SCP15_ARATH
ID SCP15_ARATH Reviewed; 436 AA.
AC Q9C7D2; Q9LHI2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine carboxypeptidase-like 15;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL15; OrderedLocusNames=At3g12240; ORFNames=F28J15.111, F28J15.13;
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 seedlings and roots.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC069472; AAG51076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP002047; BAB03133.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75171.1; -; Genomic_DNA.
DR RefSeq; NP_187832.2; NM_112060.3.
DR AlphaFoldDB; Q9C7D2; -.
DR SMR; Q9C7D2; -.
DR STRING; 3702.AT3G12240.1; -.
DR ESTHER; arath-SCP15; Carboxypeptidase_S10.
DR MEROPS; S10.A02; -.
DR PaxDb; Q9C7D2; -.
DR PRIDE; Q9C7D2; -.
DR ProteomicsDB; 232818; -.
DR EnsemblPlants; AT3G12240.1; AT3G12240.1; AT3G12240.
DR GeneID; 820404; -.
DR Gramene; AT3G12240.1; AT3G12240.1; AT3G12240.
DR KEGG; ath:AT3G12240; -.
DR Araport; AT3G12240; -.
DR TAIR; locus:2082219; AT3G12240.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9C7D2; -.
DR OMA; YWADNET; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9C7D2; -.
DR BioCyc; ARA:AT3G12240-MON; -.
DR PRO; PR:Q9C7D2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C7D2; baseline and differential.
DR Genevisible; Q9C7D2; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..436
FT /note="Serine carboxypeptidase-like 15"
FT /id="PRO_0000274629"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..326
FT /evidence="ECO:0000250"
FT DISULFID 247..261
FT /evidence="ECO:0000250"
FT DISULFID 285..292
FT /evidence="ECO:0000250"
SQ SEQUENCE 436 AA; 49350 MW; 8F33AD3A8BBEF46C CRC64;
MASWIFKLLL LLQCVLVLIQ HADSSSIIRY LPGFEGPLPF ELETGYIGVG QKEEDQLFYY
FIKSENNPEE DPLLVWLTGG PGCSSFSGLV YENGPLAFKV ETYNGSVPTL VSTTYSWTKV
ANIIYLDQPV GTGFSYSRNP FADIPSDTGS VKRVNEFVRK WLAKHPEYFS NPFYVTGNSY
SGKVIPAIVQ EISNGNYICC KPQINLQGYV IGNPVAYYDH DKDFRIPFAH GVALISDELF
ESLKASCGGS YSVVDPLNTE CLKLIEDYDK CVSGIYEELI LKSKCEHTSP DCYTYRYLLS
EYWADNETVR RALKVVKGSK GTWERCDYRV LSNQDIKSSI PFHINNSIRG YRSLVISGDH
DMTIPFLGTQ AWIRSLNYSI TEKWRPWMIL DQVAGYTKTY ANKMTLATVK GGGHTLEYKP
EENSVLFKRW ISGQPL
