ID W5N0E5_LEPOC Unreviewed; 1310 AA.
AC W5N0E5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=ATP binding cassette subfamily B member 5 {ECO:0000313|Ensembl:ENSLOCP00000014104.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014104.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014104.1}
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; AHAT01004575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000014133.1; ENSLOCP00000014104.1; ENSLOCG00000011448.1.
DR GeneTree; ENSGT00940000166052; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000011448; Expressed in pharyngeal gill and 6 other cell types or tissues.
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; 2.
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:UP000018468};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..386
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 421..657
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 746..1033
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1068..1306
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..716
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 143387 MW; 52B95F5C7496EC6D CRC64;
MDTQHEEPQY DVIPDGYNNL AFVSEEEPKD GPQSENKALP RSRKKKKEGA KKEPPKLVGF
FSLFRYADGW DIVMMILGLI CAAAHGVALP LLTVVFGQMT DSFVKSGLPL NITGNFSTNI
SYSLQCDKLP GIDIEAEMTR NAYYFVGLGA AVLLLSTIHV MMFLLAAARQ TRRIRDKYFH
AVLHQEMGWF DTHQIGVLNT RLTDDINTIN DGLGDKISIF LQMFCTFITG IIIGFVYGWK
LTLVILAVSP LLAGSAAALS KILGTLTSKE LTAYASAGAV AEEILVSIRT VVAFNGQKKA
VEKYERNLQK AKDLGVKKAI TTNASMGLTQ FIIFGSYALA FWYGTKLSVD EPENYSIGKV
LTVFFSVMIG AFSLGQAAPN LESIANARGA AYEIYSTIDS PHPIDSSSKE GYKPGSVQGD
IEFKNIHFSY PSRKDVKILQ GLDLKIERGK TIALVGASGC GKSTTIQLLQ RFYDPDAGEV
TLDGRDIRSL NVKWLRENMG IVSQEPVLFA TTIAENIRYG REDATDEDIE RAVREANAYD
FISKLPDKLN TMVGERGAQL SGGQKQRIAI ARALVKNPKI LLLDEATSAL DTQSESVVQT
ALDKARAGRT TIMIAHRLST IRTADVIAGF SSGVVVEQGT HREMMAKKGV YYSLVMQQED
SEGSTFSFDD EASEDEPELV NNGASQASIF QRSSIRRSRQ SVRRSAKTKL RRRKRGKKKK
EEEESLPDIP FGKILEMNKP EWPFLVIGCV ASLIGGAVYP CVAIVFSKII GVFGELDPDV
RRGKTTLLSL MFLLIGAVAF VTYFLEGFMF GKSGEILTMR LRSQSFKAMI RQDIAWFDDN
KNAVGILTTK LATDASLVKG AAGARLGLVT RLLCSLTIAI IVAFVFSWQL TLLILACVPF
LVGANIIQMK STAGHASKDQ KSLELSGKIS TETVENIRTV AALMSWDKSF AAMYKMNIQN
AKAALCKAPI YGLTYALGQA VPYFVNASIF RFGSWLIAHC YTEFENVFLV FSVIVFAAMS
IGQSSSFAPD FAKAKASAQR ITQLLERKPD IDIYNEGGEK PSSFEGNVEF SSVHFAYPTR
QGVQVLQGLS VKVAKGQTLA LVGGSGCGKS TSVQLLERFY NPAAGQVLVD GKDTKSLNLA
WLRAQLGLVS QEPILFDCSI AENIQYGDCS REVSQQEIEE AAKRANIHNF ILSLPQQYNT
KVGDKGAQLS GGQKQRIAIA RALVRKPKVL LLDEATSALD TESEKIVQQA LDEARQGRTC
IVIAHRLSTI QNADIIAVIR DGQVVEQGTH SELMARQGAY SALVNAQVSV
//
