SOL1_ARATH
ID SOL1_ARATH Reviewed; 491 AA.
AC Q9M9H7; Q9C9J2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Carboxypeptidase SOL1;
DE EC=3.4.17.-;
DE AltName: Full=Protein SUPPRESSOR OF LLP1 1 {ECO:0000303|PubMed:12932329};
DE Flags: Precursor;
GN Name=SOL1 {ECO:0000303|PubMed:12932329};
GN OrderedLocusNames=At1g71696 {ECO:0000312|Araport:AT1G71696};
GN ORFNames=F14O23.7 {ECO:0000312|EMBL:AAF43222.1},
GN F26A9.4 {ECO:0000312|EMBL:AAG51831.1};
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12932329; DOI=10.1016/s0960-9822(03)00533-5;
RA Casamitjana-Martinez E., Hofhuis H.F., Xu J., Liu C.-M., Heidstra R.,
RA Scheres B.;
RT "Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a
RT CLV-like pathway in the control of Arabidopsis root meristem maintenance.";
RL Curr. Biol. 13:1435-1441(2003).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24118638; DOI=10.1111/tpj.12349;
RA Tamaki T., Betsuyaku S., Fujiwara M., Fukao Y., Fukuda H., Sawa S.;
RT "SUPPRESSOR OF LLP1 1-mediated C-terminal processing is critical for CLE19
RT peptide activity.";
RL Plant J. 76:970-981(2013).
CC -!- FUNCTION: Possesses in vitro carboxypeptidase activity against the C-
CC terminal arginine and lysine residues. Involved in the maturation of
CC CLE19. Removes the C-terminal arginine residue of CLE19 proprotein. The
CC cleavage of the C-terminal arginine residue is necessary for CLE19
CC activity in vivo. Is not involved in generating active CLV3
CC (PubMed:24118638). Is not involved in CLE19 or CLV3 perception
CC (PubMed:12932329, PubMed:24118638). {ECO:0000269|PubMed:12932329,
CC ECO:0000269|PubMed:24118638}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15085};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15085};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:24118638};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9M9H7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:12932329}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51831.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ555410; CAD87769.1; -; mRNA.
DR EMBL; AC012654; AAF43222.1; -; Genomic_DNA.
DR EMBL; AC016163; AAG51831.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35219.1; -; Genomic_DNA.
DR PIR; B96739; B96739.
DR RefSeq; NP_974126.1; NM_202397.2. [Q9M9H7-1]
DR AlphaFoldDB; Q9M9H7; -.
DR SMR; Q9M9H7; -.
DR STRING; 3702.AT1G71696.2; -.
DR MEROPS; M14.A02; -.
DR PaxDb; Q9M9H7; -.
DR PRIDE; Q9M9H7; -.
DR ProteomicsDB; 232479; -. [Q9M9H7-1]
DR EnsemblPlants; AT1G71696.2; AT1G71696.2; AT1G71696. [Q9M9H7-1]
DR GeneID; 843499; -.
DR Gramene; AT1G71696.2; AT1G71696.2; AT1G71696. [Q9M9H7-1]
DR KEGG; ath:AT1G71696; -.
DR Araport; AT1G71696; -.
DR TAIR; locus:2824541; AT1G71696.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; Q9M9H7; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q9M9H7; -.
DR PRO; PR:Q9M9H7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9H7; baseline and differential.
DR Genevisible; Q9M9H7; AT.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF73; PTHR11532:SF73; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carboxypeptidase; Endosome; Glycoprotein; Hydrolase;
KW Membrane; Metal-binding; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..491
FT /note="Carboxypeptidase SOL1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434547"
FT TOPO_DOM 26..452
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12932329"
FT BINDING 125..128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 491 AA; 56046 MW; 3B17B6209BBE8082 CRC64;
MSKLRFFQSL LISTVICFFL PSINARGGHS DHIHPGDGNY SFHGIVRHLF AQEEPTPSLE
LTRGYMTNDD LEKAMKDFTK RCSKISRLYS IGKSVNGFPL WVIEISDRPG EIEAEPAFKY
IGNVHGDEPV GRELLLRLAN WICDNYKKDP LAQMIVENVH LHIMPSLNPD GFSIRKRNNA
NNVDLNRDFP DQFFPFNDDL NLRQPETKAI MTWLRDIRFT ASATLHGGAL VANFPWDGTE
DKRKYYYACP DDETFRFLAR IYSKSHRNMS LSKEFEEGIT NGASWYPIYG GMQDWNYIYG
GCFELTLEIS DNKWPKASEL STIWDYNRKS MLNLVASLVK TGVHGRIFSL DKGKPLPGLV
VVKGINYTVK AHQTYADYHR LLVPGQKYEV TASSPGYKSK TTTVWLGENA VTADFILIPE
TSSRGNQLRS SCDCSCKSCG QPLLTQFFTE TNNGITLTLF VVVVFLCFLL QRRVRFNLWK
QRQSSRRSIT V
