SCP47_ARATH
ID SCP47_ARATH Reviewed; 505 AA.
AC Q9FFB0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine carboxypeptidase-like 47;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL47; OrderedLocusNames=At5g22980; ORFNames=MRN17.21;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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, flowers and siliques.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AB005243; BAB10619.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93104.1; -; Genomic_DNA.
DR RefSeq; NP_197689.1; NM_122204.3.
DR AlphaFoldDB; Q9FFB0; -.
DR SMR; Q9FFB0; -.
DR STRING; 3702.AT5G22980.1; -.
DR ESTHER; arath-SCP47; Carboxypeptidase_S10.
DR MEROPS; S10.A44; -.
DR iPTMnet; Q9FFB0; -.
DR PaxDb; Q9FFB0; -.
DR PRIDE; Q9FFB0; -.
DR ProteomicsDB; 226611; -.
DR EnsemblPlants; AT5G22980.1; AT5G22980.1; AT5G22980.
DR GeneID; 832362; -.
DR Gramene; AT5G22980.1; AT5G22980.1; AT5G22980.
DR KEGG; ath:AT5G22980; -.
DR Araport; AT5G22980; -.
DR TAIR; locus:2172711; AT5G22980.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_1_1; -.
DR InParanoid; Q9FFB0; -.
DR OMA; HFYFWAF; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9FFB0; -.
DR PRO; PR:Q9FFB0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFB0; baseline and differential.
DR Genevisible; Q9FFB0; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
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; IPR033124; Ser_caboxypep_his_AS.
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; 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.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..505
FT /note="Serine carboxypeptidase-like 47"
FT /id="PRO_0000274662"
FT ACT_SITE 228
FT /evidence="ECO:0000250"
FT ACT_SITE 416
FT /evidence="ECO:0000250"
FT ACT_SITE 473
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138..378
FT /evidence="ECO:0000250"
FT DISULFID 306..321
FT /evidence="ECO:0000250"
FT DISULFID 344..349
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 56543 MW; 6E74CD351090B099 CRC64;
MEAKTFFLFM LFIFSQSWLS TSKRILNNPS VFSSSLNFSS GNAERLIKSF NLMPKYDVNV
IPKGSLDAPR LIERQIDFLA TAGSKNASVG PSVQEFGHYA GYYSLPHSKS AKMFYFFFES
RNKTTDPVVI WLTGGPGCSS SVAMFYENGP FKISKDLSLY WNDFGWDKVS NIIYVDQPVG
TGFSYTSDES DIRNDEDGVS NDLYDFLQAF FKEHPKFVKN DFFITGESYA GHYIPALASR
VHSGNKKKEG IPINLKGFAI GNGLTNPEIQ YGAYGDYALQ MKLISESDHE SLKQDYVECQ
NITKKCSLGG GLVCDSAVEV CTSIFNKIVA KKSGLNYYDI RKKCVGSLCY DFSRMEIFLN
KENVRKALGV GDIKFVSCSS TVYDAMIEDW MQNLEVKIPS LVNDGINLLV YAGEYDLICN
WLGNSRWVDQ MNWSGQKGFG SAKNVSFLVD GKEAGLLKNH GPLTFLKVYN AGHMVPMDQP
KASLQMLQNW MQGKLRTTPV LGFSQ
