GBA2_RAT
ID GBA2_RAT Reviewed; 912 AA.
AC Q5M868;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Non-lysosomal glucosylceramidase {ECO:0000305};
DE Short=NLGase {ECO:0000250|UniProtKB:Q9HCG7};
DE EC=3.2.1.45 {ECO:0000250|UniProtKB:Q9HCG7};
DE AltName: Full=Beta-glucocerebrosidase 2;
DE Short=Beta-glucosidase 2;
DE AltName: Full=Bile acid beta-glucosidase GBA2 {ECO:0000250|UniProtKB:Q9HCG7};
DE AltName: Full=Bile acid glucosyl transferase GBA2 {ECO:0000250|UniProtKB:Q9HCG7};
DE AltName: Full=Cholesterol glucosyltransferase GBA2 {ECO:0000250|UniProtKB:Q69ZF3};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q69ZF3};
DE AltName: Full=Cholesteryl-beta-glucosidase GBA2 {ECO:0000250|UniProtKB:Q69ZF3};
DE EC=3.2.1.- {ECO:0000250|UniProtKB:Q69ZF3};
DE AltName: Full=Glucosylceramidase 2;
DE AltName: Full=Non-lysosomal cholesterol glycosyltransferase {ECO:0000305};
DE AltName: Full=Non-lysosomal galactosylceramidase {ECO:0000305};
DE EC=3.2.1.46 {ECO:0000250|UniProtKB:Q9HCG7};
DE AltName: Full=Non-lysosomal glycosylceramidase {ECO:0000305};
GN Name=Gba2 {ECO:0000312|RGD:1305598};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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: Non-lysosomal glucosylceramidase that catalyzes the
CC hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-
CC (1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as
CC N-acylsphing-4-enine) (By similarity). GlcCers are membrane
CC glycosphingolipids that have a wide intracellular distribution (By
CC similarity). They are the main precursors of more complex
CC glycosphingolipids that play a role in cellular growth,
CC differentiation, adhesion, signaling, cytoskeletal dynamics and
CC membrane properties (By similarity). Involved in the transglucosylation
CC of cholesterol, transfers glucose from GlcCer to cholesterol, thereby
CC modifying its water solubility and biological properties (By
CC similarity). Under specific conditions, may catalyze the reverse
CC reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to
CC ceramide (such as N-acylsphing-4-enine). May play a role in the
CC metabolism of bile acids. Able to hydrolyze bile acid 3-O-glucosides as
CC well as to produce bile acid-glucose conjugates thanks to a bile acid
CC glucosyl transferase activity. Catalyzes the hydrolysis of
CC galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-
CC acylsphing-4-enine), as well as the galactosyl transfer between GalCers
CC and cholesterol in vitro with lower activity compared with their
CC activity against GlcCers (By similarity).
CC {ECO:0000250|UniProtKB:Q69ZF3, ECO:0000250|UniProtKB:Q9HCG7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639; EC=3.2.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an
CC N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390,
CC ChEBI:CHEBI:52639; EC=3.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1->3)-O-lithocholate + H2O = D-glucose +
CC lithocholate; Xref=Rhea:RHEA:58344, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29744, ChEBI:CHEBI:142611;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58345;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1->3)-O-chenodeoxycholate + H2O =
CC chenodeoxycholate + D-glucose; Xref=Rhea:RHEA:58340,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:142610; Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58341;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + chenodeoxycholate = a
CC dolichyl phosphate + beta-D-glucosyl-(1->3)-O-chenodeoxycholate +
CC H(+); Xref=Rhea:RHEA:59104, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57525,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:142610;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59105;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + octyl beta-D-glucose = beta-D-glucosyl-
CC (1->3)-O-chenodeoxycholate + octan-1-ol; Xref=Rhea:RHEA:59108,
CC ChEBI:CHEBI:16188, ChEBI:CHEBI:36234, ChEBI:CHEBI:41128,
CC ChEBI:CHEBI:142610; Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59109;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D-
CC glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17495;
CC Evidence={ECO:0000250|UniProtKB:Q69ZF3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol
CC = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside;
CC Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495,
CC ChEBI:CHEBI:22801, ChEBI:CHEBI:52639;
CC Evidence={ECO:0000250|UniProtKB:Q69ZF3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58266;
CC Evidence={ECO:0000250|UniProtKB:Q69ZF3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4E-enine +
CC cholesterol = cholesteryl 3-beta-D-glucoside + N-(9Z-octadecenoyl)-
CC sphing-4-enine; Xref=Rhea:RHEA:58324, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17495, ChEBI:CHEBI:77996, ChEBI:CHEBI:139140;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58325;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58326;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine +
CC cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-
CC galactoside; Xref=Rhea:RHEA:70235, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:18390, ChEBI:CHEBI:52639, ChEBI:CHEBI:189066;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70236;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70237;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(beta-D-galactosyl)-N-dodecanoylsphing-4-enine + cholesterol
CC = cholesteryl 3-beta-D-galactoside + N-dodecanoylsphing-4-enine;
CC Xref=Rhea:RHEA:70255, ChEBI:CHEBI:16113, ChEBI:CHEBI:72956,
CC ChEBI:CHEBI:73432, ChEBI:CHEBI:189066;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70256;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70257;
CC Evidence={ECO:0000250|UniProtKB:Q9HCG7};
CC -!- ACTIVITY REGULATION: Enzymatic activity is dependent on membrane
CC association and requires the presence of lipids.
