ID ABCG4_HUMAN Reviewed; 646 AA. AC Q9H172; A8K1B5; Q8WWH0; Q8WWH1; Q8WWH2; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=ATP-binding cassette sub-family G member 4; DE EC=7.6.2.- {ECO:0000269|PubMed:15240127, ECO:0000269|PubMed:33141061}; GN Name=ABCG4 {ECO:0000312|HGNC:HGNC:13884}; Synonyms=WHITE2; 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), AND MISCELLANEOUS. RX PubMed=11606068; DOI=10.1006/bbrc.2001.5756; RA Engel T., Lorkowski S., Lueken A., Rust S., Schlueter B., Berger G., RA Cullen P., Assmann G.; RT "The human ABCG4 gene is regulated by oxysterols and retinoids in monocyte- RT derived macrophages."; RL Biochem. Biophys. Res. Commun. 288:483-488(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Hippocampus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-118 (ISOFORMS 2; 3 AND 4), ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=11856881; DOI=10.1159/000048816; RA Annilo T., Tammur J., Hutchinson A., Rzhetsky A., Dean M., Allikmets R.; RT "Human and mouse orthologs of a new ATP-binding cassette gene, ABCG4."; RL Cytogenet. Cell Genet. 94:196-201(2001). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-646 (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Spinal ganglion; RX PubMed=12183068; DOI=10.1016/s0167-4889(02)00269-0; RA Oldfield S., Lowry C., Ruddick J., Lightman S.; RT "ABCG4: a novel human white family ABC-transporter expressed in the brain RT and eye."; RL Biochim. Biophys. Acta 1591:175-179(2002). RN [7] RP SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-108. RX PubMed=15240127; DOI=10.1016/j.bbrc.2004.06.037; RA Cserepes J., Szentpetery Z., Seres L., Ozvegy-Laczka C., Langmann T., RA Schmitz G., Glavinas H., Klein I., Homolya L., Varadi A., Sarkadi B., RA Elkind N.B.; RT "Functional expression and characterization of the human ABCG1 and ABCG4 RT proteins: indications for heterodimerization."; RL Biochem. Biophys. Res. Commun. 320:860-867(2004). RN [8] RP SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-108, FUNCTION, AND RP INTERACTION WITH ABCG1. RX PubMed=27228027; DOI=10.1371/journal.pone.0156516; RA Hegyi Z., Homolya L.; RT "Functional Cooperativity between ABCG4 and ABCG1 Isoforms."; RL PLoS ONE 11:e0156516-e0156516(2016). RN [9] RP INDUCTION, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=33141061; DOI=10.1016/j.bbagen.2020.129769; RA Yang A., Alrosan A.Z., Sharpe L.J., Brown A.J., Callaghan R., RA Gelissen I.C.; RT "Regulation of ABCG4 transporter expression by sterols and LXR ligands."; RL Biochim. Biophys. Acta 1865:129769-129769(2021). CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) CC family that may be involved in the cellular efflux of sterols, in CC particular cholesterol and desmosterol (a cholesterol precursor), to CC high-density lipoprotein (HDL) (PubMed:15240127, PubMed:33141061). May CC play an important role in the removal of amyloid-beta peptides from CC brain, in a process that can be antagonized by desmosterol. However it CC is unclear whether ABCG4 can directly transport amyloid-beta peptides CC or whether peptide export may be facilitated due to changes in the CC membrane lipid environment (By similarity). Induces apoptosis in CC various cells (PubMed:27228027). {ECO:0000250|UniProtKB:Q91WA9, CC ECO:0000269|PubMed:15240127, ECO:0000269|PubMed:27228027, CC ECO:0000269|PubMed:33141061}. 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:0000269|PubMed:33141061}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; CC Evidence={ECO:0000305|PubMed:33141061}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + desmosterol(in) + H2O = ADP + desmosterol(out) + H(+) + CC phosphate; Xref=Rhea:RHEA:67932, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q91WA9}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67933; CC Evidence={ECO:0000250|UniProtKB:Q91WA9}; CC -!- SUBUNIT: Half-transporter that forms a functional transporter via CC homo- or heterodimerization. Homodimer (PubMed:27228027). Heterodimers CC with ABCG1 (Probable) (PubMed:27228027). {ECO:0000269|PubMed:27228027, CC ECO:0000305|PubMed:15240127}. CC -!