GALC_MOUSE
ID GALC_MOUSE Reviewed; 684 AA.
AC P54818; O35151; Q3U3H7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Galactocerebrosidase {ECO:0000305};
DE Short=GALCERase;
DE EC=3.2.1.46 {ECO:0000269|PubMed:8769874};
DE AltName: Full=Galactocerebroside beta-galactosidase;
DE AltName: Full=Galactosylceramidase {ECO:0000250|UniProtKB:P54803};
DE AltName: Full=Galactosylceramide beta-galactosidase;
DE Flags: Precursor;
GN Name=Galc {ECO:0000312|MGI:MGI:95636};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND ROLE IN DISEASE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8769874; DOI=10.1046/j.1471-4159.1996.66031118.x;
RA Sakai N., Inui K., Tatsumi N., Fukushima H., Nishigaki T., Taniike M.,
RA Nishimoto J., Tsukamoto H., Yanagihara I., Ozono K., Okada S.;
RT "Molecular cloning and expression of cDNA for murine galactocerebrosidase
RT and mutation analysis of the twitcher mouse, a model of Krabbe's disease.";
RL J. Neurochem. 66:1118-1124(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Luzi P., Victoria T., Wenger D.A.;
RT "Genomic organization of the mouse galactocerebrosidase (GALC) gene.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10861297; DOI=10.1093/hmg/9.11.1699;
RA Tohyama J., Vanier M.T., Suzuki K., Ezoe T., Matsuda J., Suzuki K.;
RT "Paradoxical influence of acid beta-galactosidase gene dosage on phenotype
RT of the twitcher mouse (genetic galactosylceramidase deficiency).";
RL Hum. Mol. Genet. 9:1699-1707(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 40-684 IN COMPLEX WITH GALACTOSE,
RP ACTIVE SITE, GLYCOSYLATION AT ASN-300; ASN-379; ASN-403 AND ASN-558, AND
RP DISULFIDE BOND.
RX PubMed=21876145; DOI=10.1073/pnas.1105639108;
RA Deane J.E., Graham S.C., Kim N.N., Stein P.E., McNair R.,
RA Cachon-Gonzalez M.B., Cox T.M., Read R.J.;
RT "Insights into Krabbe disease from structures of galactocerebrosidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15169-15173(2011).
CC -!- FUNCTION: Hydrolyzes the galactose ester bonds of glycolipids such as
CC galactosylceramide and galactosylsphingosine (PubMed:8769874,
CC PubMed:10861297). Enzyme with very low activity responsible for the
CC lysosomal catabolism of galactosylceramide, a major lipid in myelin,
CC kidney and epithelial cells of small intestine and colon (By
CC similarity). {ECO:0000250|UniProtKB:P54803,
CC ECO:0000269|PubMed:10861297, ECO:0000269|PubMed:8769874}.
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:0000269|PubMed:8769874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000305|PubMed:8769874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-galactosylceramide + H2O = an N-acyl-sphingoid base + D-
CC galactose; Xref=Rhea:RHEA:43412, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36498, ChEBI:CHEBI:83273;
CC Evidence={ECO:0000269|PubMed:10861297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43413;
CC Evidence={ECO:0000305|PubMed:10861297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1)-sphing-4-enine + H2O = D-galactose +
CC sphing-4-enine; Xref=Rhea:RHEA:43908, ChEBI:CHEBI:4139,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:57934;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC Evidence={ECO:0000250|UniProtKB:P54803};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain and kidney.
CC {ECO:0000269|PubMed:8769874}.
CC -!- DISEASE: Note=Defects in Galc are the cause of the 'twitcher'
CC phenotype; an autosomal recessive leukodystrophy similar to the human
CC disease (Krabbe disease). This deficiency results in the insufficient
CC catabolism of several galactolipids that are important in the
CC production of normal myelin.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 59 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH86671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA07560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D38557; BAA07560.1; ALT_INIT; mRNA.
