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CTS32_CAEEL
ID   CTS32_CAEEL             Reviewed;         517 AA.
AC   P52714;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Serine carboxypeptidase ctsa-3.2 {ECO:0000305};
DE            EC=3.4.16.- {ECO:0000250|UniProtKB:P52719};
DE   Flags: Precursor;
GN   Name=ctsa-3.2 {ECO:0000312|WormBase:C08H9.1};
GN   ORFNames=C08H9.1 {ECO:0000312|WormBase:C08H9.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; BX284602; CAA91143.2; -; Genomic_DNA.
DR   PIR; T19106; T19106.
DR   RefSeq; NP_496134.1; NM_063733.1.
DR   AlphaFoldDB; P52714; -.
DR   SMR; P52714; -.
DR   STRING; 6239.C08H9.1; -.
DR   ESTHER; caeel-c08h9.1; Carboxypeptidase_S10.
DR   MEROPS; S10.A56; -.
DR   iPTMnet; P52714; -.
DR   PaxDb; P52714; -.
DR   EnsemblMetazoa; C08H9.1.1; C08H9.1.1; WBGene00007462.
DR   UCSC; C08H9.1; c. elegans.
DR   WormBase; C08H9.1; CE54048; WBGene00007462; ctsa-3.2.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_13_3_1; -.
DR   InParanoid; P52714; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; P52714; -.
DR   Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:P52714; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00007462; Expressed in larva and 1 other tissue.
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   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..517
FT                   /note="Serine carboxypeptidase ctsa-3.2"
FT                   /id="PRO_0000120568"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        485
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   517 AA;  59026 MW;  53F54135346B7054 CRC64;
     MWWTSLVFSV LLFDLIFISN CDYIHLPGNS DIPDLKLQSG YLNANENGTQ KMFYFLLEAR
     DIPVGEASLI IWFNGGPGCS SLSAFFEEFG PLYVNFGGKS LFENVHSWYH KANILFLESP
     IGVGFSYDTE QSNFTKVNDD SIAEQNFNSV IDFFQRKHSS YVNHDFFIAA ESYGGVYGPM
     LSALVVDSIS KREFPNENFK GLIIGNGFMN VKLSTNTMIL WSAYHDRTSP DEWDEIKEKC
     ATSGAHDVDY YDFMQFMKTT NKMDYLADNS TECGRLIEPL LGQFSETFDG YDFFNYYHDC
     YTNFSIPNAT DPIKETLAQI PRRRISALFN KHSTDGQASY RCWADDALHK YLNLKEVQNA
     LGIDRAWKDR KKKWEVCNMP IYDQYVMTHQ DMTPFFSKIF DKFTGPAFRV LIYSGDIDTA
     CNYLADGYFV RDLASIHGFK KTLKHGPWYH SEHKVIAGNF MRYEGANHLG SKLSIDVVTV
     KGSGHFVPLD RPGPALQMVH NFLTGKPGKM TNYTSPV
 
 
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