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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//