HEXA_MOUSE
ID HEXA_MOUSE Reviewed; 528 AA.
AC P29416; Q64246; Q91XG3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Beta-hexosaminidase subunit alpha {ECO:0000305};
DE EC=3.2.1.52 {ECO:0000250|UniProtKB:P06865};
DE AltName: Full=Beta-N-acetylhexosaminidase subunit alpha;
DE Short=Hexosaminidase subunit A;
DE AltName: Full=N-acetyl-beta-glucosaminidase subunit alpha;
DE Flags: Precursor;
GN Name=Hexa {ECO:0000312|MGI:MGI:96073};
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].
RC TISSUE=Testis;
RX PubMed=1379046; DOI=10.1042/bj2850593;
RA Beccari T., Hoade J., Orlacchio A., Stirling J.L.;
RT "Cloning and sequence analysis of a cDNA encoding the alpha-subunit of
RT mouse beta-N-acetylhexosaminidase and comparison with the human enzyme.";
RL Biochem. J. 285:593-596(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7833835;
RA Bianconi S., Beccari T., Stirling J.L., Sheardown S., Orlacchio A.;
RT "Organization of the gene for the alpha-subunit of mouse beta-N-
RT acetylhexosaminidase (HEXa).";
RL Biochem. Mol. Biol. Int. 34:579-586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=7959736; DOI=10.1006/geno.1994.1318;
RA Yamanaka S., Johnson O.N., Norflus F., Boles D.J., Proia R.L.;
RT "Structure and expression of the mouse beta-hexosaminidase genes, Hexa and
RT Hexb.";
RL Genomics 21:588-596(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7896264; DOI=10.1006/geno.1994.1587;
RA Wakamatsu N., Benoit G., Lamhonwah A.-M., Zhang Z.-X., Trasler J.M.,
RA Triggs-Raine B.L., Gravel R.A.;
RT "Structural organization, sequence, and expression of the mouse HEXA gene
RT encoding the alpha subunit of hexosaminidase A.";
RL Genomics 24:110-119(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Tongue;
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 [6]
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 (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
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).
CC -!- FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or
CC sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the
CC oligosaccharide moieties from proteins and neutral glycolipids, or from
CC certain mucopolysaccharides. The isozyme S is as active as the isozyme
CC A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate
CC trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and
CC the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze
CC each of these substrates, however hydrolyzes efficiently neutral
CC oligosaccharide. Only the isozyme A is responsible for the degradation
CC of GM2 gangliosides in the presence of GM2A.
CC {ECO:0000250|UniProtKB:P06865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-
CC sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D-
CC 3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-
CC acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 (d18:1(4E)) + H2O = ganglioside GM3
CC (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065,
CC ChEBI:CHEBI:71502; Evidence={ECO:0000250|UniProtKB:P06865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 + H2O = ganglioside GM3 + N-acetyl-beta-D-
CC galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-
CC sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-
CC L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-
CC GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565,
CC ChEBI:CHEBI:152566; Evidence={ECO:0000250|UniProtKB:P06865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-
CC iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = alpha-L-iduronyl-
CC (1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-
CC sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385;
CC Evidence={ECO:0000250|UniProtKB:P06865};
CC -!- ACTIVITY REGULATION: Addition of GM2A stimulates the hydrolysis of
CC sulfated glycosphingolipid SM2 and the ganglioside GM2.
CC {ECO:0000250|UniProtKB:P06865}.
CC -!- SUBUNIT: There are 3 beta-hexosaminidase isozymes: isozyme A
CC (hexosaminidase A) is an heterodimer composed of one subunit alpha and
CC one subunit beta (chain A and B); isozyme B (hexosaminidase B) is an
CC homodimer of two beta subunits (two chains A and B); isozyme S
CC (hexosaminidase S) is a homodimer of two alpha subunits. The
CC composition of the dimer (isozyme A versus isozyme S) has a significant
CC effect on the substrate specificity of the alpha subunit active site.
CC {ECO:0000250|UniProtKB:P06865}.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in testis, adrenal,
CC epididymis and heart. Low levels seen in the liver.
CC {ECO:0000269|PubMed:7896264}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; X64331; CAA45615.1; -; mRNA.
DR EMBL; U05837; AAC53246.1; -; Genomic_DNA.
DR EMBL; U05824; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05825; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05826; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05827; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05828; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05829; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05830; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05831; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05832; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05833; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05834; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05835; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U05836; AAC53246.1; JOINED; Genomic_DNA.
DR EMBL; U07721; AAA18777.1; -; Unassigned_DNA.
DR EMBL; U07709; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07710; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07711; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07712; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07713; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07714; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07715; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07716; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07717; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07718; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07719; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07720; AAA18777.1; JOINED; Unassigned_DNA.
DR EMBL; U07631; AAA18775.1; -; mRNA.
