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Database: UniProt
Entry: A0A1Q9F607_SYMMI
LinkDB: A0A1Q9F607_SYMMI
Original site: A0A1Q9F607_SYMMI 
ID   A0A1Q9F607_SYMMI        Unreviewed;      1278 AA.
AC   A0A1Q9F607;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Multidrug resistance protein 1 {ECO:0000313|EMBL:OLQ15128.1};
GN   Name=ABCB1 {ECO:0000313|EMBL:OLQ15128.1};
GN   ORFNames=AK812_SmicGene777 {ECO:0000313|EMBL:OLQ15128.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ15128.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ15128.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ15128.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OLQ15128.1}.
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DR   EMBL; LSRX01000007; OLQ15128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9F607; -.
DR   OMA; FSTEFFC; -.
DR   OrthoDB; 5487044at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
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; 1.
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; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF503; LP14331P; 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:UP000186817};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        108..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        708..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        753..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        857..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        934..962
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        974..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..350
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          394..633
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          710..998
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1034..1275
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          640..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1278 AA;  139043 MW;  94FA257A4401EC1A CRC64;
     MASNQADDAD DEMVQVEAKV ETEEVQTKNK IPAASLCKLF SMMDFVEVVV LLVGCLGAIG
     NGLSQPLLCI VFGDLIDGMG EATGGAESFT PEQMLGAMDG MMSQMEELCI TMMLVGVGAT
     FAAFLQGACF KIFAEKQAFK YRVLYFDTVL HQDVSWFDTK EVAALPAEIN DDLEKIQDAF
     GDKFGNGMMA ISAFMGGFGC AFGMGWLIAL VMCSILPFMG VGAAFMGKAV QEIQNESQSW
     YAKASAVVEE CLNAMRTVVA FGGEHRELKK FSAALVETRR GGVKNGFKVG AGMGYTMMII
     FLGYGLAFWF GMTLRYNEEL NPATGKLWEP GTIMAIFFCI FIGSFMIGNL DPSLKAMKAA
     QTAAGRFFRA LENKPDIQCR VEDKRQDISS IEKFDFENVH FTYPARPDVK VLNGLSLSIQ
     RGQKVAVVGE SGSGKSTVMA LLERFYDPDS GAVLVNGQNM TSFKISAIRR CIGYVGQEPV
     LFASSIRHNI MQGNPSASKE DFVKACNDAQ LGFVDNLPEK YNTFVGSGGG QLSGGQKQRI
     AIARALLKKA SFLFLDEATS ALDNTSEKMI QATIDSISAN TADGLGIVSI AHRLSTVRNS
     DLIYVMSRGT LVEHGNHASL MEKKGTYYAL VAAQESSHKA EDEEKDAAAI SNDHTAQNVV
     RRSSTNSGES ETQRVKREKD AEANREKEIS KNYKVPMRRL LSYNRPEWPF FIPAILGAVV
     DGSAMPVCTI ALVGSMSGFF KPDKEEMRAD LELMALTFVI IGVSAFIGST VSHGCFSILG
     EAMTQRLRVA ILTGMFRQEV GFHDDPANTP GMLSKALELW AFRVTTLCKS VQAKAAAMSS
     LLVGLVIAFV YCWEMSLVML GSIPIMIAAQ AIQMLVLLGA SKNENENITN ANQIVVDSVM
     NARTVQALGV EKGLVGMYVS WVEKSLVGMW RRNILAGLGF GISNGIMFFI MAGGFYVASI
     LIKEGVADFE GVMMAFMGIF YAGMGAGQAA VMVGDATKAK VACHDMFQLM DRVSAIEGLE
     PTGDTPKQLE AGQIEFRDVK FFYPFRPEIQ VLKGITFSIS QGQSVGLVGP SGGGKSTVMS
     LIQRFYDPQE GQVFIGADRV ALNSVNIRWW RRQIGFVGQE PILFNTTVRA NIMYGLDDGE
     TVSDEYVSQC EKMSNLAFLY KNGNKGLETE VGPRGSRLSG GQKQRVAICR ALIRNPPVML
     LDEATSALDT QSEAIVQKAL EAAREGRTSF AIAHRLSTIQ GCDVILVNAD GRVVEKGNHE
     ELMALKGVYY KLQMQAQK
//
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