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LON3_CAEEL
ID   LON3_CAEEL              Reviewed;         324 AA.
AC   Q23628;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Cuticle collagen lon-3;
DE   Flags: Precursor;
GN   Name=lon-3; ORFNames=ZK836.1;
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 [MRNA].
RX   PubMed=12019225; DOI=10.1093/genetics/161.1.83;
RA   Nystroem J., Shen Z.-Z., Aili M., Flemming A.J., Leroi A., Tuck S.P.;
RT   "Increased or decreased levels of Caenorhabditis elegans lon-3, a gene
RT   encoding a collagen, cause reciprocal changes in body length.";
RL   Genetics 161:83-97(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12524338; DOI=10.1093/genetics/162.4.1631;
RA   Suzuki Y., Morris G.A., Han M., Wood W.B.;
RT   "A cuticle collagen encoded by the lon-3 gene may be a target of TGF-beta
RT   signaling in determining Caenorhabditis elegans body shape.";
RL   Genetics 162:1631-1639(2002).
RN   [3]
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).
CC   -!- FUNCTION: Nematode cuticles are composed largely of collagen-like
CC       proteins. The cuticle functions both as an exoskeleton and as a barrier
CC       to protect the worm from its environment. Dose-dependent regulator of
CC       body length and shape.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; AF262406; AAL08218.1; -; mRNA.
DR   EMBL; AF465981; AAL76993.1; -; mRNA.
DR   EMBL; Z78201; CAB01588.1; -; Genomic_DNA.
DR   PIR; T28032; T28032.
DR   RefSeq; NP_506061.1; NM_073660.5.
DR   AlphaFoldDB; Q23628; -.
DR   SMR; Q23628; -.
DR   BioGRID; 44696; 1.
DR   DIP; DIP-25736N; -.
DR   IntAct; Q23628; 2.
DR   STRING; 6239.ZK836.1; -.
DR   EPD; Q23628; -.
DR   PaxDb; Q23628; -.
DR   PeptideAtlas; Q23628; -.
DR   PRIDE; Q23628; -.
DR   EnsemblMetazoa; ZK836.1.1; ZK836.1.1; WBGene00003057.
DR   GeneID; 179673; -.
DR   KEGG; cel:CELE_ZK836.1; -.
DR   UCSC; ZK836.1; c. elegans.
DR   CTD; 179673; -.
DR   WormBase; ZK836.1; CE15415; WBGene00003057; lon-3.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000174005; -.
DR   HOGENOM; CLU_001074_4_4_1; -.
DR   InParanoid; Q23628; -.
DR   OMA; NDIWGDM; -.
DR   PhylomeDB; Q23628; -.
DR   PRO; PR:Q23628; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003057; Expressed in larva and 4 other tissues.
DR   GO; GO:0060107; C:annuli extracellular matrix; IDA:WormBase.
DR   GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; ISS:WormBase.
DR   GO; GO:0010171; P:body morphogenesis; IGI:WormBase.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:WormBase.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   2: Evidence at transcript level;
KW   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..324
FT                   /note="Cuticle collagen lon-3"
FT                   /id="PRO_0000006431"
FT   REGION          119..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..152
FT                   /note="Triple-helical region"
FT   REGION          170..229
FT                   /note="Triple-helical region"
FT   REGION          235..294
FT                   /note="Triple-helical region"
FT   COMPBIAS        155..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  32941 MW;  F765A9A811DF146F CRC64;
     MSVTTATSGA LIFSGASLLV SLFAAASIYS QVSSIWTELD NEIDSFKLLT NDIWGDMINL
     GAGSASNRIR RQAYGGYGAT GTNAPEPQFP QGDKGPLPVP GLPFGPNVSG GSDRCQCTVE
     NTCPTGPDGE EGEQGPDGQD GVDGVPGFDG QDCPDVEQQP SQGCFTCPQG LPGPQGSQGA
     PGIRGMRGAR GQPGYPGRDG QPGMPGEMGP TGAPGDDGAP GASGMKGDDA EKPVGRQGQR
     GQPGEQGPDG EEGPAGKDAF EGPPGVEGEV GVPGYQGSAG PDGEEGPRGP SGLPGKDAEY
     CKCPTRDDGG NSHRAWRRKH KRVY
 
 
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