SCP18_ARATH
ID SCP18_ARATH Reviewed; 464 AA.
AC Q9C7Z9; F4HR86;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Serine carboxypeptidase-like 18;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL18; OrderedLocusNames=At1g33540; ORFNames=F10C21.18;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51208.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC051630; AAG51208.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31604.2; -; Genomic_DNA.
DR PIR; C86459; C86459.
DR RefSeq; NP_001319134.1; NM_001333051.1.
DR AlphaFoldDB; Q9C7Z9; -.
DR SMR; Q9C7Z9; -.
DR STRING; 3702.AT1G33540.1; -.
DR ESTHER; arath-SCP18; Carboxypeptidase_S10.
DR MEROPS; S10.A01; -.
DR PaxDb; Q9C7Z9; -.
DR PRIDE; Q9C7Z9; -.
DR EnsemblPlants; AT1G33540.1; AT1G33540.1; AT1G33540.
DR GeneID; 840248; -.
DR Gramene; AT1G33540.1; AT1G33540.1; AT1G33540.
DR KEGG; ath:AT1G33540; -.
DR Araport; AT1G33540; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9C7Z9; -.
DR OMA; ENSNRPM; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9C7Z9; -.
DR BioCyc; ARA:AT1G33540-MON; -.
DR PRO; PR:Q9C7Z9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7Z9; baseline and differential.
DR Genevisible; Q9C7Z9; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..464
FT /note="Serine carboxypeptidase-like 18"
FT /id="PRO_0000274632"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT ACT_SITE 389
FT /evidence="ECO:0000250"
FT ACT_SITE 442
FT /evidence="ECO:0000250"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..353
FT /evidence="ECO:0000250"
FT DISULFID 248..262
FT /evidence="ECO:0000250"
FT DISULFID 286..319
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 52300 MW; 1A73E0D86867858E CRC64;
MSKAWKLKLL LLLQLLLLSQ HDVDSASVIS YLPGFEGLLP FHLETGYIGV GEGEKVQLFY
YFIKSENNPE EDPLIIWLTG GPACTALSAL AFEIGPLTFK TEGYNGGLPS LVSTSYSWTK
VASIIFLDQP VGTGYSYSTT PLSYKPSDTG EAKQTYEFLQ KWLVENPQFV SNPIYVGGDS
YAGIVVPAIV QQISIGNEHG YKPQINLKGY ILGNPSTDLD SDHNSKIPYA HRMGLISDEL
YESLKRTCQG NYVKVDPTNT KCLKLMEDYG KCVSRINEGL ILIALCDLAS PNPYSGEHGG
RSYLQTLVQS DLSLPTPDCY MYRYLLASHW ANDEDVRREL HVVKGSIGKW MRCNWDLPYE
KDIKSSVPYH RNNSIIGDYR SLVYSSDHDM MVPYIGTEAW IKSLNYSITD DWRPWFVNNQ
VIGYTRTYAN NMTFATIKGG GHTAEYKPEE SFMMFQRWIS GRPL