ABCA4_MOUSE
ID ABCA4_MOUSE Reviewed; 2310 AA.
AC O35600;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Retinal-specific phospholipid-transporting ATPase ABCA4 {ECO:0000250|UniProtKB:P78363};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P78363};
DE AltName: Full=ATP-binding cassette sub-family A member 4;
DE AltName: Full=RIM ABC transporter;
DE Short=RIM protein {ECO:0000303|PubMed:9202155};
DE Short=RmP {ECO:0000303|PubMed:9202155};
DE AltName: Full=Retinal-specific ATP-binding cassette transporter;
GN Name=Abca4 {ECO:0000312|MGI:MGI:109424}; Synonyms=Abcr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=9202155; DOI=10.1016/s0014-5793(97)00517-6;
RA Azarian S.M., Travis G.H.;
RT "The photoreceptor rim protein is an ABC transporter encoded by the gene
RT for recessive Stargardt's disease (ABCR).";
RL FEBS Lett. 409:247-252(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10412977; DOI=10.1016/s0092-8674(00)80602-9;
RA Weng J., Mata N.L., Azarian S.M., Tzekov R.T., Birch D.G., Travis G.H.;
RT "Insights into the function of Rim protein in photoreceptors and etiology
RT of Stargardt's disease from the phenotype in abcr knockout mice.";
RL Cell 98:13-23(1999).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10852960; DOI=10.1073/pnas.130110497;
RA Mata N.L., Weng J., Travis G.H.;
RT "Biosynthesis of a major lipofuscin fluorophore in mice and humans with
RT ABCR-mediated retinal and macular degeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7154-7159(2000).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22735453; DOI=10.1038/ncomms1927;
RA Quazi F., Lenevich S., Molday R.S.;
RT "ABCA4 is an N-retinylidene-phosphatidylethanolamine and
RT phosphatidylethanolamine importer.";
RL Nat. Commun. 3:925-925(2012).
CC -!- FUNCTION: Flippase that catalyzes in an ATP-dependent manner the
CC transport of retinal-phosphatidylethanolamine conjugates like the 11-
CC cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine
CC from the lumen to the cytoplasmic leaflet of photoreceptor outer
CC segment disk membranes, where N-cis-retinylidene-
CC phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-
CC trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-
CC retinol (all-trans-rol) and therefore prevents the accumulation of
CC excess of 11-cis-retinal and its schiff-base conjugate and the
CC formation of toxic bisretinoid (PubMed:10852960, PubMed:10412977,
CC PubMed:22735453). Displays both ATPase and GTPase activity that is
CC strongly influenced by the lipid environment and the presence of
CC retinoid compounds (By similarity). Binds the unprotonated form of N-
CC retinylidene-phosphatidylethanolamine with high affinity in the absence
CC of ATP and ATP binding and hydrolysis induce a protein conformational
CC change that causes the dissociation of N-retinylidene-
CC phosphatidylethanolamine (By similarity).
CC {ECO:0000250|UniProtKB:F1MWM0, ECO:0000269|PubMed:10412977,
CC ECO:0000269|PubMed:10852960, ECO:0000269|PubMed:22735453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-all-trans-
CC retinylidenephosphatidylethanolamine(out) = ADP + H(+) + N-all-trans-
CC retinylidenephosphatidylethanolamine(in) + phosphate;
CC Xref=Rhea:RHEA:67188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167884,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10412977,
CC ECO:0000269|PubMed:10852960, ECO:0000269|PubMed:22735453};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67189;
CC Evidence={ECO:0000305|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22735453};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:22735453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + N-11-cis-retinylidenephosphatidylethanolamine(out)
CC = ADP + H(+) + N-11-cis-retinylidenephosphatidylethanolamine(in) +
CC phosphate; Xref=Rhea:RHEA:67192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167887, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F1MWM0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67193;
CC Evidence={ECO:0000250|UniProtKB:F1MWM0};
CC -!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and
CC ceramide. ATPase activity is stimulated by phosphatidylethanolamine.
CC Phospholipids translocase activity is highly reduced by berylium
CC fluoride and aluminum floride. N-ethylmaleimide inhibits phospholipid
CC translocase activity. {ECO:0000250|UniProtKB:P78363}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P78363}.
CC Cell projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:9202155}. Note=Localized to the rim and incisures
CC of rod outer segments disks. {ECO:0000269|PubMed:9202155}.
CC -!- TISSUE SPECIFICITY: Retinal-specific (PubMed:9202155). Seems to be
CC exclusively found in the rims of rod photoreceptor cells.
CC {ECO:0000269|PubMed:9202155}.
