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SUN1_ASPFU
ID   SUN1_ASPFU              Reviewed;         414 AA.
AC   Q4WGL5;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Secreted beta-glucosidase sun1;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=sun1; ORFNames=AFUA_7G05450;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, GLYCOSYLATION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23508952; DOI=10.1074/jbc.m112.440172;
RA   Gastebois A., Aimanianda V., Bachellier-Bassi S., Nesseir A., Firon A.,
RA   Beauvais A., Schmitt C., England P., Beau R., Prevost M.C., d'Enfert C.,
RA   Latge J.P., Mouyna I.;
RT   "SUN proteins belong to a novel family of beta-(1,3)-glucan-modifying
RT   enzymes involved in fungal morphogenesis.";
RL   J. Biol. Chem. 288:13387-13396(2013).
CC   -!- FUNCTION: Cell surface beta-glucosidase involved in cell wall
CC       biosynthesis and septation, and thus required for normal growth and
CC       correct hyphal morphogenesis. Has hydrolytic activity on linear (1->3)-
CC       beta-D-glucans such as laminaribiose and other
CC       laminarioligosaccharides. Has also a minor transferase activity.
CC       {ECO:0000269|PubMed:23508952}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:23508952};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:23508952};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted.
CC   -!- INDUCTION: Expression was detected 4h after the initiation of spore
CC       germination and during mycelial growth. {ECO:0000269|PubMed:23508952}.
CC   -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:23508952}.
CC   -!- DISRUPTION PHENOTYPE: Leads to smaller colonies and swollen and
CC       vacuolated hyphae with double cell wall and leaky tips. Leads also to
CC       decreased conidiation. {ECO:0000269|PubMed:23508952}.
CC   -!- SIMILARITY: Belongs to the SUN family. {ECO:0000305}.
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DR   EMBL; AAHF01000009; EAL86926.1; -; Genomic_DNA.
DR   RefSeq; XP_748964.1; XM_743871.1.
DR   AlphaFoldDB; Q4WGL5; -.
DR   SMR; Q4WGL5; -.
DR   STRING; 746128.CADAFUBP00008850; -.
DR   CAZy; GH132; Glycoside Hydrolase Family 132.
DR   CLAE; EXG132A_ASPFU; -.
DR   EnsemblFungi; EAL86926; EAL86926; AFUA_7G05450.
DR   GeneID; 3506240; -.
DR   KEGG; afm:AFUA_7G05450; -.
DR   VEuPathDB; FungiDB:Afu7g05450; -.
DR   eggNOG; ENOG502QPVV; Eukaryota.
DR   HOGENOM; CLU_033459_1_0_1; -.
DR   InParanoid; Q4WGL5; -.
DR   OMA; CSYACQS; -.
DR   OrthoDB; 1130819at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:AspGD.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0006076; P:(1->3)-beta-D-glucan catabolic process; IDA:AspGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR   InterPro; IPR005556; SUN.
DR   Pfam; PF03856; SUN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall; Cell wall biogenesis/degradation;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..414
FT                   /note="Secreted beta-glucosidase sun1"
FT                   /id="PRO_0000425080"
FT   REGION          115..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  43504 MW;  D99C641D515F8824 CRC64;
     MKFNTVALTL ATAGSLVTAQ HHHQHRHHQH KREDVVESSA TVVQYELDGK PISLKQVCAG
     LADNTLKFAN NDHPTGICDN LSSAAAPAST PEVTSAFAPA QFIELSSVVT SATPTSASSS
     ETVQTPAASS SSASSSSTAT GLDADFPDGE LDCSTFPSEY GAIPLDYLKL GGWSGIQYVS
     YAGNFINDIV TAVAGDTCKD GAMCSYACPP GYQKSQWPST QGATGQSVGG IECRNGKLHL
     TNPSLSKKLC IPGVGGVHVQ NTLGETVAVC RTDYPGTESE TIPIGLGGND LQPLTCPDGE
     TYYKWQGKTT SAQYYVNPKG VTPEKGCQWG DGTQPIGNWA PVNLGVGLNK GKWLSIFQNS
     PTTSEKLDFN IKIKGDNLSG SCKYENGVFY SETGSSSSGC TVQVMSGDAT FVFY
 
 
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