- INTERACTION: CC Q9H172; P45844-4: ABCG1; NbExp=2; IntAct=EBI-8584118, EBI-8584087; CC Q9H172; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-8584118, EBI-13345167; CC Q9H172; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-8584118, EBI-742388; CC Q9H172; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-8584118, EBI-744081; CC Q9H172; O95807: TMEM50A; NbExp=3; IntAct=EBI-8584118, EBI-12903814; CC Q9H172; O76024: WFS1; NbExp=3; IntAct=EBI-8584118, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27228027}; CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi- CC pass membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=B; CC IsoId=Q9H172-1; Sequence=Displayed; CC Name=2; Synonyms=T3, T4; CC IsoId=Q9H172-2; Sequence=VSP_054267; CC Name=3; Synonyms=M, T1; CC IsoId=Q9H172-3; Sequence=VSP_054268; CC Name=4; Synonyms=T2; CC IsoId=Q9H172-4; Sequence=VSP_054266; CC -!- TISSUE SPECIFICITY: Expressed specifically in the brain and the eye. CC {ECO:0000269|PubMed:11856881, ECO:0000269|PubMed:12183068}. CC -!- INDUCTION: Protein expression is stabilized by cellular cholesterol CC status and cholesterol synthesis intermediates desmosterol, lathosterol CC and lanosterol. {ECO:0000269|PubMed:33141061}. CC -!- MISCELLANEOUS: Whether ABCG4 is an LXR target gene, is still under CC debate. Studies performed in monocytes, and in one astrocyte cell line CC indicated that ABCG4 expression could be up-regulated by oxysterols and CC other LXR ligands (PubMed:11606068, PubMed:33141061). However, CC subsequent observations in a number of different cell types (primary CC mouse cells, oligodendrocytes and neuron-like cell lines) have not CC confirmed this observation (By similarity) (PubMed:33141061). CC {ECO:0000250|UniProtKB:Q91WA9, ECO:0000269|PubMed:11606068, CC ECO:0000269|PubMed:33141061}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {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; AJ308237; CAC87131.1; -; mRNA. DR EMBL; AK289830; BAF82519.1; -; mRNA. DR EMBL; AK290035; BAF82724.1; -; mRNA. DR EMBL; CH471065; EAW67464.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67465.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67466.1; -; Genomic_DNA. DR EMBL; BC041091; AAH41091.1; -; mRNA. DR EMBL; AY055472; AAL16400.1; -; Genomic_DNA. DR EMBL; AY055472; AAL16401.1; -; Genomic_DNA. DR EMBL; AY055472; AAL16402.1; -; Genomic_DNA. DR EMBL; AJ300465; CAC17140.1; -; mRNA. DR CCDS; CCDS8415.1; -. [Q9H172-1] DR PIR; JC7777; JC7777. DR RefSeq; NP_001135977.1; NM_001142505.1. [Q9H172-1] DR RefSeq; NP_001335120.1; NM_001348191.1. [Q9H172-1] DR RefSeq; NP_001335121.1; NM_001348192.1. [Q9H172-2] DR RefSeq; NP_071452.2; NM_022169.4. [Q9H172-1] DR RefSeq; XP_011541254.1; XM_011542952.2. [Q9H172-3] DR AlphaFoldDB; Q9H172; -. DR SMR; Q9H172; -. DR BioGRID; 122083; 7. DR IntAct; Q9H172; 7. DR MINT; Q9H172; -. DR STRING; 9606.ENSP00000481728; -. DR TCDB; 3.A.1.204.20; the atp-binding cassette (abc) superfamily. DR GlyCosmos; Q9H172; 1 site, No reported glycans. DR GlyGen; Q9H172; 1 site. DR iPTMnet; Q9H172; -. DR PhosphoSitePlus; Q9H172; -. DR BioMuta; ABCG4; -. DR DMDM; 17432915; -. DR MassIVE; Q9H172; -. DR PaxDb; 9606-ENSP00000481728; -. DR PeptideAtlas; Q9H172; -. DR ProteomicsDB; 80375; -. [Q9H172-1] DR Antibodypedia; 32624; 223 antibodies from 31 providers. DR DNASU; 64137; -. DR Ensembl; ENST00000615496.4; ENSP00000479253.1; ENSG00000172350.10. [Q9H172-1] DR Ensembl; ENST00000619701.5; ENSP00000481728.1; ENSG00000172350.10. [Q9H172-1] DR Ensembl; ENST00000622721.1; ENSP00000484289.1; ENSG00000172350.10. [Q9H172-1] DR GeneID; 64137; -. DR KEGG; hsa:64137; -. DR MANE-Select; ENST00000619701.5; ENSP00000481728.1; NM_022169.5; NP_071452.2. DR UCSC; uc031yhk.2; human. [Q9H172-1] DR AGR; HGNC:13884; -. DR CTD; 64137; -. DR DisGeNET; 64137; -. DR GeneCards; ABCG4; -. DR HGNC; HGNC:13884; ABCG4. DR HPA; ENSG00000172350; Group enriched (brain, retina). DR MIM; 607784; gene. DR neXtProt; NX_Q9H172; -. DR OpenTargets; ENSG00000172350; -. DR PharmGKB; PA24410; -. DR VEuPathDB; HostDB:ENSG00000172350; -. DR eggNOG; KOG0061; Eukaryota. DR GeneTree; ENSGT00940000157853; -. DR HOGENOM; CLU_000604_57_6_1; -. DR InParanoid; Q9H172; -. DR OMA; EESCQFQ; -. DR