ID G3SVP4_LOXAF Unreviewed; 2597 AA.
AC G3SVP4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 68.
DE SubName: Full=ATP binding cassette subfamily A member 12 {ECO:0000313|Ensembl:ENSLAFP00000004322.4};
GN Name=ABCA12 {ECO:0000313|Ensembl:ENSLAFP00000004322.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000004322.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000004322.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004322.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000004322.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004322.4};
RG Ensembl;
RL Submitted (JUL-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 STRING; 9785.ENSLAFP00000004322; -.
DR Ensembl; ENSLAFT00000005165.4; ENSLAFP00000004322.4; ENSLAFG00000005158.4.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000157295; -.
DR HOGENOM; CLU_000604_19_7_1; -.
DR InParanoid; G3SVP4; -.
DR TreeFam; TF105191; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0097234; C:epidermal lamellar body membrane; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005319; F:lipid transporter activity; IEA:Ensembl.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
DR GO; GO:0035627; P:ceramide transport; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0003336; P:corneocyte desquamation; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0031424; P:keratinization; IEA:Ensembl.
DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0032379; P:positive regulation of intracellular lipid transport; IEA:Ensembl.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0045055; P:regulated exocytosis; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF36; ABC TRANSPORTER A FAMILY MEMBER 7-RELATED; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 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 Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1069..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1113..1135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1178..1198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1204..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1252..1273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1989..2011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2045..2062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2069..2089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2101..2125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2188..2209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1348..1579
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 2256..2491
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 120..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2597 AA; 293295 MW; 6718641CF3F28421 CRC64;
MASQLHQLRV LVWKNWLGVK RQPLWTLVLI LWPVIIFIIL AITRTKFPPT AKPTCYLAPR
