SCP45_ARATH
ID SCP45_ARATH Reviewed; 461 AA.
AC Q93Y09; Q9C7E2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine carboxypeptidase-like 45;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL45; OrderedLocusNames=At1g28110; ORFNames=F13K9.20;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC069471; AAG51475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30918.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30919.1; -; Genomic_DNA.
DR EMBL; AY059854; AAL24336.1; -; mRNA.
DR EMBL; BT008763; AAP49525.1; -; mRNA.
DR PIR; H86406; H86406.
DR RefSeq; NP_564298.1; NM_102576.2.
DR RefSeq; NP_973926.1; NM_202197.2.
DR AlphaFoldDB; Q93Y09; -.
DR SMR; Q93Y09; -.
DR STRING; 3702.AT1G28110.2; -.
DR ESTHER; arath-SCP45; Carboxypeptidase_S10.
DR MEROPS; S10.A24; -.
DR iPTMnet; Q93Y09; -.
DR PaxDb; Q93Y09; -.
DR PRIDE; Q93Y09; -.
DR ProteomicsDB; 232942; -.
DR EnsemblPlants; AT1G28110.1; AT1G28110.1; AT1G28110.
DR EnsemblPlants; AT1G28110.2; AT1G28110.2; AT1G28110.
DR GeneID; 839704; -.
DR Gramene; AT1G28110.1; AT1G28110.1; AT1G28110.
DR Gramene; AT1G28110.2; AT1G28110.2; AT1G28110.
DR KEGG; ath:AT1G28110; -.
DR Araport; AT1G28110; -.
DR TAIR; locus:2010454; AT1G28110.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_1_1; -.
DR InParanoid; Q93Y09; -.
DR OMA; AAWFNGG; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; Q93Y09; -.
DR PRO; PR:Q93Y09; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Y09; baseline and differential.
DR Genevisible; Q93Y09; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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 Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..461
FT /note="Serine carboxypeptidase-like 45"
FT /id="PRO_0000274660"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /evidence="ECO:0000250"
FT ACT_SITE 434
FT /evidence="ECO:0000250"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..340
FT /evidence="ECO:0000250"
FT DISULFID 243..261
FT /evidence="ECO:0000250"
FT DISULFID 286..309
FT /evidence="ECO:0000250"
SQ SEQUENCE 461 AA; 51803 MW; 2CDD208490EFF087 CRC64;
MSPLQWLTIS FALIIFHSLT VSSSVLSHSD RVTRLPGQPR VGFQQYSGYV TVDDKKQRAL
FYYFAEAETN PSSKPLVLWL NGGPGCSSLG VGAFSENGPF RPKGPILVKN QHSWNQEANM
LYLETPVGVG FSYSTQSSHY EGVNDKITAR DNLVFLQRWF LKFPHYLNRS LFITGESYAG
HYVPQLAELM IQYNKKHHLF NLRGIAIGNP VLEFATDFNS RAEYFWSHGL ISDSTYKMFT
SYCNYSRYVS EYYRGSMSSM CSKVMSQVST ETSRFVDKYD VTLDVCIPSV LSQSKVVSPN
QVGESVDVCV EDETVNYLNR RDVQEALHAR LIGVREWTVC SNVLDYQLLD VEIPTINIVG
SLVKAGVPVL VYSGDQDSVI PLTGSRTLVS RLAKQLGLRT SVPYRVWFAG QQVGGWTQVY
GNVLSFATVR GASHEVPFSQ PERSLVLFKA FLDGHPLPEE F
