ABCAD_MOUSE
ID ABCAD_MOUSE Reviewed; 5034 AA.
AC Q5SSE9; Q80T20; Q8BHZ2; Q8CB91;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ATP-binding cassette sub-family A member 13 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000269|PubMed:33478937};
GN Name=Abca13 {ECO:0000312|MGI:MGI:2388707};
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4798-5034 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2887-5034 (ISOFORM 1), ALTERNATIVE SPLICING
RP (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=12706902; DOI=10.1016/s0378-1119(03)00465-7;
RA Barros S.A., Tennant R.W., Cannon R.E.;
RT "Molecular structure and characterization of a novel murine ABC
RT transporter, Abca13.";
RL Gene 307:191-200(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12697998; DOI=10.1159/000069852;
RA Prades C., Arnould I., Annilo T., Shulenin S., Chen Z.-Q., Orosco L.,
RA Triunfol M., Devaud C., Maintoux-Larois C., Lafargue C., Lemoine C.,
RA Denefle P., Rosier M., Dean M.;
RT "The human ATP binding cassette gene ABCA13, located on chromosome 7p12.3,
RT encodes a 5058 amino acid protein with an extracellular domain encoded in
RT part by a 4.8-kb conserved exon.";
RL Cytogenet. Genome Res. 98:160-168(2002).
RN [5]
RP SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF HIS-3577; LYS-3849;
RP THR-3999; LYS-4735 AND ARG-4818, AND DISRUPTION PHENOTYPE.
RX PubMed=33478937; DOI=10.1074/jbc.ra120.015997;
RA Nakato M., Shiranaga N., Tomioka M., Watanabe H., Kurisu J., Kengaku M.,
RA Komura N., Ando H., Kimura Y., Kioka N., Ueda K.;
RT "ABCA13 dysfunction associated with psychiatric disorders causes impaired
RT cholesterol trafficking.";
RL J. Biol. Chem. 296:100166-100177(2021).
CC -!- FUNCTION: May mediate the cholesterol and gangliosides transport from
CC the plasma membrane to intracellular vesicles in an ATP hydrolysis
CC dependent manner, thus playing a role in their internalization by
CC endocytic retrograde transport and may also participate in the
CC endocytosis of synaptic vesicle in cortical neurons.
CC {ECO:0000269|PubMed:33478937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:33478937};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:33478937}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SSE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSE9-2; Sequence=VSP_021073, VSP_021074;
CC Name=3;
CC IsoId=Q5SSE9-3; Sequence=VSP_021071, VSP_021072;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. May be primarily expressed
CC in kidney. {ECO:0000269|PubMed:12697998, ECO:0000269|PubMed:12706902}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for Abca13 are born
CC normally and seem to have normal appearance and life span but show
CC sensorimotor gating deficits. {ECO:0000269|PubMed:33478937}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO18684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK036546; BAC29471.1; -; mRNA.
DR EMBL; AK044229; BAC31829.1; -; mRNA.
DR EMBL; AL645994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY160971; AAO18684.1; ALT_INIT; mRNA.
DR CCDS; CCDS36110.1; -. [Q5SSE9-1]
DR RefSeq; NP_839990.2; NM_178259.3. [Q5SSE9-1]
DR SMR; Q5SSE9; -.
DR BioGRID; 234489; 9.
DR STRING; 10090.ENSMUSP00000040465; -.
DR iPTMnet; Q5SSE9; -.
DR PhosphoSitePlus; Q5SSE9; -.
DR jPOST; Q5SSE9; -.
DR PaxDb; Q5SSE9; -.
DR PeptideAtlas; Q5SSE9; -.
DR PRIDE; Q5SSE9; -.
DR ProteomicsDB; 286042; -. [Q5SSE9-1]
DR ProteomicsDB; 286043; -. [Q5SSE9-2]
DR ProteomicsDB; 286044; -. [Q5SSE9-3]
DR Antibodypedia; 51819; 72 antibodies from 15 providers.
