ABCAA_HUMAN
ID ABCAA_HUMAN Reviewed; 1543 AA.
AC Q8WWZ4; C9JZH2; C9K035; Q6PIQ6; Q7Z2I9; Q7Z7P7; Q86TD2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP-binding cassette sub-family A member 10 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:12821155};
GN Name=ABCA10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP SER-203; VAL-287 AND THR-916.
RA Arnould I., Schriml L.M., Prades C., Lachtermacher-Triunfol M.,
RA Schneider T., Maintoux C., Lemoine C., Debono D., Devaud C., Naudin L.,
RA Bauche S., Annat M., Annilo T., Allikmets R., Gold B., Denefle P.,
RA Rosier M., Dean M.;
RT "Identifying and characterizing a five-gene cluster of ATP-binding cassette
RT transporters mapping to human chromosome 17q24: a new subgroup within the
RT ABCA subfamily.";
RL GeneScreen 1:157-164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS SER-203 AND
RP VAL-287, ALTERNATIVE SPLICING (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY,
RP INDUCTION, AND FUNCTION.
RC TISSUE=Macrophage;
RX PubMed=12821155; DOI=10.1016/s0006-291x(03)01097-0;
RA Wenzel J.J., Kaminski W.E., Piehler A., Heimerl S., Langmann T.,
RA Schmitz G.;
RT "ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter.";
RL Biochem. Biophys. Res. Commun. 306:1089-1098(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANTS SER-203
RP AND VAL-287.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1125-1543 (ISOFORMS 1/2).
RC TISSUE=Liver, and Pancreatic carcinoma;
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).
CC -!- FUNCTION: Probable transporter which may play a role in macrophage
CC lipid transport and homeostasis. {ECO:0000305|PubMed:12821155}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8WWZ4-1; Sequence=Displayed;
CC Name=2; Synonyms=ABCA10delta+82;
CC IsoId=Q8WWZ4-2; Sequence=VSP_021061;
CC Name=3; Synonyms=ABCA10delta-104;
CC IsoId=Q8WWZ4-3; Sequence=VSP_021062, VSP_021063;
CC Name=4; Synonyms=ABCA10delta-176;
CC IsoId=Q8WWZ4-4; Sequence=VSP_021065, VSP_021066;
CC Name=5;
CC IsoId=Q8WWZ4-5; Sequence=VSP_021064, VSP_021067;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal
CC muscle, heart, brain and gastrointestinal tract.
CC {ECO:0000269|PubMed:12821155, ECO:0000269|Ref.1}.
CC -!- INDUCTION: Down-regulated by cholesterol loading of macrophages.
CC {ECO:0000269|PubMed:12821155}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AY028900; AAK30025.1; -; mRNA.
DR EMBL; AY247065; AAO72161.1; -; mRNA.
DR EMBL; AY247105; AAO72160.1; -; Genomic_DNA.
DR EMBL; AY247069; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247070; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247071; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247072; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247073; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247074; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247075; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247076; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247077; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247078; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247079; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247080; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247081; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247082; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247083; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247084; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247085; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247086; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247087; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247088; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247089; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247090; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247091; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247092; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247093; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247094; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247095; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247096; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247097; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247098; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247099; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247100; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247101; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247102; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247103; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AY247104; AAO72160.1; JOINED; Genomic_DNA.
DR EMBL; AL832004; CAD89903.1; -; mRNA.
DR EMBL; AC005495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031026; AAH31026.1; -; mRNA.
DR EMBL; BC051320; AAH51320.1; -; mRNA.
DR CCDS; CCDS11684.1; -. [Q8WWZ4-1]
DR RefSeq; NP_525021.3; NM_080282.3. [Q8WWZ4-1]
DR AlphaFoldDB; Q8WWZ4; -.
DR SMR; Q8WWZ4; -.
DR BioGRID; 115630; 5.
DR IntAct; Q8WWZ4; 2.
DR STRING; 9606.ENSP00000269081; -.
DR TCDB; 3.A.1.211.17; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q8WWZ4; -.
DR PhosphoSitePlus; Q8WWZ4; -.
DR BioMuta; ABCA10; -.
DR DMDM; 296439455; -.
