AMY1A_HUMAN
ID AMY1A_HUMAN Reviewed; 511 AA.
AC P0DUB6; A6NJS5; A8K8H6; P04745; Q13763; Q5T083;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Alpha-amylase 1A;
DE EC=3.2.1.1 {ECO:0000269|PubMed:12527308};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 1;
DE AltName: Full=Salivary alpha-amylase;
DE Flags: Precursor;
GN Name=AMY1A {ECO:0000312|HGNC:HGNC:474}; Synonyms=AMY1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2423416; DOI=10.1016/0378-1119(86)90110-1;
RA Nishide T., Nakamura Y., Emi M., Yamamoto T., Ogawa M., Mori T.,
RA Matsubara K.;
RT "Primary structure of human salivary alpha-amylase gene.";
RL Gene 41:299-304(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6610603; DOI=10.1016/0378-1119(84)90265-8;
RA Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S.,
RA Matsubara K.;
RT "Corrected sequences of cDNAs for human salivary and pancreatic alpha-
RT amylases.";
RL Gene 28:263-270(1984).
RN [3]
RP ERRATUM OF PUBMED:6610603, AND SEQUENCE REVISION.
RA Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S.,
RA Matsubara K.;
RL Gene 50:371-372(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56 AND 408-448.
RX PubMed=2452973; DOI=10.1128/mcb.8.3.1197-1205.1988;
RA Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.;
RT "Concerted evolution of human amylase genes.";
RL Mol. Cell. Biol. 8:1197-1205(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293 AND 450-511.
RX PubMed=2442579;
RA Handy D.E., Larsen S.H., Karn R.C., Hodes M.E.;
RT "Identification of a human salivary amylase gene. Partial sequence of
RT genomic DNA suggests a mode of regulation different from that of mouse,
RT Amy1.";
RL Mol. Biol. Med. 4:145-155(1987).
RN [9]
RP GLYCOSYLATION AT ASN-427, AND DEAMIDATION AT ASN-365; ASN-427 AND ASN-474.
RX PubMed=1710976; DOI=10.1002/elps.1150120114;
RA Bank R.A., Hettema E.H., Arwert F., Amerongen A.V., Pronk J.C.;
RT "Electrophoretic characterization of posttranslational modifications of
RT human parotid salivary alpha-amylase.";
RL Electrophoresis 12:74-79(1991).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM
RP AND CHLORIDE, DISULFIDE BONDS, AND COFACTOR.
RX PubMed=15299664; DOI=10.1107/s0907444995014119;
RA Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M.J.;
RT "Structure of human salivary alpha-amylase at 1.6-A resolution:
RT implications for its role in the oral cavity.";
RL Acta Crystallogr. D 52:435-446(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 16-511 OF WILD-TYPE AND MUTANT
RP 321-GLY--ALA-325 DEL IN COMPLEX WITH CALCIUM AND CHLORIDE, CATALYTIC
RP ACTIVITY, DISULFIDE BONDS, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12527308; DOI=10.1016/s0022-2836(02)01326-8;
RA Ramasubbu N., Ragunath C., Mishra P.J.;
RT "Probing the role of a mobile loop in substrate binding and enzyme activity
RT of human salivary amylase.";
RL J. Mol. Biol. 325:1061-1076(2003).
CC -!- FUNCTION: Calcium-binding enzyme that initiates starch digestion in the
CC oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal
CC (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose,
CC isomaltose, small amounts of glucose as well as small linear and
CC branched oligosaccharides called dextrins (PubMed:12527308).
CC {ECO:0000269|PubMed:12527308}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:12527308};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12527308,
CC ECO:0000269|PubMed:15299664};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:12527308,
CC ECO:0000269|PubMed:15299664};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- CAUTION: Three distinct genes (AMY1A, AMY1B and AMY1C), located in a
CC gene cluster on 1p21, encode proteins sharing the same peptidic
CC sequence. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Amylase entry;
CC URL="https://en.wikipedia.org/wiki/Amylase";
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DR EMBL; M18786; AAA52279.1; -; Genomic_DNA.
DR EMBL; M18715; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18717; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18719; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18721; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18723; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18725; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18727; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; M18784; AAA52279.1; JOINED; Genomic_DNA.
DR EMBL; AK292341; BAF85030.1; -; mRNA.
DR EMBL; AC105272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063129; AAH63129.1; -; mRNA.
DR EMBL; BC069347; AAH69347.1; -; mRNA.
DR EMBL; BC069463; AAH69463.1; -; mRNA.
DR EMBL; BC092444; AAH92444.1; -; mRNA.
DR EMBL; BC132985; AAI32986.1; -; mRNA.
DR EMBL; BC132987; AAI32988.1; -; mRNA.
DR EMBL; BC132995; AAI32996.1; -; mRNA.
DR EMBL; BC132997; AAI32998.1; -; mRNA.
DR EMBL; M18671; AAA58368.1; -; Genomic_DNA.
DR EMBL; M18674; AAA16183.2; -; Genomic_DNA.
DR EMBL; M19233; AAA57345.1; ALT_TERM; Genomic_DNA.
DR EMBL; M17883; AAA57345.1; JOINED; Genomic_DNA.
