SCP6_ARATH
ID SCP6_ARATH Reviewed; 452 AA.
AC Q9CAU0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine carboxypeptidase-like 6;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL6; OrderedLocusNames=At1g73270; ORFNames=T18K17.6;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CAU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CAU0-2; Sequence=VSP_041113;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and roots.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC010556; AAG52139.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35436.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57728.1; -; Genomic_DNA.
DR PIR; H96758; H96758.
DR RefSeq; NP_001320213.1; NM_001334576.1. [Q9CAU0-2]
DR RefSeq; NP_177470.4; NM_105986.4. [Q9CAU0-1]
DR AlphaFoldDB; Q9CAU0; -.
DR SMR; Q9CAU0; -.
DR STRING; 3702.AT1G73270.1; -.
DR ESTHER; arath-SCPL6; Carboxypeptidase_S10.
DR MEROPS; S10.A04; -.
DR PaxDb; Q9CAU0; -.
DR PRIDE; Q9CAU0; -.
DR ProteomicsDB; 232709; -. [Q9CAU0-1]
DR EnsemblPlants; AT1G73270.1; AT1G73270.1; AT1G73270. [Q9CAU0-1]
DR EnsemblPlants; AT1G73270.2; AT1G73270.2; AT1G73270. [Q9CAU0-2]
DR GeneID; 843661; -.
DR Gramene; AT1G73270.1; AT1G73270.1; AT1G73270. [Q9CAU0-1]
DR Gramene; AT1G73270.2; AT1G73270.2; AT1G73270. [Q9CAU0-2]
DR KEGG; ath:AT1G73270; -.
DR Araport; AT1G73270; -.
DR TAIR; locus:2197309; AT1G73270.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9CAU0; -.
DR OMA; NIWANDN; -.
DR OrthoDB; 607679at2759; -.
DR BioCyc; ARA:AT1G73270-MON; -.
DR PRO; PR:Q9CAU0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAU0; baseline and differential.
DR Genevisible; Q9CAU0; 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 Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..452
FT /note="Serine carboxypeptidase-like 6"
FT /id="PRO_0000274620"
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 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
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"
FT VAR_SEQ 442..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041113"
SQ SEQUENCE 452 AA; 51727 MW; E3B12E1DFE7A2FE8 CRC64;
MANDYISFVF KSLLLLIHLV FLGQHHVDSA SVVKSLPGFE GPLPFELETG YIGVGEEEEV
QLFYYFIKSE RNPKEDPLLL WLTGGPGCSA ISGLLYENGP LTMKLDVYNG TLPSLVSTTY
SWTKNSSMIF LDQPVGTGFS YSRTELFNKP SDTGEAKRIH EFLQKWLGKH QEFSSNPFYV
GGDSYSGITV PATVQEISKG NYQCCKPPIN LQGYMLGNPI TDSKIDGNSQ IPYAHGMALI
SDELYESLKR ICKGEYEHVD PYNTECLKLL EEFNECTSKL YRSHILYPLC EMTNPDCYIY
RYSLSHYWVN DETVRKALQI NKESIREWKR CDWSKPYTKD IISSVPYHMN NSINGYRSLI
FSGDHDFEVP LIGTQVWIKS LNYAIVDKWR PWMINNQVAG YTRTYANKMT FATVKGGGHT
AEYKPDETFI MFQRWINGQA LYGKVKLLQK TE
