ID M3ZER9_XIPMA Unreviewed; 2312 AA.
AC M3ZER9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Retinal-specific ATP-binding cassette transporter-like {ECO:0000313|Ensembl:ENSXMAP00000000711.2};
GN Name=ABCA4 {ECO:0000313|Ensembl:ENSXMAP00000000711.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000000711.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000000711.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000000711.2};
RG Ensembl;
RL Submitted (NOV-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; 8083.ENSXMAP00000000711; -.
DR Ensembl; ENSXMAT00000000713.2; ENSXMAP00000000711.2; ENSXMAG00000000681.2.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000155624; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR InParanoid; M3ZER9; -.
DR OMA; EVHQSMG; -.
DR OrthoDB; 6951at2759; -.
DR Proteomes; UP000002852; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002852};
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 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1407..1428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1714..1736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1766..1783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1795..1813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1825..1850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 975..1206
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1972..2204
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 881..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2312 AA; 262318 MW; 336D7178D29E2F16 CRC64;
MKTGSQIRLL LWKNWTLRKR QKIRFLVEIS WPVLLFIGLV WLRKANPLYQ QHECHFPNKA
LPSAGILPWI QGIFCNANNP CFRYPTQGES PGIVSNYNNS VLAQFYVDIQ ELLLNETEVR
QYGRLWREMA SFSNFMDTLR NNPSAVAGRG LKIDDILKDD EILTAFLLRD AGLSESIVYQ
LVNAQLRLEQ FAFGVPDLQL KDIACSQALL EHFIIFPSRM GLHGVRNAMC ALSQQRLQRI
EDILYANLDF FKIFRLMPQV LDSQGIDLHY WGLVLKGASE KIQVLLKRES SQELLRVVSS
LFQAGGPSSF TQLMSGVSSL FCGYPEGGGS RVLSFNWYED NNYKVFLGVN GSKNHNYVYD
DATTPFCNSL MQTLESNPVT KIVWNLVKPL LMGKILYTPD SPAVRQILKS ANTTFEELER
LQNMAKAWEE VGPQLWAFFN NSVQMNMIRD TLRNPTVMHF MDNSLVESTF STKDILNFLH
NGPEADREEG MPNLDWRNIF NIADQIIRMF NQYGECVSLD KFVAYTDESQ MIHQALYLLE
ENKFWAGVVF MDMYPWTTSI PRHVKYKIRM DIDSVERTNK IKDRYWDPGP RADPMEDQRY
LWGGFAYLQD MIEHGIIKLH TGNDWPLGVY VQQMPYPCYV DDLFMITLNR CFPMFMVLAW
IYSVSMTVKS IVLEKELRLK ETLKTMGVNN GVIWYTWFID SFIMMTASTA LLTAIITGGK
VLNYSDPLLV FFFLLIFTVA TIMQCFLMSV FFNKANLAAA CSGIIYFTLY LPHILCFAWQ
DRITNNMKLA ASLLSPVAFG FGTEYLSRYE EQGLGLQWNN IQTSPLEKDT YSFLTSILMM
VFDAVLYGIL AWYLDNVFPG QYGIGRPFYF PLQPSYWQKP APSYQEMTEQ DSKKPEAENQ
ELDIESRGTP ETYTCNGSAS KKTCKHQSKR ERLERERELL KQQQENPNQE EEDPNDGSEG
PVFFEQDPLG LVLGVQIQDL VKVYDGSSRP AVNCLNICFY EGQITSFLGH NGAGKTTTLS
ILTGLYPPTS GTAYINGRDI KTDIDIIRTS MGMCPQYNIL FNHLTVEEHI LFYSLLKGRT
PEEAEAEVEN MLLDLGLPHK RDEEAQNLSG GMQRKLSVAM AFVGGSKVVI LDEPTSGVDP
YSRRSIWDLL LKYRTGRTVI LSTHHMDEAD LLSDRIAIIS KGQLYCCGSP LFLKNCFGVG
FYLTLVRRMK DIRKRENECD CASDCSCSCS ICTKYKDQSQ NQHQQLDRVL DGDIDNITSL
IHHHVPEAKL IETIGQELTY LLPNKGFKHR AYASLFRELE ETLADMGLSS FGISDTSLEE
IFLKVTADGE AANNATTAEQ WMLQGRHNGS KVGVGQEEEN NSVNGITSDS SAGKGSRQVK
GFSLILKHFH ALLVKRFHHA TRSRKDFLAQ IVLPATFVLI SLIFTLIVPP FGEYPSLTLM
PWMYGQQFTF FSNERPFDPR MKHFTDRLLS MPGLGTRYMQ KEPSEMMCNT SASDWEQPSV
SPVVHNILQS PEWNQRNPSP SCQCSTSKKL TMMPICPAGA GGLPPRQRVE ATGDIMLDLT
DRNISDYLVK TYPSLIRTSL KSKYWVNEQR YGGLSIGGQL PILDVDPRDI QKVFHQLGQM
LNITGGHYSR LALREIGTFL HFMESEFNVK VWYNNKGWHA MVAFMNVANN AILRAFLPSF
AKPVEYGITA INHPLNLTKE QLSEVTVLTT SVDAVVAICV IFAMSFIPAS FVLYLIQERV
TKAKHLQFVS GVSPCVYWVA NFFWDLMNYF LSTAMVVGIF MAFDKKCYTS PTNLPALIAL
LLLYGWSVTP MMYPMSYVFS IPSTAYVSLS CINLFIGINS SAITFILELF ENNRSLLTFN
EWLKKLLLVF PHFCLGRGLI DMAMNQAVTD VYARFGEEHK MDPFRWDFVG KNIFFMLVEG
FVYFSLNLLI QYRFFLDHWL PDGKRTVVQD EDEDVAEERE RIYEGGSKKD ILQVRDLSKT
YVGRKRAAVD RICVGVPAGE CFGLLGVNGA GKTTTFKMLT GDTDASSGEA TVAGYSILTE
ILDVHQNMGY CPQFDAIDEL LTGREHLYLY ARLRGVPESE IPRVAEWGIQ KLGLTEYAGC
RAGTYSGGNK RKLSTAIAMI GCPALVLLDE PTTGMDPHSR RFLWNAIMSV IQDGRAVVLT
SHSMEECEAL CTRLAIMVNG TFKCLGTIQH LKYKFGDGYV VTMKIKAAKA GLSPDLEPVE
SFMESSFPGC VQREKHYNTL QYEIASSSLA RIFQLVVANK DRLSIEDYSV SQTTLDQVFV
NFAKQQTGED DDVTLHRQTA RKVMKVSPVK RK
//
