ID   B8LLS4_PICSI            Unreviewed;       434 AA.
AC   B8LLS4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Pectin acetylesterase {ECO:0000256|RuleBase:RU363114};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU363114};
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332 {ECO:0000313|EMBL:ABR16604.1};
RN   [1] {ECO:0000313|EMBL:ABR16604.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Green portion of the leader tissue
RC   {ECO:0000313|EMBL:ABR16604.1};
RA   Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA   Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA   Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT   "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes acetyl esters in homogalacturonan regions of
CC       pectin. In type I primary cell wall, galacturonic acid residues of
CC       pectin can be acetylated at the O-2 and O-3 positions. Decreasing the
CC       degree of acetylation of pectin gels in vitro alters their physical
CC       properties. {ECO:0000256|ARBA:ARBA00003534,
CC       ECO:0000256|RuleBase:RU363114}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004191, ECO:0000256|RuleBase:RU363114}.
CC   -!- SIMILARITY: Belongs to the pectinacetylesterase family.
CC       {ECO:0000256|ARBA:ARBA00005784, ECO:0000256|RuleBase:RU363114}.
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DR   EMBL; EF676719; ABR16604.1; -; mRNA.
DR   AlphaFoldDB; B8LLS4; -.
DR   ESTHER; picsi-b8lls4; Pectinacetylesterase-Notum.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR004963; PAE/NOTUM.
DR   PANTHER; PTHR21562; NOTUM-RELATED; 1.
DR   PANTHER; PTHR21562:SF5; PECTIN ACETYLESTERASE 12; 1.
DR   Pfam; PF03283; PAE; 1.
PE   2: Evidence at transcript level;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU363114};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|RuleBase:RU363114}; Hydrolase {ECO:0000256|RuleBase:RU363114};
KW   Secreted {ECO:0000256|RuleBase:RU363114}.
SQ   SEQUENCE   434 AA;  48179 MW;  0C5A60687A577D4A CRC64;
     MLLPMVTGRK MTRGSLDFEF ALFGVVLLVV MCIGKSETWE IGGRISSNVS EVSWEEAAVS
     YPPGALMVGL SLVKGAAEIG AVCLDGTLPG YHLSRGWGSG ANNWLIQLEG GGWCNDLRTC
     VYRKTTRRGS SRYMEREIVF SGILSNKRSE NPDFYNWNRV KLRYCDGASF AGDMEGENEV
     PKLYFRGQRI WRAAMADLLV EGMKNAQQAL LSGCSAGGLA SIIHCDDFRD LMPRSSKVKC
     LSDAGFFLDV MDVSGVHSLR SIYNGVVTMQ GVAKNLPRAC TSRMDPAQCF FPQHLLQDIK
     TPLFILNAGY DSWQILSSLV PTAADPQGHW HFCRLNPANC SASQLQVLQG FRMDMLNELR
     VLAGSRVGGM FINSCFAHCQ SERQDTWFAP DSPRLKKTIA ESVGDWYFDR SPSKEIDCAY
     PCDQTCHNLI FKSK
//