ID A0A2U3V2N4_TURTR Unreviewed; 1366 AA.
AC A0A2U3V2N4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LOW QUALITY PROTEIN: multidrug resistance-associated protein 9 {ECO:0000313|RefSeq:XP_004317234.1};
GN Name=ABCC12 {ECO:0000313|RefSeq:XP_004317234.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_004317234.1};
RN [1] {ECO:0000313|RefSeq:XP_004317234.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_004317234.1};
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_004317234.1; XM_004317186.1.
DR STRING; 9739.ENSTTRP00000014403; -.
DR GeneID; 101338669; -.
DR InParanoid; A0A2U3V2N4; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000245320; Chromosome 19.
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; cd18592; ABC_6TM_MRP5_8_9_D1; 1.
DR CDD; cd18599; ABC_6TM_MRP5_8_9_D2; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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 PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF10; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 12; 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:UP000245320};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..404
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 485..705
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 808..1089
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1127..1361
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1366 AA; 152343 MW; 3872BA8291CB9992 CRC64;
MVGDGPCLIS DLDWRGQQRS FSERYDPSLK TMIPVRLYAR LAPNPGDDAG LLSFATFSWL
TPVMMRGYKH TLTVDTLPPL SPYDSFDTNA KRFRILWDEE VERMGPKKAS LGREVWKFQR
TRVLMDIMAN ILCIITAAIG PMILIPQILQ QTQSTSRKVW VGVSLCTALF TTEFTKVLFW
ALAWAINYRM AIRLKVATST LVFENLVSFK TLTHISVGKL VLNILSSDSY SLFEAALFCP
LLATILILMA VCVVYAFFIV GPTALIGISV CVLFIPIQMF MAKLNSAFLX SAILVTDQRV
QTMNEFLTCI KLIXMYTWEK SFTNAIPDIR KRERRLLEKA GFVQSGNSVL APIASTIAIV
LTFTCHILLR XKLAAPVAFS VITMFNVMEF SIAILPFSVK AAAEVNVSLR RMKKILIAKS
PPSYITQPEE PDMVLLLANA TLTWEQETRG KSDLKKVQNQ KKHLLKKQRP EAYSLSPSGQ
GVTSAQEQHG SPKSVLHNIS FVVRKMGMCS KGGKVLGICG NVGSGKSSLL AALLGQMQLQ
QGIXGTLAYV SQQAWIFQGN GRENILFGEK YDHQRYQHTV RVCALQVDLS TPPYGDLTEI
GEQGLNLSGG QRQRISLAXA VYLNHEIYLL DDLLSAVDAH VGKHIFEECI EKVLXGKTVV
LVTHQLQFLE CRDEVILLED GEICEKGTXL MEERGLYAKL IHNLXGLKFK DPEHIXDAAV
VEALKESPAE RDEETGTIRV PITDEKHDGK EPETESEFVD IKGLVFVPTV PLHQLIQTES
PRGGTVTWKT YDTYIKASGG YFLSPWSLFL VMIGSSIFSD VWLGVWLNKG SKMTCGPHGI
ISTCEVGLVQ ADTGPRVYQW AYAGSMVSVL VFGISQGFTF TKTTLMASFS LHDRVFDKIL
ESPMSLFDRT PSGWLMNRFS EDTNELDVRL LFHAENFLQR FFMVPFILVI LAAVFPAVLL
VLAGLAVGFF ILLRIFHRGV QELKKVESVS WSPWFSHVAS FMQGLGTIHA YNKREDCVSN
HLLYFNCALR WFALRMDILM NIITFIVTLL VTLSFSSISA SSEGLSLSYI IQLSGLLQVC
LRTGTETQAK FTSVELLREY ISTCVPECTH PLKVGTCSLD WPSRGEITFR DYQMRYRDNT
PLILNGLNLN IQSRQTVGIV GRTGSGKSSL GMALFRLLEP ASGTILIDGM DICTAGLEDL
RTKLTVIPQD PVLFVGTVRY NLDPFASHSD EMLWQVLERT FMRDTTMKLP EKLXAEVTEN
GEDFSVGERQ LLCMARALLH NSKIILLDEA TASMDSKTGT LVQSTIKDAF KDCTVLTIAH
HLNTVLNCDH ILVLENGKVV EFDKPEVLAE KPDSAFAMLL AAENKV
//
