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SCP38_ARATH
ID   SCP38_ARATH             Reviewed;         487 AA.
AC   Q9ZUG3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Serine carboxypeptidase-like 38;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL38; OrderedLocusNames=At2g05850; ORFNames=T6P5.5;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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, roots, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AC005970; AAC95162.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05981.1; -; Genomic_DNA.
DR   EMBL; AY065440; AAL38881.1; -; mRNA.
DR   EMBL; BT000980; AAN41380.1; -; mRNA.
DR   PIR; B84472; B84472.
DR   RefSeq; NP_178642.1; NM_126598.4.
DR   AlphaFoldDB; Q9ZUG3; -.
DR   SMR; Q9ZUG3; -.
DR   STRING; 3702.AT2G05850.1; -.
DR   ESTHER; arath-scp38; Carboxypeptidase_S10.
DR   MEROPS; S10.A29; -.
DR   PaxDb; Q9ZUG3; -.
DR   PRIDE; Q9ZUG3; -.
DR   ProteomicsDB; 226609; -.
DR   EnsemblPlants; AT2G05850.1; AT2G05850.1; AT2G05850.
DR   GeneID; 815137; -.
DR   Gramene; AT2G05850.1; AT2G05850.1; AT2G05850.
DR   KEGG; ath:AT2G05850; -.
DR   Araport; AT2G05850; -.
DR   TAIR; locus:2064737; AT2G05850.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_0_1; -.
DR   InParanoid; Q9ZUG3; -.
DR   OMA; EANMLFF; -.
DR   OrthoDB; 607679at2759; -.
DR   PhylomeDB; Q9ZUG3; -.
DR   PRO; PR:Q9ZUG3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZUG3; baseline and differential.
DR   Genevisible; Q9ZUG3; 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   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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..487
FT                   /note="Serine carboxypeptidase-like 38"
FT                   /id="PRO_0000274653"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..368
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..336
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   487 AA;  54731 MW;  D85802C8B1F02469 CRC64;
     MGKQQDWSVT ACIFLSLSLA SQIHCSSQTH FPSHKGGAGL SGDTSHFNSV SRENVLSLKE
     KDLIEKLPGQ PSGISFRQYG GYVAVNEPAT RFLYYYFVEA IKPSKSTPLV LWFNGGPGCS
     SVGFGAFEEL GPFRVHSDGK TLYRNPYSWN NEANMLFFEG PISVGFSYSS TPFDWEIFGE
     QADKLTAEDN YMFLVNWLER FPEYKGRDVY ISGQSYAGHY IPQLAQIILH RNNQTFINLR
     GISIGNPGLD LLIEADNENK FILSHGLVSQ KDFEEYSKVC DFANYDMDEC PKIMPKFSIE
     HNKHLDVYNI YAPVCLNSTL SSEPKKCTTI MEVDPCRSNY VKAYLNSENV QEAMHANTTK
     LPYEWKACNH YLNSVWIDAD KDASMVPILH DLMGEGVRVL VYSGDVDAAI PFTATMAVLK
     TMNLTVVNEW RPWFTGGQLG GFTEDYERNL TYATVKGSGH SVPLDQPVHA LNLFTSFIRN
     TPLPQTP
 
 
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