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SCP28_ARATH
ID   SCP28_ARATH             Reviewed;         462 AA.
AC   Q8S8K6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Serine carboxypeptidase-like 28;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL28; OrderedLocusNames=At2g35770; ORFNames=T20F21.4;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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, roots and senescent leaves.
CC       {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM15112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BX820274; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC006068; AAM15112.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC09159.1; -; Genomic_DNA.
DR   EMBL; BX820274; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; G84772; G84772.
DR   RefSeq; NP_181120.2; NM_129135.3.
DR   AlphaFoldDB; Q8S8K6; -.
DR   SMR; Q8S8K6; -.
DR   ESTHER; arath-SCP28; Carboxypeptidase_S10.
DR   MEROPS; S10.A28; -.
DR   PaxDb; Q8S8K6; -.
DR   PRIDE; Q8S8K6; -.
DR   ProteomicsDB; 232821; -.
DR   EnsemblPlants; AT2G35770.1; AT2G35770.1; AT2G35770.
DR   GeneID; 818149; -.
DR   Gramene; AT2G35770.1; AT2G35770.1; AT2G35770.
DR   KEGG; ath:AT2G35770; -.
DR   Araport; AT2G35770; -.
DR   TAIR; locus:2058734; AT2G35770.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q8S8K6; -.
DR   OMA; HLRIWIF; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q8S8K6; -.
DR   PRO; PR:Q8S8K6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8S8K6; baseline and differential.
DR   Genevisible; Q8S8K6; 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; 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; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..462
FT                   /note="Serine carboxypeptidase-like 28"
FT                   /id="PRO_0000274643"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        254..266
FT                   /evidence="ECO:0000250"
FT   DISULFID        290..311
FT                   /evidence="ECO:0000250"
FT   CONFLICT        239
FT                   /note="H -> N (in Ref. 3; BX820274)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="Y -> H (in Ref. 3; BX820274)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="C -> R (in Ref. 3; BX820274)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="H -> N (in Ref. 3; BX820274)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  52098 MW;  EB574420E297DAC7 CRC64;
     MMITKKLYQC MCLLCMVIAL LDVVSSDDAK EQKMKDKIIS LPGQPPNLNF SQFSGYVTVD
     PAAGRALFYW LTEAPRPSGT KPLVLWLNGG PGCSSIAYGA SEEVGPFRVN PDGKTLRLNL
     YAWNKVANVL FLDSPAGVGF SYTNTSSDEL TVGDKRTGED AYRFLVRWLE RFPEYKERAF
     YIAGESYAGH YIPELAQLIV NRNKGAKNPT INLKGILMGN PLVDDYNDNK GMRDYWWNHG
     LISDESYNDL TKWCLNDSIL FPKLNCNAAL NQALSEFGDI DPYNINSPAC TTHASSNEWM
     QAWRYRGNDE CVVGYTRKYM NDPNVHKSFH ARLNGSTPWT PCSRVIRKNW KDSPKSMLPI
     IKNLLQAHLR IWIFSGDSDA VLPLSGTRHS INAMKLKSSK RWYPWYHSHG LVGGWSQVYE
     DGLLTYTTVR AAGHEVPLSQ PRLALFLFTH FLANHSLPSS PS
 
 
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