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SCP48_ARATH
ID   SCP48_ARATH             Reviewed;         510 AA.
AC   Q56WF8; Q93ZC3; Q9LXH4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Serine carboxypeptidase-like 48;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=SCPL48; OrderedLocusNames=At3g45010; ORFNames=F14D17.80;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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] OF 330-510.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) 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   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15908604}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD94954.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL353992; CAB89316.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77979.1; -; Genomic_DNA.
DR   EMBL; AY050427; AAK91443.1; -; mRNA.
DR   EMBL; AY057639; AAL15270.1; -; mRNA.
DR   EMBL; AY093993; AAM16254.1; -; mRNA.
DR   EMBL; AK222084; BAD94954.1; ALT_INIT; mRNA.
DR   PIR; T48977; T48977.
DR   RefSeq; NP_190087.1; NM_114370.4.
DR   AlphaFoldDB; Q56WF8; -.
DR   SMR; Q56WF8; -.
DR   STRING; 3702.AT3G45010.1; -.
DR   ChEMBL; CHEMBL1932908; -.
DR   ESTHER; arath-F14D17.80; Carboxypeptidase_S10.
DR   MEROPS; S10.A46; -.
DR   PaxDb; Q56WF8; -.
DR   PRIDE; Q56WF8; -.
DR   ProteomicsDB; 226605; -.
DR   EnsemblPlants; AT3G45010.1; AT3G45010.1; AT3G45010.
DR   GeneID; 823636; -.
DR   Gramene; AT3G45010.1; AT3G45010.1; AT3G45010.
DR   KEGG; ath:AT3G45010; -.
DR   Araport; AT3G45010; -.
DR   TAIR; locus:2075929; AT3G45010.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_1_1; -.
DR   InParanoid; Q56WF8; -.
DR   OMA; NCYVEMD; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q56WF8; -.
DR   PRO; PR:Q56WF8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q56WF8; baseline and differential.
DR   Genevisible; Q56WF8; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..510
FT                   /note="Serine carboxypeptidase-like 48"
FT                   /id="PRO_0000274663"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        478
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..383
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..326
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..354
FT                   /evidence="ECO:0000250"
FT   CONFLICT        455
FT                   /note="D -> G (in Ref. 3; AAL15270)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  56896 MW;  134BC30F4E64BF0A CRC64;
     MDSKTTFLTF LLCIFIFSHF SPSTSKSLTE KPLSFSPSAS LPTLTAERLI KGFNLMPTRD
     VNVIDEEGSE APRLVERAFD LPAAVDRRGS GGSPSVQDFG HHAGYYKLPN SKAARMFYFF
     FESRTNKADP VVIWLTGGPG CSSELALFYE NGPFTVSNNS SLSWNEFGWD KASNLIYVDQ
     PVGTGFSYTS DQSDLRHDED GVSNDLYDFL QAFFKEHPQF VKNDFYITGE SYAGHYIPAL
     ASRVHRGNKN KEGTHINLKG FAIGNGLTNP EIQYGAYADY ALDMNLITQS DHDNLNRYYA
     TCQQSIKECS ADGGEGDACA SSYTVCNNIF QKIMDIAGNV NYYDVRKQCE GSLCYDFSNM
     ENFLNQKSVR KALGVGDIEF VSCSTAVYEA MQMDWMRNLE VGIPALLQDG IKLLVYAGEY
     DLICNWLGNS KWVHEMEWSG QKEFVAAATV PFHVDNKEAG LMKNYGSLTF LKVHDAGHMV
     PMDQPKAALQ MLQNWMQGKL STPTGRTAHQ
 
 
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