ID SCP49_ARATH Reviewed; 516 AA.
AC P32826; Q42107; Q9CAE5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Serine carboxypeptidase-like 49;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL49; OrderedLocusNames=At3g10410; ORFNames=F13M14.32;
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16668828; DOI=10.1104/pp.98.4.1526;
RA Bradley D.;
RT "Isolation and characterization of a gene encoding a carboxypeptidase Y-
RT like protein from Arabidopsis thaliana.";
RL Plant Physiol. 98:1526-1529(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-372 AND 455-516.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
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 -!- TISSUE SPECIFICITY: Expressed in roots, senescent leaves and flowers.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04606.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M81130; AAB04606.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011560; AAG51389.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74902.1; -; Genomic_DNA.
DR EMBL; AY091767; AAM10315.1; -; mRNA.
DR EMBL; AY149954; AAN31108.1; -; mRNA.
DR EMBL; Z25955; CAA81115.1; -; mRNA.
DR EMBL; Z26528; CAA81299.1; -; mRNA.
DR RefSeq; NP_187652.1; NM_111876.5.
DR AlphaFoldDB; P32826; -.
DR SMR; P32826; -.
DR BioGRID; 5539; 3.
DR IntAct; P32826; 2.
DR STRING; 3702.P32826; -.
DR ESTHER; arath-SCP49; Carboxypeptidase_S10.
DR MEROPS; S10.A45; -.
DR GlyCosmos; P32826; 1 site, No reported glycans.
DR SwissPalm; P32826; -.
DR PaxDb; 3702-AT3G10410-1; -.
DR ProteomicsDB; 232705; -.
DR EnsemblPlants; AT3G10410.1; AT3G10410.1; AT3G10410.
DR GeneID; 820205; -.
DR Gramene; AT3G10410.1; AT3G10410.1; AT3G10410.
DR KEGG; ath:AT3G10410; -.
DR Araport; AT3G10410; -.
DR TAIR; AT3G10410; SCPL49.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; P32826; -.
DR OMA; TSCDDTV; -.
DR OrthoDB; 1647009at2759; -.
DR PhylomeDB; P32826; -.
DR PRO; PR:P32826; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P32826; baseline and differential.
DR Genevisible; P32826; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..82
FT /evidence="ECO:0000255"
FT /id="PRO_0000004333"
FT CHAIN 83..516
FT /note="Serine carboxypeptidase-like 49"
FT /id="PRO_0000004334"
FT ACT_SITE 229
FT /evidence="ECO:0000250"
FT ACT_SITE 417
FT /evidence="ECO:0000250"
FT ACT_SITE 474
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..379
FT /evidence="ECO:0000250"
FT DISULFID 307..322
FT /evidence="ECO:0000250"
FT DISULFID 345..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 57301 MW; 177C778DF657A1C1 CRC64;
MEKLTFLSLL LHFVVFIAST IPSSSFLLND RTFERSNLPS TRAEKLIREL NLFPQQDLNV
IDVADLPLTA AEGPGIVERK FVFPNILADG GPTVDDLGHH AGYYKLPKSR GASMFYFFFE
SRNKKDAPVV IWLTGGPGCS SELAVFYENG PFKITSNMSL AWNEYGWDQV SNLLYVDQPV
GTGFSYTTDK SDIRHDETGV SNDLYDFLQA FFAEHPKLAK NDFYITGESY AGHYIPAFAS
RVHKGNKANE GVHINLKGFA IGNGLTDPAL QYPAYPDYAL EMGLITQKEH DRLEKIVPLC
ELSIKLCGTD GTTSCLASYL VCNSLFSGVM SHAGGVNYYD IRKKCVGSLC YDFSNMEKFL
NLQSVRKSLG VGDIDFVSCS TSVYQAMLVD WMRNLEVGIP TLLEDGISLL VYAGEYDLIC
NWLGNSRWVN AMEWSGKTNF GAAKEVPFIV DGKEAGLLKT YEQLSFLKVR DAGHMVPMDQ
PKAALKMLKR WMENSLIEDA TVTVAAQGGE ELVAQM
//