DR EPD; Q8WWZ4; -.
DR jPOST; Q8WWZ4; -.
DR MassIVE; Q8WWZ4; -.
DR PaxDb; Q8WWZ4; -.
DR PeptideAtlas; Q8WWZ4; -.
DR PRIDE; Q8WWZ4; -.
DR ProteomicsDB; 74965; -. [Q8WWZ4-1]
DR ProteomicsDB; 74966; -. [Q8WWZ4-2]
DR Antibodypedia; 2899; 48 antibodies from 17 providers.
DR DNASU; 10349; -.
DR Ensembl; ENST00000269081.8; ENSP00000269081.4; ENSG00000154263.18. [Q8WWZ4-1]
DR Ensembl; ENST00000522406.5; ENSP00000429853.1; ENSG00000154263.18. [Q8WWZ4-5]
DR Ensembl; ENST00000523512.5; ENSP00000429945.1; ENSG00000154263.18. [Q8WWZ4-3]
DR Ensembl; ENST00000690296.1; ENSP00000509702.1; ENSG00000154263.18. [Q8WWZ4-1]
DR GeneID; 10349; -.
DR KEGG; hsa:10349; -.
DR MANE-Select; ENST00000690296.1; ENSP00000509702.1; NM_001377321.1; NP_001364250.1.
DR UCSC; uc010dfa.2; human. [Q8WWZ4-1]
DR CTD; 10349; -.
DR DisGeNET; 10349; -.
DR GeneCards; ABCA10; -.
DR HGNC; HGNC:30; ABCA10.
DR HPA; ENSG00000154263; Tissue enhanced (ovary).
DR MIM; 612508; gene.
DR neXtProt; NX_Q8WWZ4; -.
DR OpenTargets; ENSG00000154263; -.
DR PharmGKB; PA24374; -.
DR VEuPathDB; HostDB:ENSG00000154263; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162673; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8WWZ4; -.
DR OMA; SDQGIMN; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8WWZ4; -.
DR TreeFam; TF105192; -.
DR PathwayCommons; Q8WWZ4; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR SignaLink; Q8WWZ4; -.
DR BioGRID-ORCS; 10349; 12 hits in 1064 CRISPR screens.
DR ChiTaRS; ABCA10; human.
DR GenomeRNAi; 10349; -.
DR Pharos; Q8WWZ4; Tdark.
DR PRO; PR:Q8WWZ4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WWZ4; protein.
DR Bgee; ENSG00000154263; Expressed in tibial nerve and 95 other tissues.
DR ExpressionAtlas; Q8WWZ4; baseline and differential.
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: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:0006869; P:lipid transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1543
FT /note="ATP-binding cassette sub-family A member 10"
FT /id="PRO_0000253572"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1113..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 391..626
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1206..1440
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1153..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1239..1246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021061"
FT VAR_SEQ 67
FT /note="E -> GHNKSFCNGGVDISYWNKYEDTTFHF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021062"
FT VAR_SEQ 68..1543
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021063"
FT VAR_SEQ 413..452
FT /note="IFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAT -> SEERLCPA
FT AHRLRCGERLCPAAHHLGCEERPCPAATPSGN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021064"
FT VAR_SEQ 450
FT /note="S -> KKNYNGIRHAKHSRHYC (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_021065"
FT VAR_SEQ 451..1543
