ID ABCA9_HUMAN Reviewed; 1624 AA. AC Q8IUA7; Q6P655; Q8N2S4; Q8WWZ5; Q96MD8; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=ATP-binding cassette sub-family A member 9 {ECO:0000305}; DE EC=7.6.2.- {ECO:0000305|PubMed:12150964}; GN Name=ABCA9; 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), VARIANTS HIS-353 AND THR-1306, AND RP TISSUE SPECIFICITY. 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), ALTERNATIVE SPLICING RP (ISOFORMS 2; 3 AND 4), FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE. RC TISSUE=Macrophage; RX PubMed=12150964; DOI=10.1016/s0006-291x(02)00659-9; RA Piehler A., Kaminski W.E., Wenzel J.J., Langmann T., Schmitz G.; RT "Molecular structure of a novel cholesterol-responsive A subclass ABC RT transporter, ABCA9."; RL Biochem. Biophys. Res. Commun. 295:408-416(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-856 (ISOFORM 1), AND VARIANT RP HIS-353. RC TISSUE=Embryo, and Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-949. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). CC -!- FUNCTION: Transporter that may play a role in monocyte differentiation CC and lipid transport and homeostasis. {ECO:0000305|PubMed:12150964}. 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=Q8IUA7-1; Sequence=Displayed; CC Name=2; Synonyms=ABCA9delta+55; CC IsoId=Q8IUA7-2; Sequence=VSP_020705; CC Name=3; Synonyms=ABCA9delta+73; CC IsoId=Q8IUA7-3; Sequence=VSP_020707, VSP_020709; CC Name=4; Synonyms=ABCA9delta-95; CC IsoId=Q8IUA7-4; Sequence=VSP_020708, VSP_020709; CC Name=5; CC IsoId=Q8IUA7-5; Sequence=VSP_020706; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart. CC {ECO:0000269|Ref.1}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues with higher expression CC in fetal heart and kidney. {ECO:0000269|PubMed:12150964}. CC -!- INDUCTION: Up-regulated during monocyte differentiation into CC macrophages. Down-regulated by cholesterol loading of macrophages. CC {ECO:0000269|PubMed:12150964}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH62472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC11021.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY028899; AAK30024.1; -; mRNA. DR EMBL; AF423307; AAN32751.1; -; mRNA. DR EMBL; AF423346; AAN32752.1; -; Genomic_DNA. DR EMBL; AF423308; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423309; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423310; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423311; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423312; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423313; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423314; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423315; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423316; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423317; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423318; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423320; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423321; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423322; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423323; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423324; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423325; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423326; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423327; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423328; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423329; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423330; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423331; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423332; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423333; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423334; