ID MA2B1_BOVIN Reviewed; 999 AA.
AC Q29451; F1MMX7; O02848; O19138;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 4.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Lysosomal alpha-mannosidase;
DE Short=Laman;
DE EC=3.2.1.24;
DE AltName: Full=Lysosomal acid alpha-mannosidase;
DE AltName: Full=Mannosidase alpha class 2B member 1;
DE AltName: Full=Mannosidase alpha-B;
DE Contains:
DE RecName: Full=Lysosomal alpha-mannosidase A peptide;
DE Contains:
DE RecName: Full=Lysosomal alpha-mannosidase B peptide;
DE Contains:
DE RecName: Full=Lysosomal alpha-mannosidase C peptide;
DE Contains:
DE RecName: Full=Lysosomal alpha-mannosidase D peptide;
DE Contains:
DE RecName: Full=Lysosomal alpha-mannosidase E peptide;
DE Flags: Precursor;
GN Name=MAN2B1; Synonyms=MANB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP VARIANTS AM HIS-221 AND LEU-321.
RC TISSUE=Kidney;
RX PubMed=9208932; DOI=10.1111/j.1432-1033.1997.00410.x;
RA Tollersrud O.-K., Berg T., Healy P., Evjen G., Ramachandran U., Nilssen O.;
RT "Purification of bovine lysosomal alpha-mannosidase, characterization of
RT its gene and determination of two mutations that cause alpha-
RT mannosidosis.";
RL Eur. J. Biochem. 246:410-419(1997).
RN [2]
RP SEQUENCE REVISION TO 358.
RA Berg T.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 52-999 IN COMPLEX WITH ZINC ION,
RP COFACTOR, ACTIVE SITE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-134;
RP ASN-634; ASN-681 AND ASN-755.
RX PubMed=12634058; DOI=10.1016/s0022-2836(03)00172-4;
RA Heikinheimo P., Helland R., Leiros H.-K.S., Leiros I., Karlsen S.,
RA Evjen G., Ravelli R., Schoehn G., Ruigrok R., Tollersrud O.-K.,
RA McSweeney S., Hough E.;
RT "The structure of bovine lysosomal alpha-mannosidase suggests a novel
RT mechanism for low-pH activation.";
RL J. Mol. Biol. 327:631-644(2003).
CC -!- FUNCTION: Necessary for the catabolism of N-linked carbohydrates
CC released during glycoprotein turnover.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12634058};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12634058};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- PTM: Processed into 5 peptides of 35/38 kDa (A), 11/13 kDa (B) and 22
CC kDa (C), 38 kDa (D) and 13/15 kDa (E). The A, B and C peptides are
CC disulfide-linked into a 67 kDa complex.
CC -!- PTM: Heavily glycosylated. Some sugar chains are of the high-mannose
CC type.
CC -!- DISEASE: Note=Defects in MAN2B1 are the cause of lysosomal alpha-
CC mannosidosis (AM). AM is a lysosomal storage disease characterized by
CC accumulation of unbranched oligosaccharide chains. The disease
CC manifests itself by head tremor, aggressive tendency, ataxia, failure
CC to thrive, and early death. {ECO:0000269|PubMed:9208932}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; L31373; AAB67726.2; -; mRNA.
DR EMBL; U97694; AAC48763.1; -; Genomic_DNA.
DR EMBL; U97686; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97687; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97688; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97689; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97690; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97691; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97692; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; U97693; AAC48763.1; JOINED; Genomic_DNA.
DR EMBL; DAAA02019388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_776986.2; NM_174561.2.
DR PDB; 1O7D; X-ray; 2.70 A; A=51-348, B=349-432, C=433-591, D=592-873, E=874-999.
DR PDBsum; 1O7D; -.
DR AlphaFoldDB; Q29451; -.
DR SMR; Q29451; -.
DR STRING; 9913.ENSBTAP00000064540; -.
DR ChEMBL; CHEMBL1932902; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR GlyCosmos; Q29451; 8 sites, No reported glycans.
DR iPTMnet; Q29451; -.
DR PaxDb; 9913-ENSBTAP00000008193; -.
DR Ensembl; ENSBTAT00000070599.1; ENSBTAP00000064540.1; ENSBTAG00000006241.5.
DR GeneID; 282272; -.
DR KEGG; bta:282272; -.
DR CTD; 4125; -.
DR VEuPathDB; HostDB:ENSBTAG00000006241; -.
DR VGNC; VGNC:108504; MAN2B1.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_2_0_1; -.
DR InParanoid; Q29451; -.
DR OMA; LEFIWRP; -.
DR OrthoDB; 5474711at2759; -.
DR TreeFam; TF313840; -.
DR BRENDA; 3.2.1.24; 908.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-8853383; Lysosomal oligosaccharide catabolism.
DR EvolutionaryTrace; Q29451; -.
DR PRO; PR:Q29451; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000006241; Expressed in caput epididymis and 105 other cell types or tissues.
DR ExpressionAtlas; Q29451; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0043202; C:lysosomal lumen; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0006013; P:mannose metabolic process; IEA:Ensembl.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; IEA:Ensembl.
DR CDD; cd10810; GH38N_AMII_LAM_like; 1.
