ABCA3_RAT
ID ABCA3_RAT Reviewed; 1704 AA.
AC A0A0G2K1Q8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Phospholipid-transporting ATPase ABCA3 {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:Q99758};
DE AltName: Full=ATP-binding cassette sub-family A member 3 {ECO:0000305};
DE AltName: Full=Xenobiotic-transporting ATPase ABCA3 {ECO:0000250|UniProtKB:Q99758};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q99758};
DE Contains:
DE RecName: Full=150 Kda mature form {ECO:0000250|UniProtKB:Q99758};
GN Name=Abca3 {ECO:0000312|RGD:1307174};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-197, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11940594; DOI=10.1074/jbc.m201812200;
RA Mulugeta S., Gray J.M., Notarfrancesco K.L., Gonzales L.W., Koval M.,
RA Feinstein S.I., Ballard P.L., Fisher A.B., Shuman H.;
RT "Identification of LBM180, a lamellar body limiting membrane protein of
RT alveolar type II cells, as the ABC transporter protein ABCA3.";
RL J. Biol. Chem. 277:22147-22155(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent transport of phospholipids such
CC as phosphatidylcholine and phosphoglycerol from the cytoplasm into the
CC lumen side of lamellar bodies, in turn participates in the lamellar
CC bodies biogenesis and homeostasis of pulmonary surfactant. Transports
CC preferentially phosphatidylcholine containing short acyl chains. In
CC addition plays a role as an efflux transporter of miltefosine across
CC macrophage membranes and free cholesterol (FC) through intralumenal
CC vesicles by removing FC from the cell as a component of surfactant and
CC protects cells from free cholesterol toxicity.
CC {ECO:0000250|UniProtKB:Q99758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q99758};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66273;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66340, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66341;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
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:0000250|UniProtKB:Q99758};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:Q99758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:66344, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q8R420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66345;
CC Evidence={ECO:0000250|UniProtKB:Q8R420};
CC -!- SUBUNIT: Homooligomer; disulfide-linked.
CC {ECO:0000250|UniProtKB:Q99758}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q99758}. Note=Localized in the limiting membrane
CC of lamellar bodies in lung alveolar type II cells. Trafficks via the
CC Golgi, sorting vesicles (SVs) and late endosome/multivesicular body
CC network directly to the outer membrane of lamellar bodies in AT2 lung
CC epithelial cells or to lysosomes and lysosomal-related organelles
CC (LROs) in other cells where undergoes proteolytic cleveage and
CC oligosaccharide processing from high mannose type to complex type.
CC Oligomers formation takes place in a post-endoplasmic reticulum
CC compartment. {ECO:0000250|UniProtKB:Q99758}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, moderately expressed in
CC stomach, intestine, and kidney and weakly expressed in thyroid, brain,
CC liver, spleen, heart, testis, and thymus.
CC {ECO:0000269|PubMed:11940594}.
CC -!- PTM: N-glycosylated. Localization at intracellular vesicles is
CC accompanied by processing of oligosaccharide from high mannose type to
CC complex type. N-linked glycosylation at Asn-124 and Asn-140 is required
CC for stability and efficient anterograde trafficking and prevents from
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q99758}.
CC -!- PTM: Proteolytically cleaved by CTSL and to a lower extent by CTSB
CC within multivesicular bodies (MVB) and lamellar bodies (LB) leading to
CC a mature form of 150 kDa. {ECO:0000250|UniProtKB:Q99758}.
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DR EMBL; AC098526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001054650.1; XM_001054650.6.
DR RefSeq; XP_006220652.1; XM_006220590.3.
DR RefSeq; XP_006246101.1; XM_006246039.3.
DR RefSeq; XP_220219.6; XM_220219.10.
DR AlphaFoldDB; A0A0G2K1Q8; -.
DR SMR; A0A0G2K1Q8; -.
DR GlyGen; A0A0G2K1Q8; 8 sites.
DR jPOST; A0A0G2K1Q8; -.
DR Ensembl; ENSRNOT00000079700; ENSRNOP00000071944; ENSRNOG00000050057.
DR GeneID; 302973; -.
DR KEGG; rno:302973; -.
DR CTD; 21; -.
DR RGD; 1307174; Abca3.
DR GeneTree; ENSGT00940000155289; -.
DR OMA; WKNWIVL; -.
DR OrthoDB; 131191at2759; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000050057; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; A0A0G2K1Q8; baseline and differential.
DR GO; GO:0097208; C:alveolar lamellar body; ISO:RGD.
DR GO; GO:0097233; C:alveolar lamellar body membrane; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
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:0042599; C:lamellar body; ISO:RGD.
DR GO; GO:0097232; C:lamellar body membrane; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; 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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; ISS:UniProtKB.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR GO; GO:0070925; P:organelle assembly; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISO:RGD.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR GO; GO:0032464; P:positive regulation of protein homooligomerization; ISO:RGD.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:0032368; P:regulation of lipid transport; ISO:RGD.
DR GO; GO:0150172; P:regulation of phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; ISO:RGD.
