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Database: UniProt
Entry: M3XWB3_MUSPF
LinkDB: M3XWB3_MUSPF
Original site: M3XWB3_MUSPF 
ID   M3XWB3_MUSPF            Unreviewed;      2311 AA.
AC   M3XWB3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=ATP binding cassette subfamily A member 4 {ECO:0000313|Ensembl:ENSMPUP00000003363.1};
GN   Name=ABCA4 {ECO:0000313|Ensembl:ENSMPUP00000003363.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003363.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000003363.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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   EMBL; AEYP01031842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9669.ENSMPUP00000003363; -.
DR   Ensembl; ENSMPUT00000003429.1; ENSMPUP00000003363.1; ENSMPUG00000003394.1.
DR   eggNOG; KOG0059; Eukaryota.
DR   GeneTree; ENSGT00940000155624; -.
DR   HOGENOM; CLU_000604_19_0_1; -.
DR   InParanoid; M3XWB3; -.
DR   OMA; EVHQSMG; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005502; F:11-cis retinal binding; IEA:Ensembl.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005503; F:all-trans retinal binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0140347; F:N-retinylidene-phosphatidylethanolamine flippase activity; IEA:Ensembl.
DR   GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:Ensembl.
DR   GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
DR   GO; GO:0045332; P:phospholipid translocation; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR   GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
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; IPR005951; ABCA4/ABCR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01257; rim_protein; 1.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   PANTHER; PTHR19229:SF190; RETINAL-SPECIFIC PHOSPHOLIPID-TRANSPORTING ATPASE ABCA4; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        695..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        731..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        758..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1680..1702
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1722..1748
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1760..1779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1791..1813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          929..1160
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1938..2170
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1297..1343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2289..2311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2311 AA;  260804 MW;  AF9AE741B00EB9B8 CRC64;
     MGFVRQIQLL LWKNWTLRKR QKIRFVVELA WPLSLFLILI WLRNINPLYS QHECHFPNKA
     MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGTVSNYNNS ILARVFRDFQ ELVMKAPERQ
     NLGHVWKELQ TLSQLMDTLR THPERVAGRG IRIRDVLKDE ETLTLFLTRN IGLSDSVVYL
     LVNSQVRPEQ FAHGVPDLML KDIACSETLL RRFIIFSQRH GAQTVRDAMC SLSQGTLQWV
     EDTLYANVDF FKLFRVLPTL LDSSSQGINL RSWGRIFSDM SPRIQEFIHR PSVQDLLWVA
     RPLMQTGGPE TFTQLMSVLS DLLCGYPEGG GSRVFSFNWY EDNNYKAFLG IDSTRKDPIY
     SYDKRTTTFC NALIQSLESN PLTKIAWRAA KPLLMGKILF TPDSPAARRI LKNANSTFEE
     LERLRKLVKA WEEVGPQIWY FFDKSTQMTM IRDTLENPTV KAFLNNQLGE EGITVEAVLN
     FLDRGPRENQ ANDVANLNWK DVFNITDHTL RLASRYLECL ILDKFESYDD EIQLTQRALS
     LLEENRFWAG VVFPDMYPWT SALPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED
     FRYIWGGFAY LQDMIERGIT RSQAQVEVPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV
     LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM
     HGRILHYSDP FILFLFLLTF STATIMQCFL LSTFFSRASL AAACSGVIYF TLYLPHILCF
     AWQDRMTADL KMAVSLLSPV AFGFGTEYLA RFEEQGLGLQ WNNIGRSPME GDEFSFLMSM
     KMMLLDAALY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEACSTRE ERALEKTEPI
     TEEMEDPGHP EGINDSFFER ELPGLVPGVC VKNLVKIFDT YSRPAVDRLN ITFYENQITA
     FLGHNGAGKT TTLSILTGLL PPTSGTVLIG GKDIETSLDE VRQSLGMCPQ HNILFHHLTV
     AEHILFYAQL KGKSWEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGGA
     KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIISQGRLYC
     SGTPLFLKNC FGTGFYLTLV RKMKNIQSQR TGYEGNCSCA SEGFSSRCPA HIDEITPEQV
     LDGDVNELMD MIQHHVPEAK LVECIGQELI FLLPNKNFKQ RAYASLFREL EDTLADLGLS
     SFGISDTPLE EIFLKVTEDS DSGPLFAGGT HQKRENVSLQ HPWLGPKDKA RQIPQGSDGC
     SAEPAPPRGG QPSSEPEPEH RSRLNTGAPL LLQHVQALLI KRFHHTVRSH KDFLAQIVLP
     ATFVFLALML SLIVPPFGEY PALTLHPWMY GQQYTFFSLD QPGSEQLAAL ADILLNKPGF
     GNRCLKEEWL PEYPCVNSTP WKTPSVSPNI THLFQKQKWT PEDPSPSCMC STREKLTMLP
     ECPEGAGGLP PPQRIQRSTE VLQDLTNRNI SDFLVKTYPS LIRSSLKSKF WVNEQRYGGI
     SIGGKLPVLP ITGVNVSGVC KQPGDLGRTF DGPITREASK EMPAFLKHLE TEDNIKVWFN
     NKGWHALVSF LNVAHNAILR TSLHKDKNPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA
     VVAICVIFAM SFVPASFVLY LIQERVNKAK HLQFVSGVSP TTYWLTNFLW DIMNYAVSAA
     LVVGIFIGFQ KKAYTSPENL PALVALLMLY GWAVIPMMYP ASFLFDIPST AYVALSCANL
     FIGINSSAIT FILELFENNQ TLLRFNAMLR KLLVIFPHFC LGRGLIDLAL SQAVTDVYAR
     FGEEHSTNPF QWDLIGKNLV AMAAEGVVYF LLTLLIQHHF FLTRWIAEPA KEPIIDEDDD
     VAEERQRIIS GGNKTDILRL NELTKIYSGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT
     TFKMLTGDTT VTSGDATIAG KSILTNISDV HQNMGYCPQF DAIDDLLTGR EHLYLYARLR
     GVPADEIERV ANWSIQSLGL SLYADRLVGT YSGGNKRKLS TAIALMGCPP LVLLDEPTTG
     MDPQARRMLW NTIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGTFQC LGTIQHLKCK
     FGDGYIVTMK IRSPKEDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFR
     LLISHKDSLL IEEYSVTQTT LDQVFVNFAK QQTEIHDLPL HPRAAGASRQ AKVLLLLFHS
     PLSEADPQLR DWYAGSEGPQ GPDMPPTESP P
//
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