SCP35_ARATH
ID SCP35_ARATH Reviewed; 480 AA.
AC Q9LEY1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine carboxypeptidase-like 35;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL35; OrderedLocusNames=At5g08260; ORFNames=T22D6.200;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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, flowers and siliques.
CC {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AL357612; CAB93727.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91275.1; -; Genomic_DNA.
DR EMBL; AF370244; AAK44059.1; -; mRNA.
DR EMBL; AY062969; AAL33815.1; -; mRNA.
DR PIR; T50511; T50511.
DR RefSeq; NP_196443.1; NM_120909.4.
DR AlphaFoldDB; Q9LEY1; -.
DR SMR; Q9LEY1; -.
DR BioGRID; 16000; 7.
DR STRING; 3702.AT5G08260.1; -.
DR ESTHER; arath-SCP35; Carboxypeptidase_S10.
DR MEROPS; S10.A34; -.
DR PaxDb; Q9LEY1; -.
DR PRIDE; Q9LEY1; -.
DR ProteomicsDB; 232769; -.
DR EnsemblPlants; AT5G08260.1; AT5G08260.1; AT5G08260.
DR GeneID; 830722; -.
DR Gramene; AT5G08260.1; AT5G08260.1; AT5G08260.
DR KEGG; ath:AT5G08260; -.
DR Araport; AT5G08260; -.
DR TAIR; locus:2181504; AT5G08260.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; Q9LEY1; -.
DR OMA; GINSDWY; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q9LEY1; -.
DR PRO; PR:Q9LEY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LEY1; baseline and differential.
DR Genevisible; Q9LEY1; 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..480
FT /note="Serine carboxypeptidase-like 35"
FT /id="PRO_0000274650"
FT ACT_SITE 188
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /evidence="ECO:0000250"
FT ACT_SITE 452
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..363
FT /evidence="ECO:0000250"
FT DISULFID 257..270
FT /evidence="ECO:0000250"
FT DISULFID 294..331
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 53608 MW; 34FBAB3361851533 CRC64;
MKKNALWLLC ILVLPAIACG RKPEKKVTIS SSGRKEDDLV TGLPGQPPVN FKHYAGYVNL
GPEQKQKALF YWFFEAQQNS SRRPLVLWLN GGPGCSSIAY GAAQELGPFL VHDNGGKLTY
NHFSWNKEAN MLFLEAPVGV GFSYTNNSMD LQKLGDEVTA SDSLAFLINW FMKFPEFRSS
EFYISGESYA GHYVPQLAEV IYDRNKKVTK DSSINLKGFM IGNAVINEAT DMAGLVDYAW
SHAIISDEVH TSIHGSCSFE EDTTNKTEQC YNNFKGFMDA YNDIDIYSIY TPVCLSSLLS
SSPRKPKIVV SPRLLTFDDL WDKFPAGYDP CTESYAENYF NRKDVQVALH ANVTNLPYPY
SPCSGVIKRW SDAPSTMIPI IQKLLTGGLR IWIYSGDTDG RVPVTSTRYS IKKMGLKVES
PWRSWFHKSQ VAGWVETYAG GLNFVTVRGA GHQVPALAPA QSLTLFSHFI SSVPLPSKRF
