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Protein

Putative serine carboxypeptidase-like 30

Gene

SCPL30

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Probable carboxypeptidase.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei192 – 1921PROSITE-ProRule annotation
Active sitei405 – 4051PROSITE-ProRule annotation
Active sitei457 – 4571PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciARA:AT4G15100-MONOMER.

Protein family/group databases

ESTHERiarath-AT4G15100. Carboxypeptidase_S10.
MEROPSiS10.A27.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative serine carboxypeptidase-like 30 (EC:3.4.16.-)
Gene namesi
Name:SCPL30
Ordered Locus Names:At4g15100
ORF Names:dl3595w, FCAALL.186
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G15100.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 488460Putative serine carboxypeptidase-like 30PRO_0000274645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi99 ↔ 368By similarity
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi262 ↔ 275By similarity
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi299 ↔ 336By similarity
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO23364.
PRIDEiO23364.

PTM databases

iPTMnetiO23364.

Expressioni

Tissue specificityi

Expression not detected.

Gene expression databases

GenevisibleiO23364. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G15100.1.

Structurei

3D structure databases

ProteinModelPortaliO23364.
SMRiO23364. Positions 39-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.
HOGENOMiHOG000198295.
InParanoidiO23364.
KOiK16297.
OMAiETHRNIN.
PhylomeDBiO23364.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O23364-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNHTKSFSS LLISLWFTAL LILVEMVSCA RQHRRSFLAK EADLVTNLPG
60 70 80 90 100
QPDVSFKHYA GYVPVDKSNG RALFYWFFEA MDLPKEKPLV LWLNGGPGCS
110 120 130 140 150
SVGYGATQEI GPFLADTNEK GLIFNPYAWN KEVNMLFLES PVGVGFSYSN
160 170 180 190 200
TSSDYLNLDD HFAKKDAYTF LCNWFEKFPE HKGNEFYIAG ESYAGIYVPE
210 220 230 240 250
LAELVYDNNE KNNDLSLHIN LKGFLLGNPD ISNPDDWRGW VDYAWSHAVI
260 270 280 290 300
SDETHRNINR LCNFSSDDVW NNDKCNEAIA EVDKQYNEID IYSLYTSACK
310 320 330 340 350
GDSAKSSYFA SAQFKTNYHI SSKRMPPRRL AGYDPCLDDY VKVYYNRADV
360 370 380 390 400
QKALHASDGV NLKNWSICNM EIFHNWTYVV QSVLPIYQKL IAGGLRIWVY
410 420 430 440 450
SGDTDGCIPV LGTRYSLNAL GLPIKTAWRP WYHEKQVSGW VQEYDGLTFA
460 470 480
TFRGAGHTVP SFKPSSSLAF ISAFVKGVPL SSSRVETN
Length:488
Mass (Da):55,259
Last modified:February 6, 2007 - v2
Checksum:iA51A5A3698569F63
GO

Sequence cautioni

The sequence CAB10289.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78552.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97337 Genomic DNA. Translation: CAB10289.1. Sequence problems.
AL161540 Genomic DNA. Translation: CAB78552.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83556.1.
PIRiG71414.
RefSeqiNP_193246.2. NM_117599.2.
UniGeneiAt.54330.

Genome annotation databases

EnsemblPlantsiAT4G15100.1; AT4G15100.1; AT4G15100.
GeneIDi827176.
GrameneiAT4G15100.1; AT4G15100.1; AT4G15100.
KEGGiath:AT4G15100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97337 Genomic DNA. Translation: CAB10289.1. Sequence problems.
AL161540 Genomic DNA. Translation: CAB78552.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83556.1.
PIRiG71414.
RefSeqiNP_193246.2. NM_117599.2.
UniGeneiAt.54330.

3D structure databases

ProteinModelPortaliO23364.
SMRiO23364. Positions 39-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G15100.1.

Protein family/group databases

ESTHERiarath-AT4G15100. Carboxypeptidase_S10.
MEROPSiS10.A27.

PTM databases

iPTMnetiO23364.

Proteomic databases

PaxDbiO23364.
PRIDEiO23364.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G15100.1; AT4G15100.1; AT4G15100.
GeneIDi827176.
GrameneiAT4G15100.1; AT4G15100.1; AT4G15100.
KEGGiath:AT4G15100.

Organism-specific databases

TAIRiAT4G15100.

Phylogenomic databases

eggNOGiKOG1282. Eukaryota.
COG2939. LUCA.
HOGENOMiHOG000198295.
InParanoidiO23364.
KOiK16297.
OMAiETHRNIN.
PhylomeDBiO23364.

Enzyme and pathway databases

BioCyciARA:AT4G15100-MONOMER.

Miscellaneous databases

PROiO23364.

Gene expression databases

GenevisibleiO23364. AT.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Ser_caboxypep_ser_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "An expression and bioinformatics analysis of the Arabidopsis serine carboxypeptidase-like gene family."
    Fraser C.M., Rider L.W., Chapple C.
    Plant Physiol. 138:1136-1148(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiSCP30_ARATH
AccessioniPrimary (citable) accession number: O23364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.