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Q8L7B2

- SCP20_ARATH

UniProt

Q8L7B2 - SCP20_ARATH

Protein

Serine carboxypeptidase-like 20

Gene

SCPL20

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Probable carboxypeptidase.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei186 – 1861By similarity
    Active sitei421 – 4211By similarity
    Active sitei474 – 4741By similarity

    GO - Molecular functioni

    1. serine-type carboxypeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciARA:AT4G12910-MONOMER.

    Protein family/group databases

    MEROPSiS10.A11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine carboxypeptidase-like 20 (EC:3.4.16.-)
    Gene namesi
    Name:SCPL20
    Ordered Locus Names:At4g12910
    ORF Names:F25G13.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G12910.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. vacuole Source: TAIR

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 497468Serine carboxypeptidase-like 20PRO_0000274636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi90 ↔ 386By similarity
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi254 ↔ 266By similarity
    Disulfide bondi289 ↔ 353By similarity
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8L7B2.
    PRIDEiQ8L7B2.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    GenevestigatoriQ8L7B2.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G12910.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L7B2.
    SMRiQ8L7B2. Positions 28-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi495 – 4973Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2939.
    HOGENOMiHOG000198297.
    InParanoidiQ8L7B2.
    KOiK16296.
    OMAiDYLVTHD.
    PhylomeDBiQ8L7B2.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view]
    PANTHERiPTHR11802. PTHR11802. 1 hit.
    PfamiPF00450. Peptidase_S10. 1 hit.
    [Graphical view]
    PRINTSiPR00724. CRBOXYPTASEC.
    SUPFAMiSSF53474. SSF53474. 2 hits.
    PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8L7B2-1 [UniParc]FASTAAdd to Basket

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    MSIITMVWLM KVFVFVTLLS LVFVITESAP ESALITKLPG FEGTFPSKHY    50
    SGYVTIDKEH GKNLWYYFIE SEKNPSKDPV VLWLNGGPGC SSMDGFVYEH 100
    GPFNFELPKK NNSLPLLHLN PYSWSKVSNI IYLDSPVGVG FSYSNNKSDY 150
    ITGDIKTAVD SHAFLLKWFQ MFPEFQSNPF FISGESYAGV YVPTLASEVV 200
    IGNKNGVKPA LNFKGYLVGN GVADPKFDGN AFVPFAHGMG LISDELFENV 250
    TKACKGNFYE IEGLECEEQY TKVNDDTNQL NIYNILEPCY HGTSLSAFDI 300
    RSLPSSLLQL GKTEKRLPIR KRMFGRAWPV RAPVHPGIVP SWSQLLADVT 350
    VPCIDDRVAT AWLNDPEIRK AIHTKEESEI GRWELCSGKL SFYHDAGSMI 400
    DFHRNLTLSG YRALIYSGDH DMCVPFTGSE AWTKSLGYKV IDEWRAWISN 450
    DQVAGYTQGY ANNLTFLTIK GAGHTVPEYK PREALDFYSR FLEGSKI 497
    Length:497
    Mass (Da):55,833
    Last modified:February 6, 2007 - v2
    Checksum:i0258C97B8C6A9D8B
    GO

    Sequence cautioni

    The sequence CAB53091.1 differs from that shown. Reason: Frameshift at position 479.
    The sequence CAB78333.1 differs from that shown. Reason: Frameshift at position 479.
    The sequence CAB53091.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB78333.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211G → V in AAM97031. (PubMed:14593172)Curated
    Sequence conflicti221 – 2211G → V in AAN15500. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL079349 Genomic DNA. Translation: CAB53091.1. Sequence problems.
    AL161535 Genomic DNA. Translation: CAB78333.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83202.1.
    AY136365 mRNA. Translation: AAM97031.1.
    BT000181 mRNA. Translation: AAN15500.1.
    PIRiA85139.
    RefSeqiNP_193027.5. NM_117360.7.
    UniGeneiAt.45003.

    Genome annotation databases

    EnsemblPlantsiAT4G12910.1; AT4G12910.1; AT4G12910.
    GeneIDi826903.
    KEGGiath:AT4G12910.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL079349 Genomic DNA. Translation: CAB53091.1 . Sequence problems.
    AL161535 Genomic DNA. Translation: CAB78333.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83202.1 .
    AY136365 mRNA. Translation: AAM97031.1 .
    BT000181 mRNA. Translation: AAN15500.1 .
    PIRi A85139.
    RefSeqi NP_193027.5. NM_117360.7.
    UniGenei At.45003.

    3D structure databases

    ProteinModelPortali Q8L7B2.
    SMRi Q8L7B2. Positions 28-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G12910.1-P.

    Protein family/group databases

    MEROPSi S10.A11.

    Proteomic databases

    PaxDbi Q8L7B2.
    PRIDEi Q8L7B2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G12910.1 ; AT4G12910.1 ; AT4G12910 .
    GeneIDi 826903.
    KEGGi ath:AT4G12910.

    Organism-specific databases

    TAIRi AT4G12910.

    Phylogenomic databases

    eggNOGi COG2939.
    HOGENOMi HOG000198297.
    InParanoidi Q8L7B2.
    KOi K16296.
    OMAi DYLVTHD.
    PhylomeDBi Q8L7B2.

    Enzyme and pathway databases

    BioCyci ARA:AT4G12910-MONOMER.

    Gene expression databases

    Genevestigatori Q8L7B2.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 2 hits.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      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, TISSUE SPECIFICITY, NOMENCLATURE.

    Entry informationi

    Entry nameiSCP20_ARATH
    AccessioniPrimary (citable) accession number: Q8L7B2
    Secondary accession number(s): Q9SV78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 72 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

    External Data

    Dasty 3