SCP7_ARATH
ID SCP7_ARATH Reviewed; 437 AA.
AC Q9SQX6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine carboxypeptidase-like 7;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL7; OrderedLocusNames=At3g10450; ORFNames=F13M14.27, F18K10.3;
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=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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SQX6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC011560; AAG51371.1; -; Genomic_DNA.
DR EMBL; AC013428; AAF76347.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74908.1; -; Genomic_DNA.
DR EMBL; AY088751; AAM67067.1; -; mRNA.
DR RefSeq; NP_187656.1; NM_111880.5. [Q9SQX6-1]
DR AlphaFoldDB; Q9SQX6; -.
DR SMR; Q9SQX6; -.
DR STRING; 3702.AT3G10450.1; -.
DR ESTHER; arath-SCP7; Carboxypeptidase_S10.
DR MEROPS; S10.A15; -.
DR PaxDb; Q9SQX6; -.
DR ProteomicsDB; 232749; -. [Q9SQX6-1]
DR EnsemblPlants; AT3G10450.1; AT3G10450.1; AT3G10450. [Q9SQX6-1]
DR GeneID; 820209; -.
DR Gramene; AT3G10450.1; AT3G10450.1; AT3G10450. [Q9SQX6-1]
DR KEGG; ath:AT3G10450; -.
DR Araport; AT3G10450; -.
DR TAIR; locus:2075755; AT3G10450.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9SQX6; -.
DR OMA; QWANDES; -.
DR PhylomeDB; Q9SQX6; -.
DR BioCyc; ARA:AT3G10450-MON; -.
DR PRO; PR:Q9SQX6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQX6; baseline and differential.
DR Genevisible; Q9SQX6; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..437
FT /note="Serine carboxypeptidase-like 7"
FT /id="PRO_0000274621"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..327
FT /evidence="ECO:0000250"
FT DISULFID 248..262
FT /evidence="ECO:0000250"
FT DISULFID 286..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 49565 MW; BE816006FA0B720D CRC64;
MANDYVSTVL LLLSLLIFLS QRTDSASIVK SLPGFDGPLP FELETGYIGV GEEEEVQLFY
YFIKSERNPQ EDPLLLWLSG GPGCSSISGL LYENGPVNVK IEVYNGTLPS LVSTTYSWTK
VSSIIYLDQP VGTGFSYSRT KLVNKPSDSG EAKRIHEFLH KWLGKHQEFS SNPFYVGGDS
YCGMVIPALV QEISKGNYVC CKPPINLQGY ILGNPSTENE VDINYRIPYA HGMALISDEL
YESMKRICKG KYENVDPRNT KCLKLVGEYQ KCTKRINKAL IITPECVDTS PDCYMYRYLL
TTYWANDENV QRALHVNKGS IGEWVRCYFE IPYNHDIKSS VPYHMNNSID GYASLIFSGD
HDMEVPYLGT QAWIRSLNYS LIDDWRPWMI GDQIAGYTRT YANKMAFATI KGGGHTPEYK
PEESYIMFQR WISGQPL
