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SCP50_ARATH
ID   SCP50_ARATH             Reviewed;         444 AA.
AC   Q9M9Q6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Serine carboxypeptidase-like 50;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL50; OrderedLocusNames=At1g15000; ORFNames=T15D22.4, T15D22.7;
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}.
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DR   EMBL; AC012189; AAF31022.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29252.1; -; Genomic_DNA.
DR   EMBL; AY075612; AAL91626.1; -; mRNA.
DR   EMBL; BT002620; AAO11536.1; -; mRNA.
DR   PIR; D86283; D86283.
DR   RefSeq; NP_172953.1; NM_101369.2.
DR   AlphaFoldDB; Q9M9Q6; -.
DR   SMR; Q9M9Q6; -.
DR   STRING; 3702.AT1G15000.1; -.
DR   ESTHER; arath-SCP50; Carboxypeptidase_S10.
DR   MEROPS; S10.003; -.
DR   PaxDb; Q9M9Q6; -.
DR   PRIDE; Q9M9Q6; -.
DR   ProteomicsDB; 226606; -.
DR   EnsemblPlants; AT1G15000.1; AT1G15000.1; AT1G15000.
DR   GeneID; 838065; -.
DR   Gramene; AT1G15000.1; AT1G15000.1; AT1G15000.
DR   KEGG; ath:AT1G15000; -.
DR   Araport; AT1G15000; -.
DR   TAIR; locus:2196199; AT1G15000.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_1_1; -.
DR   OMA; PFHDLDK; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q9M9Q6; -.
DR   PRO; PR:Q9M9Q6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9Q6; differential.
DR   Genevisible; Q9M9Q6; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; 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   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.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..444
FT                   /note="Serine carboxypeptidase-like 50"
FT                   /id="PRO_0000274664"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        345
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..308
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   444 AA;  49222 MW;  E9E769B30DB492B8 CRC64;
     MEQATTLFIL LSTLLLAVSV ESPQPPLFPD EALPTKSGYL PVKPAPGSSM FYAFYEAQEP
     TTPLPDTPLL VWLQGGPGCS SMIGNFYELG PWRVVSRATD LERNPGAWNR LFGLLFVDNP
     IGVGFSIAAS QQDIPTNQRQ VAEHLYAALV EFLEQNPSFE NRPVYFTGES YAGKYVPAIG
     YYILKEKPNG KVNLKGLAIG NGLTDPVTQV QTHAVNVYYS GLVNAKQRVE LQKAQEISVA
     LVKSQKWREA ADARTELLTL LSNMTGLATL YNTARAIPYR TDLVVDLLNQ REAKRVLGVS
     ETVRFEECSD EVEDVLRADV MKSVKFMVEY ALERTQVLLY QGMLDLRDGV VSTEEWMKTM
     NWSGLGMFST AERRVWKDED GVVAGYVQRW GNLCHVAVTG AGHFVPTDKA VNSRDMIEGW
     VLGKGLFGGK DVKQTTSSSL YHSI
 
 
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