SCP3_ARATH
ID SCP3_ARATH Reviewed; 441 AA.
AC Q9CAU1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine carboxypeptidase-like 3;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL3; OrderedLocusNames=At1g73280; ORFNames=T18K17.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC010556; AAG52138.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35437.1; -; Genomic_DNA.
DR PIR; A96759; A96759.
DR RefSeq; NP_177471.1; NM_105987.1.
DR AlphaFoldDB; Q9CAU1; -.
DR SMR; Q9CAU1; -.
DR STRING; 3702.AT1G73280.1; -.
DR ESTHER; arath-SCP3; Carboxypeptidase_S10.
DR MEROPS; S10.A05; -.
DR PaxDb; Q9CAU1; -.
DR PRIDE; Q9CAU1; -.
DR EnsemblPlants; AT1G73280.1; AT1G73280.1; AT1G73280.
DR GeneID; 843662; -.
DR Gramene; AT1G73280.1; AT1G73280.1; AT1G73280.
DR KEGG; ath:AT1G73280; -.
DR Araport; AT1G73280; -.
DR TAIR; locus:2197304; AT1G73280.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9CAU1; -.
DR OMA; IMFERWI; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9CAU1; -.
DR BioCyc; ARA:AT1G73280-MON; -.
DR PRO; PR:Q9CAU1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAU1; baseline and differential.
DR Genevisible; Q9CAU1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..441
FT /note="Serine carboxypeptidase-like 3"
FT /id="PRO_0000274617"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /evidence="ECO:0000250"
FT ACT_SITE 419
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..331
FT /evidence="ECO:0000250"
FT DISULFID 252..266
FT /evidence="ECO:0000250"
FT DISULFID 290..297
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 50279 MW; EFCDB4975F9D457F CRC64;
MASNYVFSVL RSLLLLIHTV FLGQHHVSSA TIIKSLPGFE GPLPFELETG YIGVGEEEEV
QLFYYFIKSE RNPKEDPLLL WLSGGPGCSS ISGLLFENGP LAMKLDVYNG TLPSLVSTTY
SWTKASSMIF LDQPVGAGFS YSRTQLLNKP SDSGEAKRIH EFLQKWLGKH QEFSSNPFYV
GGDSYSGMVV PATVQEISKG NYECCNPPIN LQGYVLGNPL TDFVYDYNSR IPFAHGMALI
SDELFESLKK TCKGDYRNVH PRNTECLKFI EEFNKCTNSI CQRRIIDPFC ETETPNCYIY
RFLLAAYWAN DETVRKALQI KKETIGEWVR CHYGIPYNYD IKSSIPYHMN NSINGYRSLI
YSGDHDFEVP FLGTQAWIRS LNYSVIDDWR PWMIKDQIAG YTRTYANKMT FATIRGGGHT
IEFKPEEASI MFQRWIKGQP L