DR EMBL; M17884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30782.1; -.
DR PIR; A91543; ALHUS.
DR RefSeq; NP_001008219.1; NM_001008218.1.
DR RefSeq; NP_001008220.1; NM_001008219.2.
DR RefSeq; NP_001008222.1; NM_001008221.1.
DR RefSeq; NP_001333709.1; NM_001346780.1.
DR RefSeq; NP_004029.2; NM_004038.3.
DR RefSeq; XP_011539564.1; XM_011541262.1.
DR RefSeq; XP_016856547.1; XM_017001058.1.
DR PDB; 1C8Q; X-ray; 2.30 A; A=16-511.
DR PDB; 1JXJ; X-ray; 1.99 A; A=16-511.
DR PDB; 1JXK; X-ray; 1.90 A; A=16-511.
DR PDB; 1MFU; X-ray; 2.00 A; A=17-511.
DR PDB; 1MFV; X-ray; 2.00 A; A=17-511.
DR PDB; 1NM9; X-ray; 2.10 A; A=16-511.
DR PDB; 1Q4N; X-ray; 2.07 A; X=16-511.
DR PDB; 1SMD; X-ray; 1.60 A; A=17-511.
DR PDB; 1XV8; X-ray; 3.00 A; A/B=16-511.
DR PDB; 1Z32; X-ray; 1.60 A; X=16-511.
DR PDB; 3BLK; X-ray; 2.00 A; A=16-511.
DR PDB; 3BLP; X-ray; 1.60 A; X=16-511.
DR PDB; 3DHP; X-ray; 1.50 A; A=16-511.
DR PDBsum; 1C8Q; -.
DR PDBsum; 1JXJ; -.
DR PDBsum; 1JXK; -.
DR PDBsum; 1MFU; -.
DR PDBsum; 1MFV; -.
DR PDBsum; 1NM9; -.
DR PDBsum; 1Q4N; -.
DR PDBsum; 1SMD; -.
DR PDBsum; 1XV8; -.
DR PDBsum; 1Z32; -.
DR PDBsum; 3BLK; -.
DR PDBsum; 3BLP; -.
DR PDBsum; 3DHP; -.
DR AlphaFoldDB; P0DUB6; -.
DR SMR; P0DUB6; -.
DR BindingDB; P0DUB6; -.
DR ChEMBL; CHEMBL2478; -.
DR GlyGen; P0DUB6; 2 sites.
DR iPTMnet; P04745; -.
DR PhosphoSitePlus; P0DUB6; -.
DR MassIVE; P0DUB6; -.
DR Ensembl; ENST00000370083.9; ENSP00000359100.4; ENSG00000237763.10.
DR GeneID; 276; -.
DR GeneID; 277; -.
DR GeneID; 278; -.
DR KEGG; hsa:276; -.
DR KEGG; hsa:277; -.
DR KEGG; hsa:278; -.
DR MANE-Select; ENST00000330330.10; ENSP00000330484.5; NM_001008218.2; NP_001008219.1.
DR MANE-Select; ENST00000370083.9; ENSP00000359100.4; NM_004038.4; NP_004029.2.
DR MANE-Select; ENST00000622339.5; ENSP00000481450.2; NM_001008219.3; NP_001008220.1.
DR CTD; 276; -.
DR CTD; 277; -.
DR CTD; 278; -.
DR GeneCards; AMY1A; -.
DR HGNC; HGNC:474; AMY1A.
DR MIM; 104702; gene.
DR neXtProt; NX_P0DUB6; -.
DR OpenTargets; ENSG00000187733; -.
DR GeneTree; ENSGT00940000154802; -.
DR OMA; CYTGSEN; -.
DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000237763; Expressed in body of pancreas and 87 other tissues.
DR ExpressionAtlas; P0DUB6; baseline and differential.
DR Genevisible; P04745; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; IDA:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Chloride; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..511
FT /note="Alpha-amylase 1A"
FT /id="PRO_0000001401"
FT ACT_SITE 212
FT /note="Nucleophile"
FT ACT_SITE 248
FT /note="Proton donor"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 210
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 313
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT BINDING 352
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P00687"
FT MOD_RES 365
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1710976"
FT MOD_RES 427
FT /note="Deamidated asparagine; partial; alternate"
FT /evidence="ECO:0000269|PubMed:1710976"
FT MOD_RES 474
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1710976"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:1710976"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..101
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT DISULFID 85..130
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT DISULFID 156..175
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT DISULFID 393..399
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT DISULFID 465..477
FT /evidence="ECO:0000269|PubMed:12527308,
FT ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD"
FT CONFLICT 285
FT /note="N -> T (in Ref. 8; AAA57345)"
FT /evidence="ECO:0000305"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 46..51
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1SMD"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1SMD"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:1SMD"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:3DHP"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:3DHP"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1SMD"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:3DHP"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:3DHP"
SQ SEQUENCE 511 AA; 57768 MW; 7710BCAC83EBE8B2 CRC64;
MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP
NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN
AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLSGL
LDLALGKDYV RSKIAEYMNH LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG
SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP
RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP
FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI
KIYVSDDGKA HFSISNSAED PFIAIHAESK L