CC -!- DOMAIN: The second extracellular domain (ECD2, aa 1395-1680) undergoes
CC conformational change in response to its specific interaction with its
CC substrate all-trans-retinal. Nucleotide binding domain 1 (NBD1, aa 854-
CC 1375) binds preferentially and with high affinity with the 11-cis
CC retinal. {ECO:0000250|UniProtKB:P78363}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:F1MWM0}.
CC -!- PTM: Proteolytic cleavage by trypsin leads to a 120-kDa N-terminal
CC fragment and a 115-kDa C-terminal fragment that are linked through
CC disulfide bonds. {ECO:0000250|UniProtKB:F1MWM0}.
CC -!- PTM: Phosphorylation is independent of light exposure and modulates
CC ATPase activity. {ECO:0000250|UniProtKB:F1MWM0}.
CC -!- DISRUPTION PHENOTYPE: Delayed dark adaptation but normal final rod
CC threshold. {ECO:0000269|PubMed:10412977}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AF000149; AAC23916.1; -; mRNA.
DR EMBL; BC057853; AAH57853.1; -; mRNA.
DR CCDS; CCDS38617.1; -.
DR RefSeq; NP_031404.1; NM_007378.1.
DR AlphaFoldDB; O35600; -.
DR SMR; O35600; -.
DR BioGRID; 197901; 2.
DR STRING; 10090.ENSMUSP00000013995; -.
DR GlyConnect; 2683; 3 N-Linked glycans (1 site).
DR GlyGen; O35600; 8 sites, 3 N-linked glycans (1 site).
DR iPTMnet; O35600; -.
DR PhosphoSitePlus; O35600; -.
DR MaxQB; O35600; -.
DR PaxDb; O35600; -.
DR PRIDE; O35600; -.
DR ProteomicsDB; 285899; -.
DR Antibodypedia; 33661; 192 antibodies from 32 providers.
DR DNASU; 11304; -.
DR Ensembl; ENSMUST00000013995; ENSMUSP00000013995; ENSMUSG00000028125.
DR GeneID; 11304; -.
DR KEGG; mmu:11304; -.
DR UCSC; uc008rel.1; mouse.
DR CTD; 24; -.
DR MGI; MGI:109424; Abca4.
DR VEuPathDB; HostDB:ENSMUSG00000028125; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000155624; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR InParanoid; O35600; -.
DR OMA; DPVYSYD; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; O35600; -.
DR TreeFam; TF105191; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 11304; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Abca4; mouse.
DR PRO; PR:O35600; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35600; protein.
DR Bgee; ENSMUSG00000028125; Expressed in retinal neural layer and 76 other tissues.
DR ExpressionAtlas; O35600; baseline and differential.
DR Genevisible; O35600; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0120202; C:rod photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005503; F:all-trans retinal binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IMP:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140327; F:flippase activity; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0140347; F:N-retinylidene-phosphatidylethanolamine flippase activity; IMP:UniProtKB.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; ISO:MGI.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0005501; F:retinoid binding; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0006649; P:phospholipid transfer to membrane; IMP:MGI.
DR GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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 PANTHER; PTHR19229; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01257; rim_protein; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Sensory transduction; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..2310
FT /note="Retinal-specific phospholipid-transporting ATPase
FT ABCA4"
FT /id="PRO_0000093302"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..646
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..730
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..835
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..1375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1376..1396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1397..1726
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT TRANSMEM 1727..1747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1748..1758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1759..1779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1780..1791
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1792..1812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1813..1830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1831..1851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1852..1872