DR GO; GO:0046618; P:xenobiotic export from cell; ISS:UniProtKB.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISS:UniProtKB.
DR GO; GO:0042908; P:xenobiotic transport; ISS: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 ATP-binding; Cytoplasmic vesicle; Disulfide bond; Endosome; Glycoprotein;
KW Lipid transport; Lysosome; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1704
FT /note="Phospholipid-transporting ATPase ABCA3"
FT /id="PRO_0000452299"
FT CHAIN 175..1704
FT /note="150 Kda mature form"
FT /evidence="ECO:0000250|UniProtKB:Q99758"
FT /id="PRO_0000452300"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1310..1330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 530..763
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1381..1614
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 566..573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1416..1423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT SITE 174..175
FT /note="Cleavage; by CTSL"
FT /evidence="ECO:0000250|UniProtKB:Q99758"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1704 AA; 191767 MW; A1F47B43E9CEB8CC CRC64;
MVVLRQLRLL LWKNYTLKKR KVLVTVLELF LPLLFSGILI WLRLKIQSEN VPNATVYPDQ
HIQELPLFFS FPPPGGSWEL AYVPSHSDAA RTITEAVRRE FMIKMRVHGF SSEKDFEDYV
RYDNHSSNVL AAVVFEHTFN HSKDPLPLAV RYHLRFSYTR RNYMWTQTGN LFLKETEGWH
TASLFPLFPS PGPREPSSPD GGEPGYIREG FLAVQHAVDK AIMHYHANAS AHQLFQKLTV
ITKRFPFPPY ISDPFLIAIQ YQLPLLLMLS FTYTSLTIIR AVVQEKEKKL KEYMRMMGLS
SWLHWSAWFL MFLLFSLIVV SFMTLLFCVK VKKDIAVLSN SDPSLVLAFL LCFAISSISF
SFMVSTFFSK ANMAATVGGF LYFFTYTPYF FVAPRYNWMT LSQKLLSCLL SNVAMAMGAQ
LIGKFEAKGT GIQWCDLLNP VNVDDDFCFG QVLGMLLLDS VLYGLVTWYV EAVFPGQFGV
PQPWYFFLMP SYWCGNPRTV VGKEEEGGDP EKAFRTEYFE AEPEDLAAGI KIKHLSKVFQ
VGNKDKMGIR DLTLNLYEGQ ITVLLGHNGA GKTTTMSMLT GLFPPTSGHA YIRGYEISQD
MVQIRKSLGL CPQHDVLFDN LTVAEHLYFY AQLKGLSVQK CPEEVKQMLH TLGLEDKRDS
RSKFLSGGMK RKLAIGIALI AGSKVLMLDE PTSGMDAVSR RAIWDLLQQQ KSDRTVLLTT
HFMDEADLLG DRIAILAKGE LQCCGSSLFL KQKYGAGYHM TLVKEPHCNP EGISQLVHHH
VPNAMLESHA GAELSFILPK ESTHRFESLF AKLEKKQKEL GIASFGASVT TMEEVFLRVG
KLVDTSMDIQ AIQLPALQYQ HERRASDWAL DSNLCGVMDP TNGIGALIEE EEVLVKLNTG
LALHCQQFWA MFLKKAAYSW REWRMVAAQI LVPVTCLTLA LLAINYTSEI FDDPPLKLSL
NEYGTTVVPF SVPGTSRLGQ QLSEHLRDML QAERQEPREV LGDLEEFLVF RASVEGGGFN
ERCLVATSFK DSGERTVVTA LFNNQAYHSP ATALAIVDNL LFKLLCGPRA SIEISNYPQP
RSTLQVAKDQ FNEGRKGFDI ALNLLIAMAF LASTFSILAV SERAVQAKHV QFVSGVHVAT
FWLSALLWDL ISFLVPSLLL LVVFRAFDVH AFTRDGHMAD LLLLLMLYGW AIIPLMYLLS
FFFSAASTAY TRLTIFNILS GIATFIVVTI MRIPAVKLEE LSRTLDHVFL VLPNHCLGMA
VSNFYENYET RRYCTSSEVA THYCKKYNIQ YQENFYAWST PGIGKFVTSM AASGGIYLTL
LFLIETNLLW RLRTFVCAFR RRWTLAELQN RTSVLPEDQD VADERSRVLV PSLDSMLDTP
LIINELSKVY DQRAPLLAVD RISLAVQKGE CFGLLGFNGA GKTTTFKMLT GEETITSGDA
FVGGYSISSD IGKVRQRMGY CPQFDALLDH MTGREMLVMY ARLRGIPERL IDACVENTLR
GLLLEPHANK LVKTYSGGNK RKLSTGIALI GEPAVIFLDE PSTGMDPVAR RLLWDTVARA
RESGKAIVIT SHSMEECEAL CTRLAIMVQG QFKCLGSPQH LKSKFGSGYS LQAKVRSEGK
QEVLEEFKAF VDLTFPGSVL EDEHQDMVHY HLPGCDLSWA KVFGILEKAK EKYGVDDYSV
SQISLEQVFL SFAHLQPPTT EDGR
