ID G3QL92_GORGO Unreviewed; 1318 AA.
AC G3QL92;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=ATP binding cassette subfamily B member 11 {ECO:0000313|Ensembl:ENSGGOP00000003239.4};
GN Name=ABCB11 {ECO:0000313|Ensembl:ENSGGOP00000003239.4};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000003239.4, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000003239.4, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000003239.4, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000003239.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily.
CC {ECO:0000256|ARBA:ARBA00007577}.
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DR EMBL; CABD030016896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000003313.4; ENSGGOP00000003239.4; ENSGGOG00000003287.4.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000157564; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR TreeFam; TF105193; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000003287; Expressed in liver and 1 other cell type or tissue.
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 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
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:UP000001519};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..818
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..379
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 414..650
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 753..1040
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1075..1313
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1318 AA; 145910 MW; CD7CD98F296A9377 CRC64;
MSDSVILRSI KKFGEENDGF ESDKSCKLQD EKKGDGVRVG FFQLFRFSSS TDILLMFVGS
LCAFLHGIAQ PGVLLIFGTM TDVFIDYDVE LQELQIPGKA CVNNTIVWTN SSLNQNMTNG
TRCGLLNIES EMIKFATYYA GIAVAVLITG YIQICFWVIA AARQIQKMRK FYFRRIMRME
IGWFDCNSVG ELNTRFSDDI NKINDAIADQ MALFIQRMTS TICGFLLGFF RGWKLTLVII
SVSPLIGIGA ATIGLSVSKF TDYELKAYAK AGVVADEVIS SMRTVAAFGG EKREVERYEK
NLVFAQRWGI RKGIVMGFFT GFVWCLIFLC YALAFWYGST LVLDEGEYTP GTLVQIFLSV
IVGALNLGNA SPCLEAFATG RAAATSIFET IDRKPIIDCM SEDGYKLDRI KGEIEFHNVT
FHYPSRPEVK ILNDLHMVIK PGEMTALVGP SGAGKSTALQ LIQRFYDPCE GMVTVDGHDI
RSLNIQWLRD QIGIVEQEPV LFSTTIAENI RYGREDATME DIVQAAKEAN AYNFIMDLPQ
QFDTLVGEGG GQMSGGQKQR VAIARALIRN PKILLLDMAT SALDNESEAM VQEALSKIQH
GHTIISIAHR LSTVRAADTI IGFEHGTAVE RGTHEELLER KGVYFTLVTL QSQGNQALNE
EDIKGKLDAT EDDMLARTFS RGSYQDSLRA SIRQRSKSQL SYLVHEPPLA VVDHKSTYEE
DRKDKDIPVQ EEVEPAPVRR ILKFNAPEWP YMLVGSVGAA VNGTVTPLYA FLFSQILGTF
SIPDKEEQRS QINGVCLLFV AMGCVSLFTQ FLQGYAFAKS GELLTKRLRK FGFRAMLGQD
IAWFDDLRNS PGALTTRLAT DASQVQGAAG SQIGMIVNSF TNVTVAMIIA FSFSWKLSLV
ILCFFPFLAL SGAIQTRMLT GFASRDKQAL EMVGQITNEA LSNIRTVAGI GKERRFIEAL
ETELEKPLKT AIQKANIYGF CFAFAQCIMF IANSASYRYG GYLIPNEGLH FSYVFRVISA
VVLSATALGR AFSYTPSYAK AKISAARFFQ LLDRQPPISV YNTAGEKWDN FQGKIDFVDC
KFTYPSRPDS QVLNGLSVSI SPGQTLAFVG SSGCGKSTSV QLLERFYDPD QGKVMIDGHD
SKKVNVQFLR SNIGIVSQEP VLFACSIMDN IKYGDNTKEI PMERVIAAAK QAQLHDFVMS
LPEKYETNVG SQGSQLSRGE KQRIAIARAI VRDPKILLLD EATSALDTES EKTVQVALDK
AREGRTCIVI AHRLSTIRNA DIIAVMAQGV VIEKGTHEEL MAQKGAYYKL VTTGSPIS
//