DR Gene3D; 2.60.40.1360; -; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR048534; Man2a1-like_dom.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF21260; Laman-like_dom; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Lysosome; Metal-binding;
KW Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..50
FT CHAIN 51..999
FT /note="Lysosomal alpha-mannosidase"
FT /id="PRO_0000012060"
FT CHAIN 51..347
FT /note="Lysosomal alpha-mannosidase A peptide"
FT /id="PRO_0000012061"
FT CHAIN 348..431
FT /note="Lysosomal alpha-mannosidase B peptide"
FT /id="PRO_0000012062"
FT CHAIN 432..590
FT /note="Lysosomal alpha-mannosidase C peptide"
FT /id="PRO_0000012063"
FT PROPEP 591..621
FT /evidence="ECO:0000255"
FT /id="PRO_0000012064"
FT CHAIN 622..871
FT /note="Lysosomal alpha-mannosidase D peptide"
FT /id="PRO_0000012065"
FT CHAIN 872..999
FT /note="Lysosomal alpha-mannosidase E peptide"
FT /id="PRO_0000012066"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12634058"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 56
FT /note="Interchain (with C-360)"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT DISULFID 269..274
FT /evidence="ECO:0000269|PubMed:12634058"
FT DISULFID 360
FT /note="Interchain (with C-56)"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT DISULFID 414
FT /note="Interchain (with C-474)"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT DISULFID 474
FT /note="Interchain (with C-414)"
FT /evidence="ECO:0000269|PubMed:12634058,
FT ECO:0007744|PDB:1O7D"
FT DISULFID 495..503
FT /evidence="ECO:0000269|PubMed:12634058"
FT VARIANT 221
FT /note="R -> H (in AM; Galloway cattle)"
FT /evidence="ECO:0000269|PubMed:9208932"
FT VARIANT 321
FT /note="F -> L (in AM; Angus cattle)"
FT /evidence="ECO:0000269|PubMed:9208932"
FT CONFLICT 176
FT /note="G -> R (in Ref. 1; AAB67726/AAC48763)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..550
FT /note="Missing (in Ref. 1; AAC48763)"
FT /evidence="ECO:0000305"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 166..184
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 398..420
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 448..452
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 457..486
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 510..518
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 524..532
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 560..568
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 627..635
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 686..692
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 697..705
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 716..723
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 739..745
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 765..774
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 776..786
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 797..805
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 826..837
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 838..853
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 880..883
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 890..898
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 901..907
FT /evidence="ECO:0007829|PDB:1O7D"
FT TURN 912..919
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 929..943
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 947..950
FT /evidence="ECO:0007829|PDB:1O7D"
FT HELIX 951..953
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 978..981
FT /evidence="ECO:0007829|PDB:1O7D"
FT STRAND 986..994
FT /evidence="ECO:0007829|PDB:1O7D"
SQ SEQUENCE 999 AA; 112919 MW; C86DE7532925DB10 CRC64;
MVGDARPSGV RAGGCRGAVG SRTSSRALRP PLPPLSSLFV LFLAAPCAWA AGYKTCPKVK
PDMLNVHLVP HTHDDVGWLK TVDQYFYGIY NNIQPAGVQY ILDSVISSLL ANPTRRFIYV
EIAFFSRWWR QQTNATQKIV RELVRQGRLE FANGGWVMND EATTHYGAII DQMTLGLRFL
EETFGSDGRP RVAWHIDPFG HSREQASLFA QMGFDGFFFG RLDYQDKKVR KKTLQMEQVW
RASTSLKPPT ADLFTSVLPN MYNPPEGLCW DMLCADKPVV EDTRSPEYNA KELVRYFLKL
ATDQGKLYRT KHTVMTMGSD FQYENANTWF KNLDKLIQLV NAQQRANGIR VNVLYSTPAC
YLWELNKANL SWSVKKDDFF PYADGPYMFW TGYFSSRPAL KRYERLSYNF LQVCNQLEAL
AGPAANVGPY GSGDSAPLNE AMAVLQHHDA VSGTSRQHVA NDYARQLSEG WRPCEVLMSN
ALAHLSGLKE DFAFCRKLNI SICPLTQTAE RFQVIVYNPL GRKVDWMVRL PVSKHVYLVK
DPGGKIVPSD VVTIPSSDSQ ELLFSALVPA VGFSIYSVSQ MPNQRPQKSW SRDLVIQNEY
LRARFDPNTG LLMELENLEQ NLLLPVRQAF YWYNASTGNN LSSQASGAYI FRPNQNKPLF
VSHWAQTHLV KASLVQEVHQ NFSAWCSQVV RLYPRQRHLE LEWTVGPIPV GDGWGKEVIS
RFDTALATRG LFYTDSNGRE ILERRRNYRP TWKLNQTEPV AGNYYPVNSR IYITDGNMQL
TVLTDRSQGG SSLRDGSLEL MVHRRLLKDD ARGVGEPLNK EGSGLWVRGR HLVLLDKKET
AAARHRLQAE MEVLAPQVVL AQGGGARYRL EKAPRTQFSG LRRELPPSVR LLTLARWGPE
TLLLRLEHQF AVGEDSGRNL SSPVTLDLTN LFSAFTITNL RETTLAANQL LAYASRLQWT
TDTGPTPHPS PSRPVSATIT LQPMEIRTFL ASVQWEEDG
//