DR Ensembl; ENSMUST00000042740; ENSMUSP00000040465; ENSMUSG00000004668. [Q5SSE9-1]
DR GeneID; 268379; -.
DR KEGG; mmu:268379; -.
DR UCSC; uc007hzz.1; mouse. [Q5SSE9-3]
DR UCSC; uc007iaa.1; mouse. [Q5SSE9-1]
DR CTD; 154664; -.
DR MGI; MGI:2388707; Abca13.
DR VEuPathDB; HostDB:ENSMUSG00000004668; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000161703; -.
DR HOGENOM; CLU_000074_0_0_1; -.
DR InParanoid; Q5SSE9; -.
DR OMA; IHELVDW; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q5SSE9; -.
DR TreeFam; TF105191; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 268379; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Abca13; mouse.
DR PRO; PR:Q5SSE9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSE9; protein.
DR Bgee; ENSMUSG00000004668; Expressed in olfactory epithelium and 38 other tissues.
DR ExpressionAtlas; Q5SSE9; baseline and differential.
DR Genevisible; Q5SSE9; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0097708; C:intracellular vesicle; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0035627; P:ceramide transport; IDA:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:UniProtKB.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:UniProtKB.
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; 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 PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasmic vesicle; Lipid transport;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..5034
FT /note="ATP-binding cassette sub-family A member 13"
FT /id="PRO_0000253574"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3536..3556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3590..3610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3616..3636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3647..3667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3677..3697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3720..3740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4206..4226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4432..4452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4478..4498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4510..4530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4540..4560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4581..4601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4625..4645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3810..4042
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 4692..4931
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 4135..4165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3843..3850
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 4729..4736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT VAR_SEQ 97..107
FT /note="LSRFQTASDDR -> YEKYKHPFQNS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021071"
FT VAR_SEQ 108..5034
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021072"
FT VAR_SEQ 3340..3342
FT /note="DAL -> DGC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021073"
FT VAR_SEQ 3343..5034
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021074"
FT MUTAGEN 3577
FT /note="H->P: Does not affect protein expression. Decreases
FT intracellular cholesterol accumulation in the vesicle."
FT /evidence="ECO:0000269|PubMed:33478937"
FT MUTAGEN 3849
FT /note="K->M: Does not affect intracellular vesicle
FT localization. Affects cholesterol internalization."
FT /evidence="ECO:0000269|PubMed:33478937"
FT MUTAGEN 3999
FT /note="T->A: Does not affect protein expression. Affects
FT intracellular vesicles localization. Impairs intracellular
FT cholesterol accumulation in the vesicle."
FT /evidence="ECO:0000269|PubMed:33478937"
FT MUTAGEN 4735
FT /note="K->M: Does not affect intracellular vesicle
FT localization.Affects cholesterol internalization."
FT /evidence="ECO:0000269|PubMed:33478937"
FT MUTAGEN 4818
FT /note="R->C: Does not affect protein expression. Decreases
FT intracellular cholesterol accumulation in the vesicle."
