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GUN8_ARATH
ID   GUN8_ARATH              Reviewed;         492 AA.
AC   Q9CAC1; O23696; O23697;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Endoglucanase 8;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 1;
DE            Short=AtCEL1;
DE   AltName: Full=Endo-1,4-beta glucanase 8;
DE   Flags: Precursor;
GN   Name=CEL1; OrderedLocusNames=At1g70710; ORFNames=F5A18.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=9290636; DOI=10.1023/a:1005849627301;
RA   Shani Z., Dekel M., Tsabary G., Shoseyov O.;
RT   "Cloning and characterization of elongation specific endo-1,4-beta-
RT   glucanase (cel1) from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 34:837-842(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=12602880; DOI=10.1023/a:1021162321527;
RA   Tsabary G., Shani Z., Roiz L., Levy I., Riov J., Shoseyov O.;
RT   "Abnormal 'wrinkled' cell walls and retarded development of transgenic
RT   Arabidopsis thaliana plants expressing endo-1,4-beta-glucanase (cell)
RT   antisense.";
RL   Plant Mol. Biol. 51:213-224(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=15170254; DOI=10.1007/s00239-003-2571-x;
RA   Libertini E., Li Y., McQueen-Mason S.J.;
RT   "Phylogenetic analysis of the plant endo-beta-1,4-glucanase gene family.";
RL   J. Mol. Evol. 58:506-515(2004).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=16758197; DOI=10.1007/s00299-006-0167-9;
RA   Shani Z., Dekel M., Roiz L., Horowitz M., Kolosovski N., Lapidot S.,
RA   Alkan S., Koltai H., Tsabary G., Goren R., Shoseyov O.;
RT   "Expression of endo-1,4-beta-glucanase (cel1) in Arabidopsis thaliana is
RT   associated with plant growth, xylem development and cell wall thickening.";
RL   Plant Cell Rep. 25:1067-1074(2006).
CC   -!- FUNCTION: Required for cellulose formation of the cell wall.
CC       {ECO:0000269|PubMed:12602880}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in young expanding tissues. Expressed in
CC       xylem cells, young epidermal cells and newly formed cell walls.
CC       {ECO:0000269|PubMed:16758197, ECO:0000269|PubMed:9290636}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA67156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X98543; CAA67156.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X98544; CAA67157.1; -; mRNA.
DR   EMBL; AC011663; AAG52329.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35103.1; -; Genomic_DNA.
DR   EMBL; AY048283; AAK82545.1; -; mRNA.
DR   EMBL; AY074552; AAL67092.1; -; mRNA.
DR   PIR; E96731; E96731.
DR   RefSeq; NP_177228.1; NM_105739.4.
DR   AlphaFoldDB; Q9CAC1; -.
DR   SMR; Q9CAC1; -.
DR   BioGRID; 28628; 2.
DR   STRING; 3702.AT1G70710.1; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   PaxDb; Q9CAC1; -.
DR   PRIDE; Q9CAC1; -.
DR   ProteomicsDB; 247152; -.
DR   EnsemblPlants; AT1G70710.1; AT1G70710.1; AT1G70710.
DR   GeneID; 843408; -.
DR   Gramene; AT1G70710.1; AT1G70710.1; AT1G70710.
DR   KEGG; ath:AT1G70710; -.
DR   Araport; AT1G70710; -.
DR   TAIR; locus:2033600; AT1G70710.
DR   eggNOG; ENOG502QR9R; Eukaryota.
DR   HOGENOM; CLU_008926_1_2_1; -.
DR   InParanoid; Q9CAC1; -.
DR   OMA; YLSHANH; -.
DR   OrthoDB; 1195424at2759; -.
DR   PhylomeDB; Q9CAC1; -.
DR   BioCyc; ARA:AT1G70710-MON; -.
DR   PRO; PR:Q9CAC1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAC1; baseline and differential.
DR   Genevisible; Q9CAC1; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; ISS:TAIR.
DR   GO; GO:0042547; P:cell wall modification involved in multidimensional cell growth; IMP:TAIR.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..492
FT                   /note="Endoglucanase 8"
FT                   /id="PRO_0000249261"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        13
FT                   /note="L -> H (in Ref. 1; CAA67157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="D -> N (in Ref. 1; CAA67156)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="V -> D (in Ref. 1; CAA67157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="L -> W (in Ref. 1; CAA67156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  54610 MW;  7FDA753A52B97E88 CRC64;
     MARKSLIFPV ILLAVLLFSP PIYSAGHDYR DALRKSILFF EGQRSGKLPP DQRLKWRRDS
     ALRDGSSAGV DLSGGYYDAG DNIKFGFPMA FTTTMLSWSI IDFGKTMGPE LRNAVKAVKW
     GTDYLLKATA IPGVVFVQVG DAYSDHNCWE RPEDMDTLRT VYKIDRAHPG SDVAGETAAA
     LAAASIVFRK RDPAYSRLLL DRATRVFAFA NRYRGAYSNS LYHAVCPFYC DFNGYQDELL
     WGAAWLHKAS RKRAYREFIV KNEVILKAGD TINEFGWDNK HAGINVLISK EVLMGKAEYF
     ESFKQNADGF ICSILPGISH PQVQYSRGGL LVKTGGSNMQ HVTSLSFLLL AYSNYLSHAK
     KVVPCGELTA SPSLLRQIAK RQVDYILGDN PMGLSYMVGY GQKFPRRIHH RGSSVPSVSA
     HPSHIGCKEG SRYFLSPNPN PNLLVGAVVG GPNVTDAFPD SRPYFQQSEP TTYINAPLVG
     LLGYFSAHST WR
 
 
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