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LON1_CAEEL
ID   LON1_CAEEL              Reviewed;         312 AA.
AC   Q09566;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Protein lon-1;
DE   Flags: Precursor;
GN   Name=lon-1; ORFNames=F48E8.1;
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   FUNCTION.
RX   PubMed=12051826; DOI=10.1006/dbio.2002.0662;
RA   Maduzia L.L., Gumienny T.L., Zimmerman C.M., Wang H., Shetgiri P.,
RA   Krishna S., Roberts A.F., Padgett R.W.;
RT   "lon-1 regulates Caenorhabditis elegans body size downstream of the dbl-1
RT   TGF beta signaling pathway.";
RL   Dev. Biol. 246:418-428(2002).
CC   -!- FUNCTION: Regulates body size morphogenesis, but does not affect male
CC       tail development. {ECO:0000269|PubMed:12051826}.
CC   -!- TISSUE SPECIFICITY: Expressed in hypodermal tissues.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; FO081421; CCD71508.1; -; Genomic_DNA.
DR   PIR; T16415; T16415.
DR   RefSeq; NP_498166.1; NM_065765.6.
DR   AlphaFoldDB; Q09566; -.
DR   SMR; Q09566; -.
DR   BioGRID; 40982; 3.
DR   DIP; DIP-27422N; -.
DR   IntAct; Q09566; 2.
DR   STRING; 6239.F48E8.1a; -.
DR   PaxDb; Q09566; -.
DR   PeptideAtlas; Q09566; -.
DR   EnsemblMetazoa; F48E8.1a.1; F48E8.1a.1; WBGene00003055.
DR   GeneID; 175753; -.
DR   KEGG; cel:CELE_F48E8.1; -.
DR   UCSC; F48E8.1c; c. elegans.
DR   CTD; 175753; -.
DR   WormBase; F48E8.1a; CE01953; WBGene00003055; lon-1.
DR   eggNOG; KOG3017; Eukaryota.
DR   HOGENOM; CLU_970554_0_0_1; -.
DR   InParanoid; Q09566; -.
DR   OMA; HADTCDF; -.
DR   OrthoDB; 1528782at2759; -.
DR   PhylomeDB; Q09566; -.
DR   PRO; PR:Q09566; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003055; Expressed in adult organism and 3 other tissues.
DR   ExpressionAtlas; Q09566; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR   GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:WormBase.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR   GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   GO; GO:1901048; P:transforming growth factor beta receptor signaling pathway involved in regulation of multicellular organism growth; IGI:UniProtKB.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..312
FT                   /note="Protein lon-1"
FT                   /id="PRO_0000006299"
FT   DOMAIN          87..209
FT                   /note="SCP"
FT   REGION          265..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..302
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   312 AA;  35054 MW;  AEFC7BFF25E26288 CRC64;
     MNYLLTALIA LLAPISVAYN VPHGFLTGEA VTSHSGPNDL DGELPATDEV KREKRGYFFP
     SHFQSDSGLL SRSEHPNEYL KKWITHEHNR YRRMVPASDM NMLYWSDELA ASAQRHADTC
     DFRHSRGRIN VGENIWAAPY SNYSDAISIW FNEVHNPRCG CNHAYKHCCG HYVQVVWAKT
     NLVGCGFSRC RDVQGVWGRG HRNVFVCHYN PQGNTVFVTA RGQLYAMPAF TWASGDNGKC
     SNCPANAPAC YQGLCYMPKN YEAPTTTTES TTTSTTTEEP TTTCEPDEPE AEGADNNQEE
     EEENNDGFRM RV
 
 
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