DR EMBL; AF003886; AAB71823.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF003870; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003871; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003872; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003873; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003874; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003875; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003876; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003877; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003878; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003879; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003880; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003881; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003882; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003883; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003884; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AF003885; AAB71823.1; JOINED; Genomic_DNA.
DR EMBL; AK154760; BAE32809.1; -; mRNA.
DR EMBL; CH466549; EDL18937.1; -; Genomic_DNA.
DR EMBL; BC086671; AAH86671.1; ALT_INIT; mRNA.
DR CCDS; CCDS36517.1; -.
DR RefSeq; NP_032105.2; NM_008079.4.
DR PDB; 3ZR5; X-ray; 2.10 A; A=40-684.
DR PDB; 3ZR6; X-ray; 2.44 A; A=40-684.
DR PDB; 4CCC; X-ray; 2.09 A; A=41-684.
DR PDB; 4CCD; X-ray; 1.97 A; A=41-684.
DR PDB; 4CCE; X-ray; 2.06 A; A=41-684.
DR PDB; 4UFH; X-ray; 2.16 A; A=41-684.
DR PDB; 4UFI; X-ray; 2.40 A; A=41-684.
DR PDB; 4UFJ; X-ray; 2.20 A; A=41-684.
DR PDB; 4UFK; X-ray; 2.40 A; A=43-684.
DR PDB; 4UFL; X-ray; 2.40 A; A=43-684.
DR PDB; 4UFM; X-ray; 2.40 A; A=43-684.
DR PDB; 5NXB; X-ray; 3.60 A; A/B=41-684.
DR PDB; 6Y6S; X-ray; 2.10 A; A=41-684.
DR PDB; 6Y6T; X-ray; 2.25 A; A=41-684.
DR PDBsum; 3ZR5; -.
DR PDBsum; 3ZR6; -.
DR PDBsum; 4CCC; -.
DR PDBsum; 4CCD; -.
DR PDBsum; 4CCE; -.
DR PDBsum; 4UFH; -.
DR PDBsum; 4UFI; -.
DR PDBsum; 4UFJ; -.
DR PDBsum; 4UFK; -.
DR PDBsum; 4UFL; -.
DR PDBsum; 4UFM; -.
DR PDBsum; 5NXB; -.
DR PDBsum; 6Y6S; -.
DR PDBsum; 6Y6T; -.
DR AlphaFoldDB; P54818; -.
DR SMR; P54818; -.
DR BioGRID; 199817; 2.
DR STRING; 10090.ENSMUSP00000021390; -.
DR BindingDB; P54818; -.
DR ChEMBL; CHEMBL2218; -.
DR SwissLipids; SLP:000001418; -.
DR CAZy; GH59; Glycoside Hydrolase Family 59.
DR GlyGen; P54818; 6 sites.
DR iPTMnet; P54818; -.
DR PhosphoSitePlus; P54818; -.
DR EPD; P54818; -.
DR MaxQB; P54818; -.
DR PaxDb; P54818; -.
DR PeptideAtlas; P54818; -.
DR PRIDE; P54818; -.
DR ProteomicsDB; 267416; -.
DR Antibodypedia; 26266; 239 antibodies from 28 providers.
DR DNASU; 14420; -.
DR Ensembl; ENSMUST00000021390; ENSMUSP00000021390; ENSMUSG00000021003.
DR GeneID; 14420; -.
DR KEGG; mmu:14420; -.
DR UCSC; uc007olf.2; mouse.
DR CTD; 2581; -.
DR MGI; MGI:95636; Galc.
DR VEuPathDB; HostDB:ENSMUSG00000021003; -.
DR eggNOG; ENOG502QQ1Q; Eukaryota.
DR GeneTree; ENSGT00390000003303; -.
DR HOGENOM; CLU_015456_2_0_1; -.
DR InParanoid; P54818; -.
DR OMA; VASDNLW; -.
DR OrthoDB; 364933at2759; -.