FT /evidence="ECO:0000269|PubMed:33478937"
FT CONFLICT 3048
FT /note="F -> L (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3099
FT /note="T -> M (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3166
FT /note="A -> T (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3199
FT /note="K -> N (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3238
FT /note="N -> T (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3368
FT /note="T -> I (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 3917
FT /note="T -> K (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4024
FT /note="A -> T (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4076
FT /note="C -> S (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4490
FT /note="C -> W (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4495
FT /note="V -> G (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4498
FT /note="A -> T (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4517
FT /note="L -> V (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4649
FT /note="L -> V (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4670
FT /note="A -> V (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4700
FT /note="S -> R (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
FT CONFLICT 4798
FT /note="C -> G (in Ref. 1; BAC31829)"
FT /evidence="ECO:0000305"
FT CONFLICT 4885
FT /note="V -> M (in Ref. 3; AAO18684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5034 AA; 568897 MW; 23D41658044635AF CRC64;
MGHAGRQFQA LLWKNWICRL RHPVLSLAEF FWPCILFMIL TVLRFQEPPR HRENCYLQAR
DLPSRGVLPF VQGLLCNTGS SCRNISFESS MDHHFRLSRF QTASDDRKVS SLAFLNEIQD
LAEDIFETMD KAKNLQKLWL KRSETPGSSY GSGFLTMDLN KTEDVISKLE SLHQQPHIWD
FLHSLPRLYM SSAHLEDSMG AVTHFLQAGL NSLASLGDLD WLPLHQTIPQ VSRHVLNVTI
STLRFLQQHS AVVNETIYHL SLKNIVWDPQ KVQSDLKSQF GFNDFQMQHI LNYSAKLEEI
PTHSFLERMV CSILSNTSED EAESKGYRAD CHPKWSAVKN YIIHAVSWLK LYGQVFDQWQ
QGSLLQSLLA GASHSLAALR EQFKQQSESW KVVEALHTAL LILNDSLAAD VPRDYHLFPQ
IFQHLSKLQH ALSDLSPWPA LKRLLLLDTV LRNMIAQDLR FVQEFLSYLE RSAKDFIPAG
SEGWRLEKDV LFQGLNQLLT KNASALCLNG HLSQEAALPT GNSSIWRSVW GVLCHTLFFN
ETSVLNELLR AVKDAGHSLQ AVIAGHTNGS VSEHGGHFGW QDLGTQLSEI SLTCSRVFQL
PRADTSPENS FSPGGCESQL VSIVVSHILE DVQMSTQKKS YWKILSKIVR KTCELARYVN
MNGSLQNSGL ISFSEDSPCY TQDMNWKVII DNYFVFFNNF KKSPITSITT AFNFTKHLLV
VDQKLHTLEN GQMNILLSFV EFVEKLLSNP SGSFPAPEFD NLSSLTELVF NATVSWLTHL