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_021066"
FT VAR_SEQ 453..1543
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021067"
FT VARIANT 203
FT /note="P -> S (in dbSNP:rs9909216)"
FT /evidence="ECO:0000269|PubMed:12821155,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1"
FT /id="VAR_028384"
FT VARIANT 287
FT /note="I -> V (in dbSNP:rs11657804)"
FT /evidence="ECO:0000269|PubMed:12821155,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.1"
FT /id="VAR_028385"
FT VARIANT 916
FT /note="M -> T (in dbSNP:rs4968849)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_028386"
FT VARIANT 1322
FT /note="R -> W (in dbSNP:rs10491178)"
FT /id="VAR_055469"
FT CONFLICT 140
FT /note="C -> Y (in Ref. 3; CAD89903)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> G (in Ref. 3; CAD89903)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="F -> S (in Ref. 3; CAD89903)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="L -> S (in Ref. 3; CAD89903)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="F -> L (in Ref. 3; CAD89903)"
FT /evidence="ECO:0000305"
FT CONFLICT 1216
FT /note="R -> I (in Ref. 2; AAO72160/AAO72161 and 4;
FT AAH51320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1543 AA; 175790 MW; 47E932434314B538 CRC64;
MNKMALASFM KGRTVIGTPD EETMDIELPK KYHEMVGVIF SDTFSYRLKF NWGYRIPVIK
EHSEYTEHCW AMHGEIFCYL AKYWLKGFVA FQAAINAAII EVTTNHSVME ELTSVIGINM
KIPPFISKGE IMNEWFHFTC LVSFSSFIYF ASLNVARERG KFKKLMTVMG LRESAFWLSW
GLTYICFIFI MSIFMALVIT SIPIVFHTGF MVIFTLYSLY GLSLIALAFL MSVLIRKPML
AGLAGFLFTV FWGCLGFTVL YRQLPLSLGW VLSLLSPFAF TAGMAQITHL DNYLSGVIFP
DPSGDSYKMI ATFFILAFDT LFYLIFTLYF ERVLPDKDGH GDSPLFFLKS SFWSKHQNTH
HEIFENEINP EHSSDDSFEP VSPEFHGKEA IRIRNVIKEY NGKTGKVEAL QGIFFDIYEG
QITAILGHNG AGKSTLLNIL SGLSVSTEGS ATIYNTQLSE ITDMEEIRKN IGFCPQFNFQ
FDFLTVRENL RVFAKIKGIQ PKEVEQEVKR IIMELDMQSI QDIIAKKLSG GQKRKLTLGI
AILGDPQVLL LDEPTAGLDP FSRHRVWSLL KEHKVDRLIL FSTQFMDEAD ILADRKVFLS
NGKLKCAGSS LFLKRKWGIG YHLSLHRNEM CDTEKITSLI KQHIPDAKLT TESEEKLVYS
LPLEKTNKFP DLYSDLDKCS DQGIRNYAVS VTSLNEVFLN LEGKSAIDEP DFDIGKQEKI
HVTRNTGDES EMEQVLCSLP ETRKAVSSAA LWRRQIYAVA TLRFLKLRRE RRALLCLLLV
LGIAFIPIIL EKIMYKVTRE THCWEFSPSM YFLSLEQIPK TPLTSLLIVN NTGSNIEDLV
HSLKCQDIVL EIDDFRNRNG SDDPSYNGAI IVSGDQKDYR FSVACNTKKL NCFPVLMGIV
SNALMGIFNF TELIQMESTS FSRDDIVLDL GFIDGSIFLL LITNCVSPFI GMSSISDYKK
NVQSQLWISG LWPSAYWCGQ ALVDIPLYFL ILFSIHLIYY FIFLGFQLSW ELMFVLVVCI
IGCAVSLIFL TYVLSFIFRK WRKNNGFWSF GFFIILICVS TIMVSTQYEK LNLILCMIFI
PSFTLLGYVM LLIQLDFMRN LDSLDNRINE VNKTILLTTL IPYLQSVIFL FVIRCLEMKY
GNEIMNKDPV FRISPRSRET HPNPEEPEEE DEDVQAERVQ AANALTAPNL EEEPVITASC
LHKEYYETKK SCFSTRKKKI AIRNVSFCVK KGEVLGLLGH NGAGKSTSIK MITGCTKPTA
GVVVLQGSRA SVRQQHDNSL KFLGYCPQEN SLWPKLTMKE HLELYAAVKG LGKEDAALSI
SRLVEALKLQ EQLKAPVKTL SEGIKRKLCF VLSILGNPSV VLLDEPFTGM DPEGQQQMWQ
ILQATVKNKE RGTLLTTHYM SEAEAVCDRM AMMVSGTLRC IGSIQHLKNK FGRDYLLEIK
MKEPTQVEAL HTEILKLFPQ AAWQERYSSL MAYKLPVEDV HPLSRAFFKL EAMKQTFNLE
EYSLSQATLE QVFLELCKEQ ELGNVDDKID TTVEWKLLPQ EDP