DR PhylomeDB; P54818; -.
DR TreeFam; TF312985; -.
DR BRENDA; 3.2.1.46; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 14420; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Galc; mouse.
DR PRO; PR:P54818; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P54818; protein.
DR Bgee; ENSMUSG00000021003; Expressed in stroma of bone marrow and 227 other tissues.
DR ExpressionAtlas; P54818; baseline and differential.
DR Genevisible; P54818; MM.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004336; F:galactosylceramidase activity; IDA:UniProtKB.
DR GO; GO:0006683; P:galactosylceramide catabolic process; IDA:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001286; Glyco_hydro_59.
DR InterPro; IPR035394; Glyco_hydro_59_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR15172; PTHR15172; 1.
DR Pfam; PF02057; Glyco_hydro_59; 1.
DR Pfam; PF17387; Glyco_hydro_59M; 1.
DR PRINTS; PR00850; GLHYDRLASE59.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lysosome; Reference proteome; Signal;
KW Sphingolipid metabolism.
FT SIGNAL 1..42
FT /evidence="ECO:0000250"
FT CHAIN 43..684
FT /note="Galactocerebrosidase"
FT /id="PRO_0000012232"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:21876145"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21876145"
FT BINDING 109
FT /ligand="substrate"
FT BINDING 151
FT /ligand="substrate"
FT BINDING 197
FT /ligand="substrate"
FT BINDING 396
FT /ligand="substrate"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21876145"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21876145"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21876145"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21876145"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..394
FT /evidence="ECO:0000269|PubMed:21876145"
FT CONFLICT 376
FT /note="G -> A (in Ref. 2; AAB71823)"
FT /evidence="ECO:0000305"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4CCD"
FT TURN 67..73
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4CCD"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 168..186
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4CCC"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4CCD"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 558..567
FT /evidence="ECO:0007829|PDB:4CCD"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:4CCD"
FT HELIX 585..590
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:4CCD"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 628..636
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 639..644
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 662..670
FT /evidence="ECO:0007829|PDB:4CCD"
FT STRAND 673..683
FT /evidence="ECO:0007829|PDB:4CCD"
SQ SEQUENCE 684 AA; 77256 MW; DD4BD45AE898C524 CRC64;
MANSQPKASQ QRQAKVMTAA AGSASRVAVP LLLCALLVPG GAYVLDDSDG LGREFDGIGA
VSGGGATSRL LVNYPEPYRS EILDYLFKPN FGASLHILKV EIGGDGQTTD GTEPSHMHYE
LDENYFRGYE WWLMKEAKKR NPDIILMGLP WSFPGWLGKG FSWPYVNLQL TAYYVVRWIL
GAKHYHDLDI DYIGIWNERP FDANYIKELR KMLDYQGLQR VRIIASDNLW EPISSSLLLD
QELWKVVDVI GAHYPGTYTV WNAKMSGKKL WSSEDFSTIN SNVGAGCWSR ILNQNYINGN
MTSTIAWNLV ASYYEELPYG RSGLMTAQEP WSGHYVVASP IWVSAHTTQF TQPGWYYLKT
VGHLEKGGSY VALTDGLGNL TIIIETMSHQ HSMCIRPYLP YYNVSHQLAT FTLKGSLREI
QELQVWYTKL GTPQQRLHFK QLDTLWLLDG SGSFTLELEE DEIFTLTTLT TGRKGSYPPP
PSSKPFPTNY KDDFNVEYPL FSEAPNFADQ TGVFEYYMNN EDREHRFTLR QVLNQRPITW
AADASSTISV IGDHHWTNMT VQCDVYIETP RSGGVFIAGR VNKGGILIRS ATGVFFWIFA
NGSYRVTADL GGWITYASGH ADVTAKRWYT LTLGIKGYFA FGMLNGTILW KNVRVKYPGH
GWAAIGTHTF EFAQFDNFRV EAAR
