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YPP4_CAEEL
ID   YPP4_CAEEL              Reviewed;         243 AA.
AC   Q19948; Q8IG24;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Uncharacterized protein F32A5.4;
DE   Flags: Precursor;
GN   ORFNames=F32A5.4;
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], AND ALTERNATIVE SPLICING.
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-55, 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-55, 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q19948-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q19948-2; Sequence=VSP_007539;
CC   -!- SIMILARITY: Belongs to the protease inhibitor I33 family.
CC       {ECO:0000305}.
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DR   EMBL; FO080735; CCD66274.1; -; Genomic_DNA.
DR   EMBL; FO080735; CCD66275.1; -; Genomic_DNA.
DR   PIR; T16229; T16229.
DR   RefSeq; NP_495508.1; NM_063107.3. [Q19948-1]
DR   RefSeq; NP_871977.1; NM_182177.3. [Q19948-2]
DR   AlphaFoldDB; Q19948; -.
DR   BioGRID; 39524; 8.
DR   STRING; 6239.F32A5.4a.2; -.
DR   MEROPS; I33.002; -.
DR   iPTMnet; Q19948; -.
DR   EPD; Q19948; -.
DR   PaxDb; Q19948; -.
DR   PeptideAtlas; Q19948; -.
DR   EnsemblMetazoa; F32A5.4a.1; F32A5.4a.1; WBGene00017970. [Q19948-1]
DR   EnsemblMetazoa; F32A5.4b.1; F32A5.4b.1; WBGene00017970. [Q19948-2]
DR   GeneID; 174188; -.
DR   KEGG; cel:CELE_F32A5.4; -.
DR   UCSC; F32A5.4a.1; c. elegans. [Q19948-1]
DR   CTD; 174188; -.
DR   WormBase; F32A5.4a; CE01274; WBGene00017970; -. [Q19948-1]
DR   WormBase; F32A5.4b; CE32640; WBGene00017970; -. [Q19948-2]
DR   eggNOG; ENOG502S3IQ; Eukaryota.
DR   GeneTree; ENSGT00970000196274; -.
DR   HOGENOM; CLU_099985_0_0_1; -.
DR   InParanoid; Q19948; -.
DR   OMA; YFDGCMV; -.
DR   OrthoDB; 1378670at2759; -.
DR   PRO; PR:Q19948; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00017970; Expressed in larva and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.30.1120.50; -; 2.
DR   InterPro; IPR010480; Pepsin-I3.
DR   InterPro; IPR038412; Pepsin-I3_sf.
DR   Pfam; PF06394; Pepsin-I3; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..243
FT                   /note="Uncharacterized protein F32A5.4"
FT                   /id="PRO_0000002401"
FT   REGION          95..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   DISULFID        141..239
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..76
FT                   /note="MKLLALVALCAVGVASHRDKRQLSIGTISVSGAGGSTGCVVTGNVLYANGIR
FT                   LRNLTSSEQSELATYQTEVEQYKT -> MTWHFFQ (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_007539"
SQ   SEQUENCE   243 AA;  26463 MW;  F8549B0E253D2F44 CRC64;
     MKLLALVALC AVGVASHRDK RQLSIGTISV SGAGGSTGCV VTGNVLYANG IRLRNLTSSE
     QSELATYQTE VEQYKTQLRN ILSQRRENLR NRLMSQGRNQ QQQSNDVSSQ GGNDDGSIPK
     APEKPSFCTA EDTTQYYFDG CMVQGNKVYV GGQYARDLSS DEISELQTFD TQQTAYQNAV
     QSQMQSQVQG LFGGSDFLSA LFGGDRFNQQ QQRQQPSSTT PASTSSTTLP PKPTVPQFCT
     AIF
 
 
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