KRLKADSHDA APQELLEFDH LVTEKIQRLK NHWMKKGSKN ILNFLELILL EMNSELQEFR
LNGIPQEERT NIEGFSTLVN FSVAEYEKIL CKRFTFSQLF HSYWPKSPAI NADFIHLSET
IIQSLCGLSF LTQEQVSIAL NTVSALQNTS ELFSALSEPQ KQELDNFLTH VYINVFKDKN
IALFLQTYSS FYRYIHKFFN IQNREPLIAY FTQISRHILD LIKQFNIQNI REALSFLSET
TEALGMISEV SHCQQLLSIF NFLELQAWSL MARGGPAEAV IHASLTGLKQ LFAADEGFRV
SLLQYVTQCF NGSAATLVAS ECFIQENATI SSVNYSGNEG SSLPFPWTQF FSNLSVNGSA
ISEFTAIHCT LSWIQTWAEI WRSIAQIFKL ELSIFTPLHV GITQLLDDLG NYGNISKDCQ
GIVPTYLTAR LILNLFRNIT QENNFHDWDG LQDLRDLWVA FGNELTTVQS LNLDQVEKTF
ITMETSLHQL KTFPMKINAS REFLYSLFDV FIELSKASDY VDRNVELINN FLSDDLPDHQ
AKFASIIKEL KETILFLRHV SQGRTLSACA DIFQRLTELI FEDSLLLVNT SNKPEHILAM
LSSMFSSKNT SSSLEGCITW IDIINHLCIM YNSSSLPSHS YNILGSFKDM GDKMSSALNI
LTWMLNKKRP ICPWNESNIN CVNIYLKDIT DFLNIIVTTG LEKENVPNVE ILLSLFNDST
KQVDMIITNL TEDLNVASQS NWKHFKDLLL RPTEMSDDIP DQFQNIWQHI IALGKEMQKL
LKGIFHSVLG NNFSSNTETM FSVFSTSPKE GDISHLGKSI YNLANYFALN LTHNLQNSSE
VFPHEILKAV DLSIQLTRDV FNFLMPAVHF NIPQNSDHAQ TLKKVTSLMQ SLKKADIELL
VGQLGENSEI LMSFFKNLSR SGIDNLGVNM LVGLVEKFVD SSHSWSVSHL LRLSRLLPKD
VVDTVLDVYY ALPHIVGLLR RIVDKNITES LRDVYNFTLL HGITMFKITK EDFADVVKTL
LDAVELVSDE PAIVPEALMC LTRVWCANYT TFRLEKNPKV EDCNIQRHMP SSFFHMVTSL
LDLLHLPPPS DSQCIGEKYA VEITRRLACA VHDLADWNSI LSELLEIFHV KNLLVKTLQG
FWHKVLLFMS SSGIQGNGSI PELCPTSTIK QGALQIIEKL KYVNFTKFSL GETILDRLGN
LDRILSLTKG TEKSVQNNIY LNLERLFKLI SATWTLRNST HYLLSPITNF LNGNYTGWSL
FKNNRTSSNI EELWLDFKQI PKDLTSNWSL GQLLSDINKN IQGAGLQNTT VQLPQLLELL
DSSPLKTSEI IEGFLFLIKP WLREYENGDF FRFIQSLLNA VASGNSTDVS RLARDFTMYL
GYLRNQSREG NFDVGFFSHM LDQEHLTDLP VVQRLLESIV MNSVSSFAAL SQETPPSFSG
TNLQIADLMN LILKHAQSKN HAEAEGSTED FLKQLPETFF SSVINGLHSD VTAEVSFVPR
DKILEILKLD PFLTWMNKNP LMNIFSGLKT LYYLIKSSFS LDNRELSGVL KDLSHTHPWE
TTVKTDAEGH LDFFSVVTQF LSQVNSSEDL SKFNQNLRSV LYLVQESSTE MATIIDTVLH
STSGACYSPY PMLQHSTVAK LSDLFSDVNS SFPLRSREIL ESTMRLFGTI SQVGEESHVL
ESALEIFRTL TMLVNSTVEL GHLASTADSM VRLLNLAKIV SRKMATMLGT LSISSTEDSG
KFLDTLYSFM LQSVPHHVKQ ITTLKKGDPF IVEKTKDLLI PFLDLAFGMI GVTPNVSQDS
DVFSMPFSIL SYINQSRDFS ETLEGMAENL ISIKISLRDW EHFVAMIKNR TQNFSIDAAD
LWEEILGCLV PISNITTQMD FLKLYELSST SHPQVPKQER THDVIRYLDG MLTDNGTERE
TFLKMVIDLT LQALWNGLKE DNWDIFNLLL AFAQHPNDLL KAIESVVAVS SGIHSDYPDD
FNQDSFSDLS LIQNTTRYQL AKAVLIGLGK AGFSREGLPL NNTQWTHFTR TLFHPDYNSF
PNSTPHQNVT SAKDGRTKDE MMVILHGSEP MPYLQRFLKA LFVSIEHWQE VPQAEQSVFE
