL LVQNSAAMIA GLVIAFVANW KMSFIILVLL PLFGANGYVQ VKFLKGFTAD
AKKKYEEASQ VANDAVGSIR TVASFCAEEK VMQLYQQKCE GPMNAGIREG LVGGVGYGVS
FFLLFAVYAT AFYAGARLVD VGQATFAEVF QVFFVLTLAA VGVSQSSSLA PDTGKAKNAA
ASIFAILDRE SKIDSSDESG TTLENVKGEI EFHHVSFRYP TRPDIQIFRD LCLAIHSGKT
VALVGESGSG KSTAISLLQR FYDPDSGHIT LDGVEIQKLQ LKWFRQQMGL VSQEPVLFNE
TIRANIAYGK EGNATEAEIS AAAELANAHK FISGLQQGYD TTVGERGIQL SGGQKQRVAI
ARAIVKDPKI LLLDEATSAL DAESERVVQD ALDRVMVNRT TLVVAHRLST IKGADLIAVV
KNGAIAEKGK HETLINIKDG IYASLVALHM SASS
//
