SCP5_ARATH
ID SCP5_ARATH Reviewed; 438 AA.
AC Q9CAU2; F4HQ63;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine carboxypeptidase-like 5;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL5; OrderedLocusNames=At1g73290; ORFNames=T18K17.4;
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 seedlings, roots, and siliques.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010556; AAG52136.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35438.2; -; Genomic_DNA.
DR PIR; B96759; B96759.
DR RefSeq; NP_001319372.1; NM_001334580.1.
DR AlphaFoldDB; Q9CAU2; -.
DR SMR; Q9CAU2; -.
DR STRING; 3702.AT1G73290.1; -.
DR ESTHER; arath-SCP5; Carboxypeptidase_S10.
DR MEROPS; S10.A03; -.
DR PaxDb; Q9CAU2; -.
DR PRIDE; Q9CAU2; -.
DR ProteomicsDB; 226607; -.
DR EnsemblPlants; AT1G73290.1; AT1G73290.1; AT1G73290.
DR GeneID; 843663; -.
DR Gramene; AT1G73290.1; AT1G73290.1; AT1G73290.
DR KEGG; ath:AT1G73290; -.
DR Araport; AT1G73290; -.
DR TAIR; locus:2197299; AT1G73290.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9CAU2; -.
DR OMA; QIHKESK; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9CAU2; -.
DR BioCyc; ARA:AT1G73290-MON; -.
DR PRO; PR:Q9CAU2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAU2; baseline and differential.
DR Genevisible; Q9CAU2; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..438
FT /note="Serine carboxypeptidase-like 5"
FT /id="PRO_0000274619"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT ACT_SITE 363
FT /evidence="ECO:0000250"
FT ACT_SITE 416
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..328
FT /evidence="ECO:0000250"
FT DISULFID 251..263
FT /evidence="ECO:0000250"
FT DISULFID 287..294
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 49938 MW; 658B38457534F6C6 CRC64;
MANYISSVLK SLLLLLHLVF LIQQHVDSAS IVKFLPGFEG SLPFELETGY IGIGEEEEVQ
LFYYFIKSER NPKEDPLLLW LSGGPGCSSI SGLLFENGPL AMKLDVYNGT LPSLVPTTYS
WTKTSSMIFL DQPVGTGFSY SRTQQYNKPS DSGEAKRIHE FLQKWLSKHQ EFSSNPFYVA
GDSYSGMVVP ATVQEISKGN YQCCSPPINL QGYVLGNPIT EHAIDYNYRI PFAHGMALIS
DELYESLKRV CKGEYVDPRD TECLKLVEEF SKCTKGVCQE VVIKPLCVTE TPNCYIYRYL
LTTYWVNDVN VRKALQINKE SIGEWVRCYF GIPYTHDIKS SVPYHMNNSI NGYRSLIYSG
DHDLNVPFLA TQAWVRSLNY SIIDNWRPWM IKDQIGGYTK TYANKMTFAT VRGGGHTAEY
KPYETYIMFH RWINGQPL
