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Database: UniProt
Entry: A0A3L8SM17_CHLGU
LinkDB: A0A3L8SM17_CHLGU
Original site: A0A3L8SM17_CHLGU 
ID   A0A3L8SM17_CHLGU        Unreviewed;      1569 AA.
AC   A0A3L8SM17;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Canalicular multispecific organic anion transporter 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00005916 {ECO:0000313|EMBL:RLW04172.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW04172.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW04172.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW04172.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW04172.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004608}. Endosome, multivesicular body membrane
CC       {ECO:0000256|ARBA:ARBA00004333}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004653}. Late endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004656}. Melanosome membrane
CC       {ECO:0000256|ARBA:ARBA00024320}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004374}. Secreted, extracellular exosome
CC       {ECO:0000256|ARBA:ARBA00004550}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLW04172.1}.
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DR   EMBL; QUSF01000014; RLW04172.1; -; Genomic_DNA.
DR   STRING; 44316.ENSEGOP00005010140; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032585; C:multivesicular body 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; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR   CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 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; IPR032410; MTABC_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF176; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 2; 1.
DR   Pfam; PF00664; ABC_membrane; 3.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF16185; MTABC_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 3.
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:UP000276834};
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        34..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        476..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        960..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1014..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1095..1126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1146..1166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1237..1257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..524
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          612..835
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          970..1288
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1324..1558
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          260..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1569 AA;  174947 MW;  CE60290A7FECA23D CRC64;
     MSAALEKFCG SVFWNDSYLA RPDADLPVCF QQTVLVWIPL GFFWILAPWQ LLPMCKSRAK
     KSSVTKLYII KQVLAALLML TAVAELALAF VDAEQGAVPA VQYTNPSLYI ATWIMVLLVQ
     DARRFCLRRD SGVLFCFWIL TLLCGILPFQ SLVRKALQEP ISDLPRFILF FISYGLQLLL
     FLVSGFSDIA PETKEIWKKN PEVTASFLSS VTFQWYSSIV FKGYRKPLEI EDVWELKDKD
     KTKALYTAFE KNMRTAMQKA RAELEKRKRK KRRQEGDPDH GNSMSKAQSQ DILVLEEKQT
     KKKKKKGDNE DSGPPKDYPK GWLMKTLVKT FQQNLLLAVA FKVVHDALVF VSPQLLKLLI
     AFVSDEDSFA WQGYLYAILL FLAAVIQSLC LQQHFSLCFQ LGINVRASLI AAIYKKSLTM
     SGATRKESTV GETVNLMSAD AQRFMDLANF IHQLWSSPLQ IILSIVFLWG ELGPSVLAGI
     ATLVLLLPIN ALLVAKAKTI QERNMKNKDE RMKIMTEILN GIKVSLASFA VYVLVDENNI
     LDAQKAFTAI SLFNVLRFPM ATLPMVISSL VQANVSTARL ERYLSGEDLD TSAIHHNPIA
     GRQCCAFLRG HLRLGAGWQR CHKRPSCLCS VTLDIMPGSL VAVVGAVGSG KSSLVSAMLG
     EMENIRGHIN IQGSLAYVPQ QAWIQNATLK DNIIFGSELD EARYQQVLKA CALLPDLELL
     PAGDQTEIGE KGINLSGGQK QRVSLARAVY SNADIYILDD PLSAVDAHVG KYLFEHVLGP
     KGLLQKKTRI LVTHSISFLP QVDNIVVLAA GAVSEHGSYS TLLANKGAFS QFLNLYGNQE
     EDVSEENTAV VWGGVVSGQC LTLPSLIPLL VAEALAGDEE EADEAVDPCM EERTEDVVTL
     TLKREASIHR RKLSRSFSKK STSSQKKAQE EPPKKLKGQQ LIEKEAVETG RVKFSMYLRY
     LRAVGLCFTF WIVMGYVGQY AAYVGTNLWL SDWTDDSVRY QNQTYPTERR DLRIGVFGAL
     GVSQALFLLF ATMLSARGTV RASRVMHQQL LSNILRAPMS FFDTTPIGRI VNRFAKDIFT
     VDETIPMSFR SWISCFMAII STLIVICLAT PFFTVVIIPL SIFYYFVLVR NWALSEASAL
     LRAVPWWLLG FVLVTSLCCS FQRFYVSTSR QLRRLDSVTR SPIYSHFGET VSGLSVIRAY
     GHQERFLKQN EITMDINQKS VYSWIVSNRW LAIRLEFVGS LVVFFSALLA VIAKGTLEGG
     IVGLSVSSAL NVTQTLNWLV RTSSELETNI VAVERVHEYV TVKNEAPWVT KKRPPHGWPS
     RGEIQFIDYK VRYRPELDLV LQGITCNIGS TEKVGVVGRT GAGKSSLTNC LFRVLEAAGG
     KIIIDNVDIA TIGLHDLRKS LTIIPQDPVL FTGTLRMNLD PFDQYSDEEV WKALELAHLK
     TFVQGLPERL LHLVSEAGEN LSVGQRQLVC LARALLRKAK ILILDEATAA VDLETDHLIQ
     TTIRSAFADC TVLTIAHRLH TIMDSNRVMV LHAGQIVEFD SPEQLLMKQG IFSAMAKDAG
     ITAAESTAL
//
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