MAN7_ARATH
ID MAN7_ARATH Reviewed; 431 AA.
AC Q9FJZ3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase 7;
DE EC=3.2.1.78;
DE AltName: Full=Beta-mannanase 7;
DE AltName: Full=Endo-beta-1,4-mannanase 7;
DE Short=AtMAN7;
DE Flags: Precursor;
GN Name=MAN7; OrderedLocusNames=At5g66460; ORFNames=K1F13.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
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 [4]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=16897088; DOI=10.1007/s10142-006-0034-3;
RA Yuan J.S., Yang X., Lai J., Lin H., Cheng Z.-M., Nonogaki H., Chen F.;
RT "The endo-beta-mannanase gene families in Arabidopsis, rice, and poplar.";
RL Funct. Integr. Genomics 7:1-16(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP GIBBERELLIN.
RX PubMed=23461773; DOI=10.1111/tpj.12162;
RA Iglesias-Fernandez R., Barrero-Sicilia C., Carrillo-Barral N.,
RA Onate-Sanchez L., Carbonero P.;
RT "Arabidopsis thaliana bZIP44: a transcription factor affecting seed
RT germination and expression of the mannanase-encoding gene AtMAN7.";
RL Plant J. 74:767-780(2013).
CC -!- FUNCTION: Required for both, loosening of the micropylar endosperm, and
CC rupture of the seed coat in germinating seeds. May participate in the
CC hydrolysis of the mannans in the cell wall of germinating seeds.
CC {ECO:0000269|PubMed:23461773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23461773,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, siliques and seeds
CC (PubMed:16897088). Expressed in root vasculature, leaf hydathodes,
CC anther filaments, stigma, sepal vasculature, at the base and apical
CC parts of siliques, and replum. Expressed in the micropylar endosperm
CC and radicle tip in early germinating seeds (PubMed:23461773).
CC {ECO:0000269|PubMed:16897088, ECO:0000269|PubMed:23461773}.
CC -!- INDUCTION: By gibberellin in germinating seeds.
CC {ECO:0000269|PubMed:23461773}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AB013389; BAB10922.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98217.1; -; Genomic_DNA.
DR EMBL; BT000452; AAN17429.1; -; mRNA.
DR EMBL; BT008749; AAP49511.1; -; mRNA.
DR RefSeq; NP_201447.1; NM_126044.4.
DR AlphaFoldDB; Q9FJZ3; -.
DR SMR; Q9FJZ3; -.
DR BioGRID; 22020; 1.
DR IntAct; Q9FJZ3; 2.
DR STRING; 3702.AT5G66460.1; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; Q9FJZ3; -.
DR PRIDE; Q9FJZ3; -.
DR ProteomicsDB; 238235; -.
DR EnsemblPlants; AT5G66460.1; AT5G66460.1; AT5G66460.
DR GeneID; 836778; -.
DR Gramene; AT5G66460.1; AT5G66460.1; AT5G66460.
DR KEGG; ath:AT5G66460; -.
DR Araport; AT5G66460; -.
DR TAIR; locus:2154905; AT5G66460.
DR eggNOG; ENOG502QS4Q; Eukaryota.
DR HOGENOM; CLU_031603_0_0_1; -.
DR InParanoid; Q9FJZ3; -.
DR OMA; EAPWQKT; -.
DR OrthoDB; 1003648at2759; -.
DR PhylomeDB; Q9FJZ3; -.
DR BioCyc; ARA:AT5G66460-MON; -.
DR BRENDA; 3.2.1.78; 399.
DR PRO; PR:Q9FJZ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJZ3; baseline and differential.
DR Genevisible; Q9FJZ3; AT.
DR GO; GO:0071944; C:cell periphery; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:TAIR.
DR GO; GO:0010047; P:fruit dehiscence; IGI:TAIR.
DR GO; GO:1990059; P:fruit valve development; IGI:TAIR.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR GO; GO:0009828; P:plant-type cell wall loosening; IGI:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; PTHR31451; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..431
FT /note="Mannan endo-1,4-beta-mannosidase 7"
FT /id="PRO_0000277480"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B3A0S5"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:B3A0S5"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ SEQUENCE 431 AA; 48573 MW; FA5BB16113E0F3DF CRC64;
MKLLALFPFL AIVIQLSCWE LGTDALPSGG FVRTKGVQFS LNGYPYYANG FNAYWLMYVA
SDPSQRSKIS TAFQDASRHG LTVARTWAFS DGGYRALQYS PGSYNEDMFQ GLDFALAEAR
RHGIKIILSF ANNYESFGGR KQYVDWARSR GRPVSSEDDF FTDSLVKDFY KNHIKAVLNR
FNTFTKVHYK DDPTIMAWEL MNEPRCPSDP SGRAIQAWIT EMAAHVKSLD RNHLLEAGLE
GFYGQSSPQS KTLNPPGQFG TDFIANNRIP GIDFVTVHSY PDEWFPDSSE QSQMDFLNKW
LDAHIQDAQN VLHKPIILAE FGKSMKKPGY TPAQRDIVFN TVYSKIYGSA KRGGAAAGGL
FWQLLVNGID NFQDGYGIIL SQSSSTVNVI SQQSRKLTLI RKIFARMINV EKWKRARGQG
QVGKRGHKIN N