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1873..1893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1894..2310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 929..1160
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1937..2169
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 891..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2243..2248
FT /note="Essential for ATP binding and ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT REGION 2266..2310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2282..2310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 963..970
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1054
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT BINDING 1971..1979
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 2072..2073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT SITE 1309
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 901
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1MWM0"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..81
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 75..324
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 370..519
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 641..1489
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 1443..1454
FT /evidence="ECO:0000250|UniProtKB:P78363"
FT DISULFID 1487..1501
FT /evidence="ECO:0000250|UniProtKB:P78363"
SQ SEQUENCE 2310 AA; 260209 MW; 8370C6C8A62EF294 CRC64;
MGFLRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS QHECHFPNKA
MPSAGLLPWL QGIFCNMNNP CFQNPTPGES PGTVSNYNNS ILARVYRDFQ ELFMDTPEVQ
HLGQVWAELR TLSQFMDTLR THPERFAGRG LQIRDILKDE EALTLFLMRN IGLSDSVAHL
LVNSQVRVEQ FAYGVPDLEL TDIACSEALL QRFIIFSQRR GAQTVRDALC PLSQVTLQWI
EDTLYADVDF FKLFHVLPTL LDSSSQGINL RFWGGILSDL SPRMQKFIHR PSVQDLLWVS
RPLLQNGGPE TFTQLMSILS DLLCGYPEGG GSRVFSFNWY EDNNYKAFLG IDSTRKDPAY
SYDKRTTSFC NSLIQSLESN PLTKIAWRAA KPLLMGKILF TPDSPAARRI MKNANSTFEE
LDRVRKLVKA WEEVGPQIWY FFEKSTQMTV IRDTLQHPTV KDFINRQLGE EGITTEAVLN
FFSNGPQEKQ ADDMTSFDWR DIFNITDRFL RLANQYLECL VLDKFESYDD EVQLTQRALS
LLEENRFWAG VVFPGMYPWA SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED
FRYIWGGFAY LQDMVEQGIV KSQMQAEPPI GVYLQQMPYP CFVDDSFMII LNRCFPIFMV
LAWIYSVSMT VKGIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMAL SIFLLTLFIM
HGRILHYSDP FILFLFLLAF ATATIMQSFL LSTLFSKASL AAACSGVIYF TLYLPHVLCF
AWQDRMTADL KTTVSLLSSV AFGFGTEYLV RFEEQGLGLQ WSNIGKSPLE GDEFSFLLSM
KMMLLDAALY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL
TEEMEDPEHP EGMNDSFFER ELPGLVPGVC VKNLVKVFEP SGRPAVDRLN ITFYENQITA
FLGHNGAGKT TTLSILTGLL PPTSGTVLIG GKDIETNLDV VRQSLGMCPQ HNILFHHLTV
AEHILFYAQL KGRSWEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDS
KVVVLDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIISQGRLYC
SGTPLFLKNC FGTGFYLTLV RKMKNIQSQR GGCEGVCSCT SKGFSTRCPT RVDEITEEQV
LDGDVQELMD LVYHHVPEAK LVECIGQELI FLLPNKNFKQ RAYASLFREL EETLADLGLS
SFGISDTPLE EIFLKVTEDA GAGSMFVGGA QQKREQAGLR HPCSAPTEKL RQYAQAPHTC
SPGQVDPPKG QPSPEPEDPG VPFNTGARLI LQHVQALLVK RFHHTIRSRK DFVAQIVLPA
TFVFLALMLS IIVPPFGEFP ALTLHPWMYG HQYTFFSMDE PNNEHLEVLA DVLLNRPGFG
NRCLKEEWLP EYPCINATSW KTPSVSPNIT HLFQKQKWTA AHPSPSCKCS TREKLTMLPE
CPEGAGGLPP PQRTQRSTEV LQDLTNRNIS DYLVKTYPAL IRSSLKSKFW VNEQRYGGIS
IGGKLPAIPI SGEALVGFLS GLGQMMNVSG GPVTREASKE MLDFLKHLET TDNIKVWFNN
KGWHALVSFL NVAHNAILRA SLPRDRDPEE YGITVISQPL NLTKEQLSDI TVLTTSVDAV
VAICVIFAMS FVPASFVLYL IQERVTKAKH LQFISGVSPT TYWLTNFLWD IMNYAVSAGL
VVGIFIGFQK KAYTSPDNLP ALVSLLMLYG WAVIPMMYPA SFLFEVPSTA YVALSCANLF
IGINSSAITF VLELFENNRT LLRFNAMLRK LLIVFPHFCL GRGLIDLALS QAVTDVYAQF
GEEYSANPFQ WDLIGKNLVA MAIEGVVYFL LTLLIQHHFF LTRWIAEPAR EPVFDEDDDV
AEERQRVMSG GNKTDILKLN ELTKVYSGSS SPAVDRLCVG VRPGECFGLL GVNGAGKTTT
FKMLTGDTTV TSGDATVAGK SILTSISDVH QNMGYCPQFD AIDDLLTGRE HLYLYARLRG
VPSKEIEKVA NWGIQSLGLS LYADRLAGTY SGGNKRKLST AIALTGCPPL LLLDEPTTGM
DPQARRMLWN TIVSIIREGR AVVLTSHSME ECEALCTRLA IMVKGTFQCL GTIQHLKYKF
GDGYIVTMKI KSPKDDLLPD LNPVEQFFQG NFPGSVQRER HHSMLQFQVP SSSLARIFQL
LISHKDSLLI EEYSVTQTTL DQVFVNFAKQ QTETYDLPLH PRAAGASWQA KLEEKSGRLQ
TQEPLPAGSE QLANGSNPTA AEDKHTRSPQ
