SCP31_ARATH
ID SCP31_ARATH Reviewed; 492 AA.
AC O04084; A4FVT3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine carboxypeptidase-like 31;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=SCPL31; OrderedLocusNames=At1g11080; ORFNames=T19D16.4;
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O04084-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, senescent leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:15908604}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BT003972; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U95973; AAB65475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28680.1; -; Genomic_DNA.
DR EMBL; BT003972; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT030381; ABO38794.1; -; mRNA.
DR PIR; G86244; G86244.
DR RefSeq; NP_172575.2; NM_100981.4. [O04084-1]
DR AlphaFoldDB; O04084; -.
DR SMR; O04084; -.
DR STRING; 3702.AT1G11080.2; -.
DR ESTHER; arath-SCP31; Carboxypeptidase_S10.
DR MEROPS; S10.A36; -.
DR PaxDb; O04084; -.
DR PRIDE; O04084; -.
DR EnsemblPlants; AT1G11080.1; AT1G11080.1; AT1G11080. [O04084-1]
DR GeneID; 837649; -.
DR Gramene; AT1G11080.1; AT1G11080.1; AT1G11080. [O04084-1]
DR KEGG; ath:AT1G11080; -.
DR Araport; AT1G11080; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; O04084; -.
DR OMA; KICNMEI; -.
DR PRO; PR:O04084; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04084; baseline and differential.
DR Genevisible; O04084; 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 Alternative splicing; Carboxypeptidase; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..492
FT /note="Serine carboxypeptidase-like 31"
FT /id="PRO_0000274646"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
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 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..376
FT /evidence="ECO:0000250"
FT DISULFID 270..283
FT /evidence="ECO:0000250"
FT DISULFID 307..344
FT /evidence="ECO:0000250"
FT CONFLICT 224
FT /note="S -> P (in Ref. 3; BT003972)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="P -> H (in Ref. 3; BT003972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 55445 MW; CA7D667A11DF00E6 CRC64;
MDNYQTKNIS NLLTSLCFTT LLILAPVVIC TRQHRFDSPK RSLLANEQDL VTGLPGQPDV
SFRHYAGYVP VDESNGRAMF YWFFEAMDLP KEKPLVLWLN GGPGCSSVGY GATQEIGPFL
VDTNGNGLNF NPYAWNKEAN MLFLESPVGV GFSYSNTSSD YQKLGDDFTA RDAYTFLCNW
FEKFPEHKEN TFYIAGESYA GKYVPELAEV VYDNNNNNKK NGSSFHINLK GILLGNPETS
DAEDWRGWVD YAWSHAVISD ETHRIITRTC NFSSDNTWSN DECNEAVAEV LKQYHEIDIY
SIYTSVCIGD SARSSYFDSA QFKTNSRISS KRMPPRLMGG YDPCLDDYAR VFYNRADVQK
SLHASDGVNL KNWSICNMEI FNNWTGSNPS VLPIYEKLIA GGLRIWVYSG DTDGRVPVLA
TRYSLNALEL PIKTAWRPWY HEKQVSGWLQ EYEGLTFATF RGAGHAVPCF KPSSSLAFFS
AFLSGVPPPP SR