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423335; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423336; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423337; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423338; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423339; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423340; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423341; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423342; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423343; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423344; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; AF423345; AAN32752.1; JOINED; Genomic_DNA. DR EMBL; BC062472; AAH62472.1; ALT_INIT; mRNA. DR EMBL; AK057068; BAB71359.1; -; mRNA. DR EMBL; AK074491; BAC11021.1; ALT_INIT; mRNA. DR CCDS; CCDS11681.1; -. [Q8IUA7-1] DR RefSeq; NP_525022.2; NM_080283.3. [Q8IUA7-1] DR AlphaFoldDB; Q8IUA7; -. DR SMR; Q8IUA7; -. DR BioGRID; 115631; 7. DR IntAct; Q8IUA7; 3. DR STRING; 9606.ENSP00000342216; -. DR TCDB; 3.A.1.211.16; the atp-binding cassette (abc) superfamily. DR GlyCosmos; Q8IUA7; 3 sites, No reported glycans. DR GlyGen; Q8IUA7; 3 sites. DR iPTMnet; Q8IUA7; -. DR PhosphoSitePlus; Q8IUA7; -. DR SwissPalm; Q8IUA7; -. DR BioMuta; ABCA9; -. DR DMDM; 74762471; -. DR jPOST; Q8IUA7; -. DR MassIVE; Q8IUA7; -. DR PaxDb; 9606-ENSP00000342216; -. DR PeptideAtlas; Q8IUA7; -. DR ProteomicsDB; 70529; -. [Q8IUA7-1] DR ProteomicsDB; 70531; -. [Q8IUA7-3] DR ProteomicsDB; 70532; -. [Q8IUA7-4] DR Antibodypedia; 31822; 203 antibodies from 31 providers. DR DNASU; 10350; -. DR Ensembl; ENST00000340001.9; ENSP00000342216.3; ENSG00000154258.17. [Q8IUA7-1] DR Ensembl; ENST00000495634.5; ENSP00000465601.1; ENSG00000154258.17. [Q8IUA7-5] DR GeneID; 10350; -. DR KEGG; hsa:10350; -. DR MANE-Select; ENST00000340001.9; ENSP00000342216.3; NM_080283.4; NP_525022.2. DR UCSC; uc002jhu.4; human. [Q8IUA7-1] DR AGR; HGNC:39; -. DR CTD; 10350; -. DR DisGeNET; 10350; -. DR GeneCards; ABCA9; -. DR HGNC; HGNC:39; ABCA9. DR HPA; ENSG00000154258; Low tissue specificity. DR MIM; 612507; gene. DR neXtProt; NX_Q8IUA7; -. DR OpenTargets; ENSG00000154258; -. DR PharmGKB; PA24384; -. DR VEuPathDB; HostDB:ENSG00000154258; -. DR eggNOG; KOG0059; Eukaryota. DR GeneTree; ENSGT00940000162444; -. DR HOGENOM; CLU_054320_0_0_1; -. DR InParanoid; Q8IUA7; -. DR OMA; FTTGMAQ; -. DR OrthoDB; 6951at2759; -. DR PhylomeDB; Q8IUA7; -. DR TreeFam; TF105192; -. DR PathwayCommons; Q8IUA7; -. DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis. DR SignaLink; Q8IUA7; -. DR BioGRID-ORCS; 10350; 6 hits in 1150 CRISPR screens. DR ChiTaRS; ABCA9; human. DR GeneWiki; ABCA9; -. DR GenomeRNAi; 10350; -. DR Pharos; Q8IUA7; Tbio. DR PRO; PR:Q8IUA7; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8IUA7; Protein. DR Bgee; ENSG00000154258; Expressed in mucosa of stomach and 160 other cell types or tissues. DR ExpressionAtlas; Q8IUA7; baseline and differential. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. 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 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 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; IPR026082; ABCA. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR19229:SF120; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 9; 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; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; Q8IUA7; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Glycoprotein; Membrane; KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1624 FT /note="ATP-binding cassette sub-family A member 9" FT /id="PRO_0000250680" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 221..243 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 300..320 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 