SCP51_ARATH
ID SCP51_ARATH Reviewed; 461 AA.
AC Q67Y83; Q680E1; Q945N4; Q9SJJ9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Serine carboxypeptidase-like 51;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL51; OrderedLocusNames=At2g27920; ORFNames=T1E2.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=15908604; DOI=10.1104/pp.104.057950;
RA Fraser C.M., Rider L.W., Chapple C.;
RT "An expression and bioinformatics analysis of the Arabidopsis serine
RT carboxypeptidase-like gene family.";
RL Plant Physiol. 138:1136-1148(2005).
CC -!- FUNCTION: Probable carboxypeptidase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67Y83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67Y83-2; Sequence=VSP_022854, VSP_022855;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, flowers and
CC siliques. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC006929; AAD21510.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08059.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08060.1; -; Genomic_DNA.
DR EMBL; AF412049; AAL06502.1; -; mRNA.
DR EMBL; BT003041; AAO23606.1; -; mRNA.
DR EMBL; AK175926; BAD43689.1; -; mRNA.
DR EMBL; AK176585; BAD44348.1; -; mRNA.
DR PIR; E84678; E84678.
DR RefSeq; NP_001031434.1; NM_001036357.1. [Q67Y83-2]
DR RefSeq; NP_565663.1; NM_128351.3. [Q67Y83-1]
DR AlphaFoldDB; Q67Y83; -.
DR SMR; Q67Y83; -.
DR STRING; 3702.AT2G27920.1; -.
DR ESTHER; arath-SCP51; Carboxypeptidase_S10.
DR MEROPS; S10.017; -.
DR PaxDb; Q67Y83; -.
DR PRIDE; Q67Y83; -.
DR ProteomicsDB; 232707; -. [Q67Y83-1]
DR EnsemblPlants; AT2G27920.1; AT2G27920.1; AT2G27920. [Q67Y83-1]
DR EnsemblPlants; AT2G27920.3; AT2G27920.3; AT2G27920. [Q67Y83-2]
DR GeneID; 817336; -.
DR Gramene; AT2G27920.1; AT2G27920.1; AT2G27920. [Q67Y83-1]
DR Gramene; AT2G27920.3; AT2G27920.3; AT2G27920. [Q67Y83-2]
DR KEGG; ath:AT2G27920; -.
DR Araport; AT2G27920; -.
DR TAIR; locus:2057873; AT2G27920.
DR eggNOG; KOG1283; Eukaryota.
DR HOGENOM; CLU_008523_1_0_1; -.
DR InParanoid; Q67Y83; -.
DR OMA; RWIQSTA; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q67Y83; -.
DR PRO; PR:Q67Y83; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q67Y83; baseline and differential.
DR Genevisible; Q67Y83; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carboxypeptidase; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..461
FT /note="Serine carboxypeptidase-like 51"
FT /id="PRO_0000274665"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022854"
FT VAR_SEQ 67..114
FT /note="IILWLQGGPGASGVGIGNFQEVGPLDTFLKPRNSTWLKKADLLFVDSP ->
FT MAYHPLAPRWTWSFRGWYREFSGGWTIRHISQAQKLNLVEESRSFVC (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022855"
FT CONFLICT 398
FT /note="G -> E (in Ref. 4; BAD43689)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="E -> V (in Ref. 4; BAD44348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51752 MW; 5C97456D1807CAAD CRC64;
MKTTVVYLVI LCLIVSCTNG ETKHVRKINS DGSEAWGYVE VRPKAHMFWW HYKSPYRVEN
PSKPWPIILW LQGGPGASGV GIGNFQEVGP LDTFLKPRNS TWLKKADLLF VDSPVGAGYS
FVEGNQKDLY VKSDEEAAQD LTKLLQQLFN KNQTLNQSPL FIVAESYGGK IAVKLGLSVI
DAVQSGKLKL HLGGVILGDS WISPEDFVFS WGPLLKHVSR LDDNGLDSSN SLAEKIKTQI
KNGEYVGATQ TWMDLENLIS SKSNFVDFYN FLLDTGMDPV SLTTSLKIKK EEKIKKYSRY
LNDMRSLSDV EDVEGDLDKL MNGVIKKKLK IIPNDLIWGN NSDDVFTAME AAFMKPVIED
VDELLATGVD VTIYNGQLDV ICSTSGTEAW VHKLRWEGLE EFKKMEREPL FCESDRATRG
FTKSYKNLHF YWILGAGHFV PVDEPCVALK MVGEITKSPQ L
