SCP1_ARATH
ID SCP1_ARATH Reviewed; 441 AA.
AC Q8RWJ6; Q9LVX9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine carboxypeptidase-like 1;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL1; OrderedLocusNames=At5g36180; ORFNames=MAB16.13;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=BAA96893.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018112; BAA96893.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94054.1; -; Genomic_DNA.
DR EMBL; AY093044; AAM13043.1; -; mRNA.
DR EMBL; AY128925; AAM91325.1; -; mRNA.
DR RefSeq; NP_198467.2; NM_123009.4.
DR AlphaFoldDB; Q8RWJ6; -.
DR SMR; Q8RWJ6; -.
DR STRING; 3702.AT5G36180.1; -.
DR ESTHER; arath-Q9LVX9; Carboxypeptidase_S10.
DR MEROPS; S10.A07; -.
DR PaxDb; Q8RWJ6; -.
DR PRIDE; Q8RWJ6; -.
DR EnsemblPlants; AT5G36180.1; AT5G36180.1; AT5G36180.
DR GeneID; 833615; -.
DR Gramene; AT5G36180.1; AT5G36180.1; AT5G36180.
DR KEGG; ath:AT5G36180; -.
DR Araport; AT5G36180; -.
DR TAIR; locus:2158946; AT5G36180.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_0_1_1; -.
DR InParanoid; Q8RWJ6; -.
DR OMA; RTHIANK; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q8RWJ6; -.
DR BioCyc; ARA:AT5G36180-MON; -.
DR PRO; PR:Q8RWJ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWJ6; baseline and differential.
DR Genevisible; Q8RWJ6; 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 1"
FT /id="PRO_0000274615"
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; 49986 MW; 794F540FB5649258 CRC64;
MANKYVSSVL KSLLVLLHLV FLSKQHVDSA SIVKSLPGFE GQLPFELETG YIGVGEEEEV
QLFYYFIKSE RNPKEDPLIL WLTGGPGCSA ISGLLFENGP LTMKLDVYNG TLPSLVSTTY
SWTKTSSIIF LDQPVGTGFS YSRTQQFNKP SDSGEAKRIH EFLQKWLGKH QVFSSNPFYV
AGDSYSGLVV PATVQEISKG NYECCNPPIN LQGYVLGNPL TDYTTGSNSR IPFAHGMALI
SDELYESLKK TCKGEYTNVH PRNTQCLKFV EEFNKCTNRI FQQLILDPLC ETETPDCYIY
RYLLTTYWAN DATVREALQI NKESIGEWVR CYYSIPYNND IKSSMPYHVN NSISGYRSLI
YSGDHDFEVP YLGTQAWIRS LNYSIIDDWR PWMVKNQIAG YTRTYANKMT FATIKGGGHT
AESKPEEASI MFQRWINGQP L