329..349 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 354..374 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 398..418 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 864..884 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1026..1046 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1065..1085 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1108..1128 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1136..1156 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1163..1183 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1200..1220 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 481..716 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 1288..1521 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 517..524 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 1326..1333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 195 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 949 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 267..1624 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_020705" FT VAR_SEQ 268..1624 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020706" FT VAR_SEQ 1429 FT /note="L -> VRAGLVVALQVP (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_020707" FT VAR_SEQ 1429 FT /note="L -> AGDSGHL (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_020708" FT VAR_SEQ 1430..1624 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_020709" FT VARIANT 353 FT /note="R -> H (in dbSNP:rs1860447)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1" FT /id="VAR_027594" FT VARIANT 785 FT /note="N -> S (in dbSNP:rs17684521)" FT /id="VAR_027595" FT VARIANT 1306 FT /note="K -> T (in dbSNP:rs2302294)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_027596" FT VARIANT 1356 FT /note="G -> S (in dbSNP:rs9916254)" FT /id="VAR_027597" FT CONFLICT 1430 FT /note="C -> R (in Ref. 1; AAK30024)" FT /evidence="ECO:0000305" SQ SEQUENCE 1624 AA; 184362 MW; 0847DC95DCC680D1 CRC64; MSKRRMSVGQ QTWALLCKNC LKKWRMKRQT LLEWLFSFLL VLFLYLFFSN LHQVHDTPQM SSMDLGRVDS FNDTNYVIAF APESKTTQEI MNKVASAPFL KGRTIMGWPD EKSMDELDLN YSIDAVRVIF TDTFSYHLKF SWGHRIPMMK EHRDHSAHCQ AVNEKMKCEG SEFWEKGFVA FQAAINAAII EIATNHSVME QLMSVTGVHM KILPFVAQGG VATDFFIFFC IISFSTFIYY VSVNVTQERQ YITSLMTMMG LRESAFWLSW GLMYAGFILI MATLMALIVK SAQIVVLTGF VMVFTLFLLY GLSLITLAFL MSVLIKKPFL TGLVVFLLIV FWGILGFPAL YTRLPAFLEW TLCLLSPFAF TVGMAQLIHL DYDVNSNAHL DSSQNPYLII ATLFMLVFDT LLYLVLTLYF DKILPAEYGH RCSPLFFLKS CFWFQHGRAN HVVLENETDS DPTPNDCFEP VSPEFCGKEA IRIKNLKKEY AGKCERVEAL KGVVFDIYEG QITALLGHSG AGKTTLLNIL SGLSVPTSGS VTVYNHTLSR MADIENISKF TGFCPQSNVQ FGFLTVKENL RLFAKIKGIL PHEVEKEVQR VVQELEMENI QDILAQNLSG GQNRKLTFGI AILGDPQVLL LDEPTAGLDP LSRHRIWNLL KEGKSDRVIL FSTQFIDEAD ILADRKVFIS NGKLKCAGSS LFLKKKWGIG YHLSLHLNER CDPESITSLV KQHISDAKLT AQSEEKLVYI LPLERTNKFP ELYRDLDRCS NQGIEDYGVS ITTLNEVFLK LEGKSTIDES DIGIWGQLQT DGAKDIGSLV ELEQVLSSFH ETRKTISGVA LWRQQVCAIA KVRFLKLKKE RKSLWTILLL FGISFIPQLL EHLFYESYQK SYPWELSPNT YFLSPGQQPQ DPLTHLLVIN KTGSTIDNFL HSLRRQNIAI EVDAFGTRNG TDDPSYNGAI IVSGDEKDHR FSIACNTKRL NCFPVLLDVI SNGLLGIFNS SEHIQTDRST FFEEHMDYEY GYRSNTFFWI PMAASFTPYI AMSSIGDYKK KAHSQLRISG LYPSAYWFGQ ALVDVSLYFL ILLLMQIMDY IFSPEEIIFI IQNLLIQILC SIGYVSSLVF LTYVISFIFR NGRKNSGIWS FFFLIVVIFS IVATDLNEYG FLGLFFGTML IPPFTLIGSL FIFSEISPDS MDYLGASESE IVYLALLIPY LHFLIFLFIL RCLEMNCRKK LMRKDPVFRI SPRSNAIFPN PEEPEGEEED IQMERMRTVN AMAVRDFDET PVIIASCLRK EYAGKKKNCF SKRKKKIATR NVSFCVKKGE VIGLLGHNGA GKSTTIKMIT GDTKPTAGQV ILKGSGGGEP LGFLGYCPQE NALWPNLTVR QHLEVYAAVK GLRKGDAMIA ITRLVDALKL QDQLKAPVKT LSEGIKRKLC FVLSILGNPS VVLLDEPSTG MDPEGQQQMW QVIRATFRNT ERGALLTTHY MAEAEAVCDR VAIMVSGRLR CIGSIQHLKS KFGKDYLLEM KLKNLAQMEP LHAEILRLFP QAAQQERFSS LMVYKLPVED VRPLSQAFFK LEIVKQSFDL EEYSLSQSTL EQVFLELSKE QELGDLEEDF DPSVKWKLLL QEEP //