AMY4_SCHPO
ID AMY4_SCHPO Reviewed; 774 AA.
AC O42918; Q96WR2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-amylase 4;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Meiotic expression up-regulated protein 7;
DE Flags: Precursor;
GN Name=meu7; Synonyms=aah4; ORFNames=SPBC16A3.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 525-774.
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
RN [3]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [4]
RP GENE NAME.
RX PubMed=16751704; DOI=10.1271/bbb.50693;
RA Morita T., Tanaka N., Hosomi A., Giga-Hama Y., Takegawa K.;
RT "An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein
RT required for cell wall integrity and morphogenesis in Schizosaccharomyces
RT pombe.";
RL Biosci. Biotechnol. Biochem. 70:1454-1463(2006).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA16864.1; -; Genomic_DNA.
DR EMBL; AB054318; BAB60884.1; -; mRNA.
DR PIR; T39539; T39539.
DR RefSeq; NP_596776.1; NM_001023797.1.
DR AlphaFoldDB; O42918; -.
DR SMR; O42918; -.
DR BioGRID; 276301; 11.
DR STRING; 4896.SPBC16A3.13.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O42918; -.
DR EnsemblFungi; SPBC16A3.13.1; SPBC16A3.13.1:pep; SPBC16A3.13.
DR GeneID; 2539749; -.
DR KEGG; spo:SPBC16A3.13; -.
DR PomBase; SPBC16A3.13; meu7.
DR VEuPathDB; FungiDB:SPBC16A3.13; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_361368_0_0_1; -.
DR InParanoid; O42918; -.
DR OMA; PWKHEEH; -.
DR PhylomeDB; O42918; -.
DR PRO; PR:O42918; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISM:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; ISS:PomBase.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR015340; A_amylase_C_dom.
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; 2.
DR Pfam; PF09260; DUF1966; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Cell membrane; Disulfide bond;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..750
FT /note="Alpha-amylase 4"
FT /id="PRO_0000001356"
FT PROPEP 751..774
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000255454"
FT REGION 184..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT SITE 553
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 750
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..60
FT /evidence="ECO:0000250"
FT DISULFID 229..314
FT /evidence="ECO:0000250"
FT DISULFID 495..539
FT /evidence="ECO:0000250"
FT DISULFID 690..724
FT /evidence="ECO:0000250"
SQ SEQUENCE 774 AA; 89459 MW; 92CEAAE45664269B CRC64;
MKLSLKDLAL SIILVLGVAP PVQALSAEEW KKQSVYNVMT DRFATSKVVP HCDVKAEKYC
GGNWQGIVDH LDYIRDLGFT AISISPVVEQ LEGPEYHGEA YHGHRPKNYY RLNPHFGNEE
DLKELSDALH GKGMYLMVDV AINHTISEYF EDDYFKNTYF DKTHIDHKCK EHCSCHHDKF
PRPVPHNGTK PDHKPWKHEE HCHHGKFPRP VPHNGTKPDH KPWKHEEHCS CHHDKFPRPV
PHNGTKPDHK PWKHEEHCSC HHDKFPRPVP HNGTKPDHKP WKHEEHCHHG KFPRPIPHNG
TKPDHKPWKH EEHCHHGRFP RPVPHNGTKP DHKPWKHEEH CSCHHDKFSR PVPHNGTKPD
HKPWKHEEHC HHGKFLRPVP HNVTKPDHKP WKHEEHCHHG KFPRPVPHNG TKPDHKPWKH
EEHCSCHEDH SVHERPSAKG ALEDYIQTFV ETFQIDGIRF DAMGDKYRKY WPDFCKAAGV
FCMGDLKSSD SLKVCDWQND LEGLSNFPVR ESAVKAFLMN NPEGIVDLAD KMTDMRGLCV
NPLLLGNFVE NKDLPRMASI SSDPATLKNA IAFVLMGDGI PMMYNGQELA MRGEEVPYNR
PAIWEKGFPK RNPYYKFTST INRFRKAMIE SKDGEAFLNM QSDISIVDKR ILLLRRGKVI
TVLNNLGSYY IHFHYTVSAE EHKWMDVLSC KSVPVQDNRQ VFMVRNGEPM ILYPEESAYE
MGLCPSPIQL TEDYNSEGSL SINVEEAQTS KAPEQNRGFT NVLAALLLSL LMIL
