ID A0A1S3GXT1_DIPOR Unreviewed; 1576 AA.
AC A0A1S3GXT1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-binding cassette sub-family A member 8-like isoform X1 {ECO:0000313|RefSeq:XP_012893505.1};
GN Name=LOC106003217 {ECO:0000313|RefSeq:XP_012893505.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012893505.1};
RN [1] {ECO:0000313|RefSeq:XP_012893505.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012893505.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_012893505.1; XM_013038051.1.
DR STRING; 10020.ENSDORP00000009024; -.
DR GeneID; 106003217; -.
DR KEGG; dord:106003217; -.
DR InParanoid; A0A1S3GXT1; -.
DR OrthoDB; 6951at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF148; ABC-TYPE ORGANIC ANION TRANSPORTER ABCA8; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840,
KW ECO:0000313|RefSeq:XP_012893505.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 224..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 862..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 979..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1017..1038
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1058..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1088..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1155..1172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..714
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1240..1473
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1194..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 178566 MW; C85178C3A4C1733F CRC64;
MGNREIQVCQ QTWALLHKNI LKKWRMKRET LMEWMNAFLL LLLLYIYPND HQVNDFSSLN
SMDLGRVDSF SGPRFTIAYT PLTNTTQQIM KKVASTSFMT GREVFGMSDE ESIKEVTANY
HEEIARVIFT DTYSYHLKFV LGKRIPEKKE HRDHTAHCVE IDEDIDCQLS IFWKEGFVAL
QAAINAAIIE VTTNHSVMEE LMSVTGKLMV VHPFIGQGGV TTDFFILFCI IAFSPFSYYA
SANVTRERKK MKGLMKMMGL RDLAFWLSWG LLYAGFIFIM ALCLALVIKS IQFFVMTDFM
IVFTLFLLYG LSTIALAFLM SVLVKKSFLT GQLVFLLTIF WGSLGFTALY RYLPVSLEWI
LSIFSPFAFM LGMSQMLHLD YDLNSNASPD PSSSNLIIAT NFMLAFDTFL YLALTMYFEK
ILPNEYGHRY PPLFFLKSSF WSPEQKPEHM TLDNVVDSDS SLNDSFEPVS PEFHGKEGIR
IRNVTKEYKG KPDKIEALKD LALDIYEGQI TAILGHSGAG KSTLLNVLSG LSVPTKGSVT
IYNKELSDAA ELENILQMVG VCPQSNVQFD FLTVRENLRL FAKIRGILPQ EVDKEVNRVL
LELEMKNIQD VLAQNLSGGQ KRKLSFGIAI LGDPQIFLLD EPTAGLDPIS RHRVWNLLKE
RKADRVILFS TQFMDEADIL ADRKVFLSKG KLKCAGSSLF LKKKWGIGYH LSLQLKEICA
RENITSLVKQ HIPNAKLSAE SEGKLVYTLP LETTCRFPEL YKDLDNSPGL GIENYGVSMT
TLNEVFLKLE GKSAVDELDT DILGDTQVER AGDTERLMEM EHILSSLREM RKMTSGVALW
AYQICAIAKV RLLKLKHEKK ALLSLLLILA AGFCPLLLEY ILIKIYQNSY TWELSPHLYF
LALGQPPQAP LTQLLIINKT GASIDDFLHS VEHQNIALEV DKSGTGTGVD DPSYNGAIIV
SGNEKKIQSN PFQYLGHTTF WLILASSCPP YIAMSSIDDY KSKTWSQLRI SGLFPSAYWF
GQACVDIPLY CFIFIFMYLM DFALSFQETL FTVVNRIIQI PCSIGYVLSL IFFTYVISFI
FRKGRKNSGI WSFCFFVITL FSVAGFFFEN YENIPLYCIT FLIPPATLIG CLFISLDLIM
LSVFGEEGSR RTDPFLVLLI PLLHFFIFLF ILRCLEWKFG KKSMRKDPFF RISPRSSDAL
QNPEQPEGED EDVQMERVRT TNSLNSTNFD ETPVIIASCL RKEYARKRKH CFSKRKNKIA
TRNISFCVRK GEILGLLGHN GAGKSTSIKV ITGDMKPTAG QVLLKGSSEG DPLGFLGYCP
QEDVLWPSLT VREHLEVFAA VKGLSKGDKE VTITRLVDAL KLQDHLKAPV KTLAEGVKRK
LCFALSILGN PSVLLLDEPS TGMDPEGQQQ MWQAIRATVR NTEGAALLTT HYMAEAEAVC
DRVAIMVSGR LRCIGSIQHL KSKFGKDYLL EMKVKTPAQG EPLHEEILKL FPQAARQDRY
SSLMVYKLPV EDVRPLAQAF FKLEKVKQNF DLEDYSLSQS TLEQVFLELS KEQELDGFDE
ELDLSVKWKL LPQEEP
//
