位置:首页 > 蛋白库 > SCP27_ARATH
SCP27_ARATH
ID   SCP27_ARATH             Reviewed;         459 AA.
AC   Q9SFB5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Serine carboxypeptidase-like 27;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL27; OrderedLocusNames=At3g07990; ORFNames=F17A17.33;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC013483; AAF21209.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74628.1; -; Genomic_DNA.
DR   EMBL; BT015083; AAT71955.1; -; mRNA.
DR   EMBL; BT015904; AAU95440.1; -; mRNA.
DR   RefSeq; NP_187456.1; NM_111678.3.
DR   AlphaFoldDB; Q9SFB5; -.
DR   SMR; Q9SFB5; -.
DR   STRING; 3702.AT3G07990.1; -.
DR   ESTHER; arath-SCP27; Carboxypeptidase_S10.
DR   MEROPS; S10.A23; -.
DR   PaxDb; Q9SFB5; -.
DR   PRIDE; Q9SFB5; -.
DR   ProteomicsDB; 232704; -.
DR   EnsemblPlants; AT3G07990.1; AT3G07990.1; AT3G07990.
DR   GeneID; 819990; -.
DR   Gramene; AT3G07990.1; AT3G07990.1; AT3G07990.
DR   KEGG; ath:AT3G07990; -.
DR   Araport; AT3G07990; -.
DR   TAIR; locus:2077422; AT3G07990.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q9SFB5; -.
DR   OMA; CTDRYAK; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q9SFB5; -.
DR   PRO; PR:Q9SFB5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SFB5; baseline and differential.
DR   Genevisible; Q9SFB5; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..459
FT                   /note="Serine carboxypeptidase-like 27"
FT                   /id="PRO_0000274642"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        252..264
FT                   /evidence="ECO:0000250"
FT   DISULFID        288..312
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  52141 MW;  416109FFC2DC8499 CRC64;
     MDYSFLLIIL LLTISTSCCA APSSYVEEQL RDRISNLPGQ PSNVDFRQYS GYVTVHEERG
     RALFYWLVES PLARDPKSRP LVLWLNGGPG CSSVAYGAAE EIGPFRVGSD GKTLHSKLYA
     WNKLANLLFL ESPAGVGFSY SNTTSDLYTT GDQRTAEDSY IFLVNWFERF PQYKHREFYI
     VGESYAGHFV PQLSKLVHER NKGFKNPAIN LKGFMVGNAV TDDYHDYIGT FEYWWNHGLI
     SDSTYHQLKT ACYSVSSQHP SMQCMVALRN AELEQGNIDP YSIFTKPCNS TVALKRFLKG
     RYPWMSRAYD PCTERYSNVY FNRLDVQKAL HANVTRLSYP WKACSDIVGS YWDDSPLSML
     PIYKELITAG LKIWVFSGDT DAVVPITATR YSVDALKLAT ITNWYPWYDH GKVGGWSQVY
     KGLTLVTVAG AGHEVPLHRP RQAFILFRSF LESKPMPMT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025