MCQVFQQLQK PMKTVKMLQR VEMMALRVLI IFAENPSLTK DILCAALSCK QGAMRHLILA
ALQGVTLVHR HYQEIGKIWF SPDQLDCERL SRNLSSALEG FKSILDNASS HRCTCQPLVG
VVQQHIRRLT KSLEEVWMSK IPAMTFLSNF TVTEDVKIKD LMRNITKFTE DLRSFFHISE
ETIHSILEAN ISHSKVLSSV LTIALSGKCD EEILHLLLTF PESEKSWFVT RELCSLPGSQ
VFSLLVMMGQ NLNLRNLIYK TLIPSEANGL LKSLLDVVAS LSSILARAQH ALEYLPEFLH
TFKITALLDM PDFQQVSSKG QTRSSAFASF QSVMKLLCKD QESFLSNSNM FINLPRVNEL
LEDNKEKFNI PHDSTPFCLK LYQEILQSPN GALVWSFLKP VLHGKILYTP NSPEINEVIQ
KANYTFYFVD KIKVLSETFL KISKLFQGSG NGQMFNQLQD ALRNKFIRNF VESQLHIDMD
KLTEDLQTYG RMLDKMFNHV EAGHFRFLGG MLANLSSCVV LDRFQAVETV DTLETKAHEL
MQQNSFLASI IFNSSLRHRH IRSAPHKLPP HVTYTIRTNV LYSMRTDMIK NPSWKFHPQN
LPAGGFKYNY IFVPLQDMIE RAIIVVQTGQ ESLEPTTQAQ AAPYPCHTSD LFLNNVGFFF
PLIMMLTWMV AVASMVRKLV YEREIQIEEY MRMMGLHPTI HFLSWFLENM ATLALSSAAL
AVILKMSGIF MHSDAFIIFL YLLDFGVSAV MMSYFLSVFF NQANTAALCT SLGYMISFLP
YVVLLVLHNQ LSFAIQTLLC LLSTTAFGQG VFFITFLEGQ EEGIQWGNMY RAPEPGGMTF
GWVCWMILFD AILYFLGGWY FSNLVPGTFG LGKPWYFPFT ASYWKSICGL MERRRCSLSS
GLFFFNEDFG NKGLSQQNGP GEMEGGNPGV ALISVTKEYE DHKVAVQELT LTFHRDQITA
LLGTNGAGKT TIISMLMGLF PPTSGTITIN GKNLQTDLSK VREELGVCPQ QDVLLDNLTV
REHLMLFASI KAPWWTTKEL QQQVNKTLDE VELTQHQHKP AGVLSGGMKR KLSIGIAFMG
MSKTVVLDEP SSGVDPCSRR SLWDILLKYR EGRTIIFTTH HLDEAEMLSD HVAVLQQGRL
RCYAPPADLK ETYGQGLTLT LSKQPSILET QEPKDVARVT SLIQIYIPQA FLKDSCGGEL
TYTIPKDADR TCFKGLCQAL DQNLQHLHLT GYGISDTTLE EVFLMLLQDT NKKSYITPDN
KVEPQNERPV GPLSPHNVSP LSTPPEGALP EPIGGCQLLL GQAVALLRKR LLHTLRAWKS
TTSDLLLPVL FVALAMGLFM VQPLAITYPP LKLTPGHYET AETYFFSSGN HGPDLTHVLL
RKFRDQDPVC ADAFRMNSSS WHRDPYSGPE SQDSCGCLKC PNKSAGAPSL TNCLGHTLLN
LSGYDVEEYL LVPSAKPRLG GWSFGGQIPN DAEDVKTNTS KPRTLAKVWY NQKGFHSLPS
YLNHLNNLIL WHHLPANAVD WRQYGITLYS HPYGGALLNE DRILESIRQC GVALCIVLGF
SILSASIGSS VVRDRVTGAK RLQHISGLGH RTYWLINFLY DMLFYLVSVC LCVAVIGAFQ
LTAFTFRENL AATALLLALF GYAMIPWMYL MSRIFSSSDV AFISYISLNF IFGLCTMLMT
TMPRLLAIIS KAQNLQKIYN VLKWAFTIFP QFCLGQGLIE LCYNQIKYDL THNFGIDSYV
SPFEMNFLGW IFVELTLQGT FLLLLRLMLH GDLLRWPRDH SVLQDIVKPA KDIDVETEQM
RVLEGRTGGD MMVLCNLSKS YRSVFGGKTT AVHGISLGIP RGECFGLLGV NGAGKSTTFK
ILNGETPPSS GYTVIRTPQG DMVDLASAGK AGILIGYCPQ QDALDELLTG WEHLQYYCRL
RGIPKQYIPE VAADLVRRLH LESHVDKPVA TYSGGTRRKL STALALVGKP DILLLDEPSS
GMDPCSKRYL WQTITQEVRD GCAAVLTSHS MEECEALCTR LAIMVDGSFR CLGPPQHIKN
RFGDGYTVKV WLHKEGSQPS AVSDCLKLHF PGIQFKGQRL NLLEYHVQKS WECLADLFKV
LENNKSLLNI EHYSISQTTL EQVFVNFATE QLQTPCFPVD SPSTDAQHPC YTRI