NLPSTGFFPF LQTLLCDTDS KCKNTPYGPQ DLLRRKGIDA TVFKDNEILT KSPSLEEDSN
LSLQRTKVPG SGHTSAATVF PIPSPDLEST GTYTFNGSQV LARFLDLEKL LKQNSTSEDV
RRELCESYPT YIADHTFSWT TLGKNVFNKF CLSNMSLLES SLQELRNQIS QISSDPNNQK
IVFQDMVKAL SFFSQLQKQT AVWQLLSSFP NVFQNATTLS NLFGVLRKAS SALLVVQKVY
PHVTTNKGFR TLQKSVKHLL MTLDSTTEGG SHNTTHLWNE DDGQTLSPSS LAAQLLILEN
FEDALLNIST DSPYIPYLVC VRNITDNLAR GSQENLRLLQ STIRFRKSFL RNGSYEDSIP
PVPEIMKSKL SQLRNLTELL CDSEMSSSIE KTCQLSNISF GDLCEENAFH VQFLEAAELA
TEIASGLLYH ENVISEKLRN LLTGDPSKIN LNMDRFLEQA LQMNYLENIT QLMPTIEAML
HVNNSADSSE KPGQLIEMFK NVEELKEELR RTTGMSNMTI NKMLAIPIPD NRAEIISRVF
WLHSCDANIS NPKLEDAMKE FCNLSLTERS RQSYLIGLTL LHYLDIYNFT YKARVFFPRQ
NQKPVEKMVE LFIRLKEILN LMASRTTLLL DKMRPLKQMH LPRGVPLTQG IYRGNRMNTP
QGSFSTISQA LCSQGITTEY LNAMLPSSQR PEGNHTKDFF TYKLSKEQVA LKYGIPLNTT
PFCFSLYKDI VNMPAGPVIW AFLKPMLLGR ILYAPYTPVT KAIMEKSNVT LRQLAELREK
SQEWMDKSPF FMNSFHLINQ TIPMLQNTLR NPFVQVFVKF SVGLDAVELL KSIDELDTLR
IKLENHMDII DHLNTLSSLT VNISSCILYD RIQAANTIEE MEGEAKRLYK TNELFGSVIF
KLPSNRRWQK GYASENVSLP PVIKYTIRMS LKTAQTTRSL RTKIWAPGPH NSPSHNQIYG
RAFIYLQDSI ERAIIELQTG SNSQEIAVQV QAIPYPCFMK DNFLTSVSYS LPIVLMVAWV
VFIAAFVKKL VYEKDLRLHE YMKMMGVNTC SHFFAWFIES VGFLLVTIII LIIILKFGNI
LPKTNGFILF LYFSDYSFSV IAMSYLISVF FHNTNIAALI GSLIYIIAFF PFIVLITVEN
ELSYIVKIFM SLLSPTAFSY ASQYIARYEE QGIGLQWDNM YSSPVQDDTT SFGWLCCLIL
ADSFIYFLIA WYIRNVFPGT YGIAAPWYFP ILPSYWKERF GCSEVKHEKS NGLVFTHIMM
QNTNPSASPE CMFPSNIEPE PKDLTVGVAL HGVTKIYGSK VAVDNLNLNF YEGHITSLLG
PNGAGKTTTI SMLTGLFGAS AGTIFVYGKD IKTDLNTVRK NMGVCMQHDV LFSYLTTKEH
LLLYGSIKVP HWTKKQLHEE VKRTLKDTGL YSHRHKRVGT LSGGMKRKLS ISIALIGGSR
VVILDEPSTG VDPCSRRSIW DVISKNKTAR TIILSTHHLD EAEVLSDRIA FLEQGGLRCC
GSPFYLKEAF GDGYHLTITK KKCPNLNANS ICDTMAVTAM IRSHLPEAYL KEIIGGELVY
VLPPFSTKVS GAYLSLLRAL DNGMSGLNIG CYGISDTTVE EVFLNLTKDS QKNGDMSLEH
FPQKKIGNSS TNGVSTPDDL SVSSSNFTDR DDKILTRGER LDGFGLFLKK VMAILIKRFH
HTRRNWKGII AQVILPVVFV TTAMGLGTLR DSGNSYPELQ LSPSLYGTTE QTSFYANFNT
TTKPLVSAMW AFPGIDNICL NISDLRCLKE GSLGEWNTSG EPSTIFNVCT CSFIFQKCPE
SNYYPPHRRT YSSQVIYDLS GHPIENYLIS TANEFSQKRY GGWSFGLPLT NDLRFDITGV
PVNRTLAKVW YDPEGYHSLP AYLNSLNNFL LRVNMSKYDA ARHGIIMYSH PYPGVQDQEQ
ATISSLIDIL VALSILMGYS VTTASFVTYV VREHQTKAKQ LQHISGIGVT CYWVTNFIYD
MVFYLVPVAF SIGVIVIFRL PAFYSGNNLG AVSLLLLLFG YATFSWMYLL AGFFHETGIA
FITYVCVNLF FGINSIVSLS VVYFLSKEKP NDPTLELISE TLKRIFLIFP QFCFGYGLIE
LSQQQSVLDF LKAYGVEYPS ETFEMNKLGA MFVALVSQGT MFFFLRLLIN EWLIKKFRLF
FRKFSSSPVM EVVDEDEDVR AERLRVENGA AEFDLVQLHR LTKTYQLIHK KIIAVNNISI
GIPAGECFGL LGVNGAGKTT IFKMLTGDVI PSSGNILIRN KTGSLGHVDS HSSLVGYCPQ
EDALDDLVTV EEHLYFYARI HGIPEKDIKE TVHKLLRRLH LMPYKDRATS MCSYGTKRKL
STALALIGKP SILLLDEPSS GMDPKSKRHL WRIIAEEVQN KCSVILTSHS MEECEALCTR
LAIMVNGRFQ CIGSLQHIKS RFGRGFTVKV HLKNNEVSME ALTRFMRLHF PKTYLKDQHL
SMLEYHVPVT AGGVANIFDL LETNKTALNI TNFLVSQTTL EEVFINFAKD QKSYEAADVS
SDDSTISVDS QDDRIES
//