SCP14_ARATH
ID SCP14_ARATH Reviewed; 435 AA.
AC Q9C7D3; Q9LHI3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine carboxypeptidase-like 14;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL14; OrderedLocusNames=At3g12230; ORFNames=F28J15.110, F28J15.14;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 senescent leaves.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC069472; AAG51078.1; -; Genomic_DNA.
DR EMBL; AP002047; BAB03132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75170.1; -; Genomic_DNA.
DR RefSeq; NP_187831.1; NM_112059.2.
DR AlphaFoldDB; Q9C7D3; -.
DR SMR; Q9C7D3; -.
DR STRING; 3702.AT3G12230.1; -.
DR ESTHER; arath-SCP14; Carboxypeptidase_S10.
DR MEROPS; S10.A02; -.
DR PaxDb; Q9C7D3; -.
DR PRIDE; Q9C7D3; -.
DR ProteomicsDB; 232817; -.
DR EnsemblPlants; AT3G12230.1; AT3G12230.1; AT3G12230.
DR GeneID; 820403; -.
DR Gramene; AT3G12230.1; AT3G12230.1; AT3G12230.
DR KEGG; ath:AT3G12230; -.
DR Araport; AT3G12230; -.
DR TAIR; locus:2082229; AT3G12230.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9C7D3; -.
DR OMA; WLSHEPL; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9C7D3; -.
DR BioCyc; ARA:AT3G12230-MON; -.
DR PRO; PR:Q9C7D3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C7D3; baseline and differential.
DR Genevisible; Q9C7D3; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..435
FT /note="Serine carboxypeptidase-like 14"
FT /id="PRO_0000274628"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..325
FT /evidence="ECO:0000250"
FT DISULFID 246..260
FT /evidence="ECO:0000250"
FT DISULFID 284..291
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 49020 MW; 0891A9867576CE06 CRC64;
MGSWIPKLLL LQLVLLLTKH ADSSSIIKYL PGFEGPLPFE LETGYIGVGD EDEDQMFYYF
IKSESNPEED PLLVWLSGGP GCSSFTGLVY ENGPLGFKVE AYNGSIPTLV STTYSWTKVA
NIIYLDQPVG AGFSYSRNPF ADRPSDTGSA KLVNEFVRKW LAKHPDYFSN PFYVTGNSYS
GKVIPAIVQE ISNGNYICCK PQINLQGYVI GNPVAYYDHD KDSRIPFAHG VALISDELFE
SLKRSCGGSY SIVDPLNTEC LKLIKDYHKC VSGIYQELIL KPKCETTSPD CYTYRYLLSI
YWANNEIVRR ALKVVEGSKG KWERCDLSVR SNQDIKSSIP YHMNNSIKGY RSLVISGDHD
MTIPFLGTQA WIRSLNYSIT EKWRPWMILD QVAGYTKTYA NKMTLATVKG GGHTLEYKPE
ENSILFKRWI SGQPL