CC {ECO:0000250|UniProtKB:Q69ZF3}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q69ZF3}.
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000250|UniProtKB:Q69ZF3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q69ZF3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q69ZF3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q69ZF3}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q69ZF3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q69ZF3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q69ZF3}. Note=Localization to the plasma
CC membrane and alternative topologies have also been reported.
CC {ECO:0000250|UniProtKB:Q9HCG7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5M868-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5M868-2; Sequence=VSP_024385, VSP_024386;
CC -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase family.
CC {ECO:0000305}.
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DR EMBL; AABR03040369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088200; AAH88200.1; -; mRNA.
DR AlphaFoldDB; Q5M868; -.
DR SMR; Q5M868; -.
DR STRING; 10116.ENSRNOP00000022002; -.
DR CAZy; GH116; Glycoside Hydrolase Family 116.
DR PaxDb; Q5M868; -.
DR PRIDE; Q5M868; -.
DR UCSC; RGD:1305598; rat. [Q5M868-1]
DR RGD; 1305598; Gba2.
DR eggNOG; KOG2119; Eukaryota.
DR InParanoid; Q5M868; -.
DR OMA; HDLGAPN; -.
DR PhylomeDB; Q5M868; -.
DR TreeFam; TF313888; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00296; -.
DR PRO; PR:Q5M868; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016364; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q5M868; baseline and differential.
DR Genevisible; Q5M868; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0090498; C:extrinsic component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0004336; F:galactosylceramidase activity; IEA:RHEA.
DR GO; GO:0004348; F:glucosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0046527; F:glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050295; F:steryl-beta-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0006680; P:glucosylceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; ISS:UniProtKB.
DR GO; GO:0030259; P:lipid glycosylation; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0097035; P:regulation of membrane lipid distribution; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR014551; B_Glucosidase_GBA2-typ.
DR InterPro; IPR006775; GH116_catalytic.
DR InterPro; IPR024462; GH116_N.
DR Pfam; PF04685; DUF608; 1.
DR Pfam; PF12215; Glyco_hydr_116N; 1.
DR PIRSF; PIRSF028944; Beta_gluc_GBA2; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cholesterol metabolism; Endoplasmic reticulum;
KW Glycosidase; Glycosyltransferase; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW Steroid metabolism; Sterol metabolism; Transferase.
FT CHAIN 1..912
FT /note="Non-lysosomal glucosylceramidase"
FT /id="PRO_0000283760"
FT REGION 886..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 181..195
FT /note="FIVCLRRDGRTVYQQ -> VRKGAGRRRSDSWLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024385"
FT VAR_SEQ 196..912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024386"
SQ SEQUENCE 912 AA; 102747 MW; C4A47C8C5F3D248A CRC64;
MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY CNSEDSGQLM
ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS NLVKHFGMGL RYLKWWYRKT
QVEKKTPFID MFNSVPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ
FIVCLRRDGR TVYQQVLSLE LPSVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT
CRQITPILPH DYQDSSLPVG VFVWDVENEG DETLDVSIMF SMRNGLGGED DAAGGLWNEP
FRLEQDGTTV QGLLLHHPTP PNPYTMAVAA RHTADTTVTY TTAFDPDSTG QQVWQDLLQD
GQLDSPAGQS TPTQRGEGVA GAVCASSKLL PRGRCCLEFS LAWDMPRIMF GAKGQVHYRR
YTRFFGSDGD VAPALSHYAL CQYAGWENSI SAWQNPVLDD RSLPAWYKSA LFNELYFLAD
GGTVWLEVPE DSLPEELGGS MYQLRPILQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM
LWPKLELSLQ YDMALATFKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY
LIHDTADWKD LNLKFVLQVY RDYYLTGDQG FLKDMWPVCL AVMESEMKFD KDQDGLIENG
GYADQTYDGW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQDKFSSIL CRGREAYERL
LWNGRYYNYD SSSQPQSRSV MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALKTIFELN
VQAFAGGAMG AVNGMQPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY
RTVWERLGLA FQTPEAYCQQ RVFRSLAYMR PLSIWAMQLA LQQQQHKKNS SRPAVTQGTA
PSQPECGPKR SL
