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SCP34_ARATH
ID   SCP34_ARATH             Reviewed;         499 AA.
AC   Q0WPR4; Q3E976; Q9FMX9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Serine carboxypeptidase-like 34;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL34; OrderedLocusNames=At5g23210; ORFNames=MKD15.7;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0WPR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0WPR4-2; Sequence=VSP_022850, VSP_022851, VSP_022852,
CC                                  VSP_022853;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice site
CC       and to an intron retention. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AB007648; BAB11176.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93133.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93136.1; -; Genomic_DNA.
DR   EMBL; AK228998; BAF00885.1; -; mRNA.
DR   RefSeq; NP_001078616.1; NM_001085147.2. [Q0WPR4-2]
DR   RefSeq; NP_851062.2; NM_180731.3. [Q0WPR4-1]
DR   AlphaFoldDB; Q0WPR4; -.
DR   SMR; Q0WPR4; -.
DR   BioGRID; 17660; 4.
DR   STRING; 3702.AT5G23210.1; -.
DR   ESTHER; arath-SCPL34; Carboxypeptidase_S10.
DR   MEROPS; S10.A39; -.
DR   PaxDb; Q0WPR4; -.
DR   PRIDE; Q0WPR4; -.
DR   ProteomicsDB; 226608; -. [Q0WPR4-1]
DR   EnsemblPlants; AT5G23210.1; AT5G23210.1; AT5G23210. [Q0WPR4-1]
DR   EnsemblPlants; AT5G23210.4; AT5G23210.4; AT5G23210. [Q0WPR4-2]
DR   GeneID; 832385; -.
DR   Gramene; AT5G23210.1; AT5G23210.1; AT5G23210. [Q0WPR4-1]
DR   Gramene; AT5G23210.4; AT5G23210.4; AT5G23210. [Q0WPR4-2]
DR   KEGG; ath:AT5G23210; -.
DR   Araport; AT5G23210; -.
DR   TAIR; locus:2166870; AT5G23210.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q0WPR4; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q0WPR4; -.
DR   PRO; PR:Q0WPR4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q0WPR4; baseline and differential.
DR   Genevisible; Q0WPR4; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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   Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..499
FT                   /note="Serine carboxypeptidase-like 34"
FT                   /id="PRO_0000274649"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        106..383
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..280
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..351
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_022850"
FT   VAR_SEQ         97..103
FT                   /note="LLWLNGG -> MSKSMKR (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_022851"
FT   VAR_SEQ         452..459
FT                   /note="GGWTVEYD -> NLVPSYKL (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_022852"
FT   VAR_SEQ         460..499
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_022853"
SQ   SEQUENCE   499 AA;  56329 MW;  6150FB81A2E7BCBD CRC64;
     MGSHSVEFSV LVLFLVSFLL GSTSAEKLCS DNDGDNGCFR SRVLAAQRAD RVKELPGQPP
     VKFRQYAGYV TVNETHGRAL FYWFFEATQN PSKKPVLLWL NGGPGCSSIG FGAAEELGPF
     FPQNSSQPKL KLNPYSWNKA ANLLFLESPV GVGFSYTNTS RDIKQLGDTV TARDSYNFLV
     NWFKRFPQYK SHDFYIAGES YAGHYVPQLS ELIYKENKIA SKKDFINLKG LMIGNALLDD
     ETDQKGMIEY AWDHAVISDA LYEKVNKNCD FKQKLVTKEC NDALDEYFDV YKILDMYSLY
     APKCVPTSTN SSTSHSVAGN RPLPAFRSIL RPRLISHNEG WRRMAAGYDP CASEYTEKYM
     NRKDVQEALH ANVTNISYPW THCSDTVSFW SDAPASMLPT LRTLVSAGLR VWVFSGDTDG
     RIPVTATRYS LKKLGLKIVQ DWTPWYTKLQ VGGWTVEYDG LMFVTVRGAG HQVPTFKPRE
     ALQLIHHFLG NKKLPTFPF
 
 
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