DR EMBL; X79061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X79062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK075895; BAC36036.1; -; mRNA.
DR EMBL; AK075911; BAC36049.1; -; mRNA.
DR EMBL; AK144168; BAE25744.1; -; mRNA.
DR EMBL; AK159814; BAE35394.1; -; mRNA.
DR EMBL; CH466522; EDL25971.1; -; Genomic_DNA.
DR EMBL; BC010755; AAH10755.1; -; mRNA.
DR CCDS; CCDS23250.1; -.
DR PIR; I48253; I48253.
DR RefSeq; NP_034551.2; NM_010421.5.
DR AlphaFoldDB; P29416; -.
DR SMR; P29416; -.
DR BioGRID; 200280; 33.
DR ComplexPortal; CPX-689; Beta-hexosaminidase A complex.
DR ComplexPortal; CPX-691; Beta-hexosaminidase S complex.
DR IntAct; P29416; 1.
DR STRING; 10090.ENSMUSP00000026262; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR GlyConnect; 2151; 1 N-Linked glycan (1 site).
DR GlyGen; P29416; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P29416; -.
DR PhosphoSitePlus; P29416; -.
DR EPD; P29416; -.
DR MaxQB; P29416; -.
DR PaxDb; P29416; -.
DR PeptideAtlas; P29416; -.
DR PRIDE; P29416; -.
DR ProteomicsDB; 273335; -.
DR DNASU; 15211; -.
DR Ensembl; ENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
DR GeneID; 15211; -.
DR KEGG; mmu:15211; -.
DR UCSC; uc009pxw.1; mouse.
DR CTD; 3073; -.
DR MGI; MGI:96073; Hexa.
DR VEuPathDB; HostDB:ENSMUSG00000025232; -.
DR eggNOG; KOG2499; Eukaryota.
DR GeneTree; ENSGT00390000008107; -.
DR HOGENOM; CLU_007082_0_0_1; -.
DR InParanoid; P29416; -.
DR OMA; QNIFCAG; -.
DR OrthoDB; 545162at2759; -.
DR PhylomeDB; P29416; -.
DR TreeFam; TF313036; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR BioGRID-ORCS; 15211; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Hexa; mouse.
DR PRO; PR:P29416; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P29416; protein.
DR Bgee; ENSMUSG00000025232; Expressed in stroma of bone marrow and 257 other tissues.
DR Genevisible; P29416; MM.
DR GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR GO; GO:1905379; C:beta-N-acetylhexosaminidase complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043202; C:lysosomal lumen; IC:ComplexPortal.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISO:MGI.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:MGI.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR GO; GO:0006689; P:ganglioside catabolic process; IMP:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IMP:ComplexPortal.
DR GO; GO:0030214; P:hyaluronan catabolic process; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0051651; P:maintenance of location in cell; IMP:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IGI:MGI.
DR GO; GO:0019953; P:sexual reproduction; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Lysosome; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PROPEP 23..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000011995"
FT CHAIN 89..528
FT /note="Beta-hexosaminidase subunit alpha"
FT /id="PRO_0000011996"
FT REGION 422..423
FT /note="Critical for hydrolysis GM2 gangliosides"
FT /evidence="ECO:0000250"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..104
FT /evidence="ECO:0000250"
FT DISULFID 277..328
FT /evidence="ECO:0000250"
FT DISULFID 504..521
FT /evidence="ECO:0000250"
FT CONFLICT 56
FT /note="A -> G (in Ref. 1; CAA45615 and 2; AAC53246)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> E (in Ref. 4; X79061/X79062)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="E -> Q (in Ref. 4; X79061/X79062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60613 MW; 95DEA72D767094EF CRC64;
MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV SSAAQAGCVV
LDEAFRRYRN LLFGSGSWPR PSFSNKQQTL GKNILVVSVV TAECNEFPNL ESVENYTLTI
NDDQCLLASE TVWGALRGLE TFSQLVWKSA EGTFFINKTK IKDFPRFPHR GVLLDTSRHY
LPLSSILDTL DVMAYNKFNV FHWHLVDDSS FPYESFTFPE LTRKGSFNPV THIYTAQDVK
EVIEYARLRG IRVLAEFDTP GHTLSWGPGA PGLLTPCYSG SHLSGTFGPV NPSLNSTYDF
MSTLFLEISS VFPDFYLHLG GDEVDFTCWK SNPNIQAFMK KKGFTDFKQL ESFYIQTLLD
IVSDYDKGYV VWQEVFDNKV KVRPDTIIQV WREEMPVEYM LEMQDITRAG FRALLSAPWY
LNRVKYGPDW KDMYKVEPLA FHGTPEQKAL VIGGEACMWG EYVDSTNLVP RLWPRAGAVA
ERLWSSNLTT NIDFAFKRLS HFRCELVRRG IQAQPISVGY CEQEFEQT