OrthoDB; 1126902at2759; -. DR PhylomeDB; Q9H172; -. DR TreeFam; TF105210; -. DR PathwayCommons; Q9H172; -. DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis. DR SignaLink; Q9H172; -. DR BioGRID-ORCS; 64137; 9 hits in 1150 CRISPR screens. DR GeneWiki; ABCG4; -. DR GenomeRNAi; 64137; -. DR Pharos; Q9H172; Tbio. DR PRO; PR:Q9H172; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9H172; Protein. DR Bgee; ENSG00000172350; Expressed in right hemisphere of cerebellum and 140 other cell types or tissues. DR ExpressionAtlas; Q9H172; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0034041; F:ABC-type sterol transporter activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; IEA:Ensembl. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB. DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd03213; ABCG_EPDR; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; IPR043926; ABCG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1. DR PANTHER; PTHR48041:SF75; ATP-BINDING CASSETTE SUB-FAMILY G MEMBER 4; 1. DR Pfam; PF01061; ABC2_membrane; 1. DR Pfam; PF19055; ABC2_membrane_7; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR Genevisible; Q9H172; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasmic vesicle; KW Endosome; Glycoprotein; Lipid transport; Membrane; Nucleotide-binding; KW Reference proteome; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..646 FT /note="ATP-binding cassette sub-family G member 4" FT /id="PRO_0000093392" FT TOPO_DOM 1..393 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 394..414 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 415..425 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 426..446 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 447..472 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 473..493 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 494..503 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 504..524 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 525..532 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 533..553 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 554..617 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 618..638 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 639..646 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 61..301 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 386..641 FT /note="ABC transmembrane type-2" FT BINDING 102..109 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CARBOHYD 422 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..100 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11856881" FT /id="VSP_054266" FT VAR_SEQ 1..79 FT /note="MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSH FT LPKRSAVDIEFVELSYSVREGPCWRKR -> MRDLELREVKQLARGHTA (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11856881" FT /id="VSP_054267" FT VAR_SEQ 1..79 FT /note="MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSH FT LPKRSAVDIEFVELSYSVREGPCWRKR -> MCGFSHAFQKRIVAS (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:11856881" FT /id="VSP_054268" FT VARIANT 352 FT /note="P -> L (in dbSNP:rs35060365)" FT /id="VAR_048141" FT MUTAGEN 108 FT /note="K->M: Abrogates ATPase activity. Induces a FT dominant-negative effect on ABCG1 ATP-activity. Does not FT affect subcellular localization." FT /evidence="ECO:0000269|PubMed:15240127, FT ECO:0000269|PubMed:27228027" SQ SEQUENCE 646 AA; 71896 MW; 9CCEC6E150772611 CRC64; MAEKALEAVG CGLGPGAVAM AVTLEDGAEP PVLTTHLKKV ENHITEAQRF SHLPKRSAVD IEFVELSYSV REGPCWRKRG YKTLLKCLSG KFCRRELIGI MGPSGAGKST FMNILAGYRE SGMKGQILVN GRPRELRTFR KMSCYIMQDD MLLPHLTVLE AMMVSANLKL SEKQEVKKEL VTEILTALGL MSCSHTRTAL LSGGQRKRLA IALELVNNPP VMFFDEPTSG LDSASCFQVV SLMKSLAQGG RTIICTIHQP SAKLFEMFDK LYILSQGQCI FKGVVTNLIP YLKGLGLHCP TYHNPADFII EVASGEYGDL NPMLFRAVQN GLCAMAEKKS SPEKNEVPAP CPPCPPEVDP IESHTFATST LTQFCILFKR TFLSILRDTV LTHLRFMSHV VIGVLIGLLY LHIGDDASKV FNNTGCLFFS MLFLMFAALM PTVLTFPLEM AVFMREHLNY WYSLKAYYLA KTMADVPFQV VCPVVYCSIV YWMTGQPAET SRFLLFSALA TATALVAQSL GLLIGAASNS LQVATFVGPV TAIPVLLFSG FFVSFKTIPT YLQWSSYLSY VRYGFEGVIL TIYGMERGDL TCLEERCPFR EPQSILRALD VEDAKLYMDF LVLGIFFLAL RLLAYLVLRY RVKSER //