SCPL2_ARATH
ID SCPL2_ARATH Reviewed; 441 AA.
AC Q9CAU3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine carboxypeptidase-like 2;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL2; OrderedLocusNames=At1g73300; ORFNames=T18K17.3;
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=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 and roots.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC010556; AAG52135.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35439.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60225.1; -; Genomic_DNA.
DR PIR; C96759; C96759.
DR RefSeq; NP_001322525.1; NM_001334583.1.
DR RefSeq; NP_177473.1; NM_105989.2.
DR AlphaFoldDB; Q9CAU3; -.
DR SMR; Q9CAU3; -.
DR ESTHER; arath-SCP2; Carboxypeptidase_S10.
DR MEROPS; S10.A07; -.
DR MEROPS; S10.A16; -.
DR PaxDb; Q9CAU3; -.
DR PRIDE; Q9CAU3; -.
DR EnsemblPlants; AT1G73300.1; AT1G73300.1; AT1G73300.
DR EnsemblPlants; AT1G73300.2; AT1G73300.2; AT1G73300.
DR GeneID; 843664; -.
DR Gramene; AT1G73300.1; AT1G73300.1; AT1G73300.
DR Gramene; AT1G73300.2; AT1G73300.2; AT1G73300.
DR KEGG; ath:AT1G73300; -.
DR Araport; AT1G73300; -.
DR TAIR; locus:2197294; AT1G73300.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q9CAU3; -.
DR OMA; NPSNTEC; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q9CAU3; -.
DR BioCyc; ARA:AT1G73300-MON; -.
DR PRO; PR:Q9CAU3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR Genevisible; Q9CAU3; 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..441
FT /note="Serine carboxypeptidase-like 2"
FT /id="PRO_0000274616"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /evidence="ECO:0000250"
FT ACT_SITE 419
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..331
FT /evidence="ECO:0000250"
FT DISULFID 252..266
FT /evidence="ECO:0000250"
FT DISULFID 290..297
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 50265 MW; FD61EA4BD16D5FC0 CRC64;
MANKYFSSVL KSLLLLLHLV FLSKQHVDSA SIVKFLPGFE GPLPFELETG YIGIGEEEEV
QLFYYFIKSE RNPKEDPLIL WLTGGPGCSS ISGLLFENGP LTMKLDVYNG TLPSLVSTTY
SWTKTSSMIF LDQPVGTGFS YSRTQQFNKP SDSGEAKRIH EFLQKWLGKH QEFSSNPFYV
AGDSYSGLVV PATVQEISKG NYECCNPPIN LQGYVLGNPL TDYAIDSNSR IPFAHGMALI
SDELYESLKK TCKGEYTNVH PRNTQCLKFI EEFNKCTNRI LQQLILDPLC ETETPDCYIY
RYLLTTYWAN DATVREALQI NKESIGEWVR CYRTIPYDND IKSSMPYHVN NSISGYRSLI
YSGDHDLEVP YLGTQAWIRS LNYSIIDDWR PWMIKNQIAG YTRTYANKMT FATIKGGGHT
IEFKPEEASI MFQRWINGQP L
