ID COL99_CAEEL Reviewed; 716 AA.
AC O76368; A8WIS7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 4.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Putative cuticle collagen 99;
DE Flags: Precursor;
GN Name=col-99; ORFNames=F29C4.8;
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-474, 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-474, 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 -!- 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=O76368-1; Sequence=Displayed;
CC Name=a;
CC IsoId=O76368-2; Sequence=VSP_036609;
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; FO080227; CCD62185.1; -; Genomic_DNA.
DR EMBL; FO080227; CCD62186.1; -; Genomic_DNA.
DR PIR; T33149; T33149.
DR RefSeq; NP_001122775.2; NM_001129303.2. [O76368-1]
DR RefSeq; NP_499869.3; NM_067468.4. [O76368-2]
DR AlphaFoldDB; O76368; -.
DR BioGRID; 49891; 1.
DR STRING; 6239.F29C4.8j.1; -.
DR GlyCosmos; O76368; 1 site, No reported glycans.
DR iPTMnet; O76368; -.
DR PaxDb; 6239-F29C4-8b; -.
DR PeptideAtlas; O76368; -.
DR EnsemblMetazoa; F29C4.8a.1; F29C4.8a.1; WBGene00000674. [O76368-2]
DR EnsemblMetazoa; F29C4.8b.1; F29C4.8b.1; WBGene00000674. [O76368-1]
DR GeneID; 185112; -.
DR UCSC; F29C4.8b; c. elegans.
DR AGR; WB:WBGene00000674; -.
DR WormBase; F29C4.8a; CE46547; WBGene00000674; col-99. [O76368-2]
DR WormBase; F29C4.8b; CE46192; WBGene00000674; col-99. [O76368-1]
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; O76368; -.
DR OMA; CSWKPME; -.
DR PhylomeDB; O76368; -.
DR Reactome; R-CEL-1442490; Collagen degradation.
DR Reactome; R-CEL-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-CEL-446107; Type I hemidesmosome assembly.
DR Reactome; R-CEL-8948216; Collagen chain trimerization.
DR PRO; PR:O76368; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000674; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; O76368; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IDA:WormBase.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF428; SCAVENGER RECEPTOR CLASS A MEMBER 3; 1.
DR Pfam; PF01391; Collagen; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Cuticle; Disulfide bond; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..716
FT /note="Putative cuticle collagen 99"
FT /id="PRO_0000250375"
FT REGION 85..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..238
FT /note="Triple-helical region"
FT REGION 183..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..298
FT /note="Triple-helical region"
FT REGION 302..330
FT /note="Triple-helical region"
FT REGION 385..411
FT /note="Triple-helical region"
FT REGION 422..467
FT /note="Triple-helical region"
FT REGION 503..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..557
FT /note="Triple-helical region"
FT REGION 566..603
FT /note="Triple-helical region"
FT REGION 605..664
FT /note="Triple-helical region"
FT COMPBIAS 569..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT VAR_SEQ 126..134
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_036609"
SQ SEQUENCE 716 AA; 72187 MW; 253E00E29E5A31AF CRC64;
MTSPSPSGNV VVVGTDGTSS VSDRWPPQKT WISPPRVPID RHFVTAAVPH VLMFLLVCIV
FTAQQTRIST LEKRIDQLVV QIDQLPSSDS NTDDDDVAKS RRVRNSCMCP AGPPGERGPV
GPPGLRGSPG WPGLPGLPAP YYRRPRVPLS NNLDESISRK MRAFGMLYSP DGQAIQLRGM
PGPPGPAGPK GLRGYPGFPG PIGLDGPRGL PGTPGSKGDR GERGPLGPPG FPGPKGDRGV
MTGPYVGPHA GPGPMSHHTN MGNVLPGPPG PPGPPGPAGR DGRHGLKGDR GLPGFDGESK
IGPKGETGSP GRDGIPGARG PPGERGEKGD TAFLSTYPRV ASSSTASSPG PPGPPGPPGV
CHASQCTGIQ GPPGEPGRTI IGPQGPPGEK GERGERGEPG DRGLPGAAGA ANLLNGGKAL
VGPPGPPGRD GRPGDKGEKG EQGLRGDMGL PGPEGTPGKR GRRGRHGISL VAPNGTINED
LKKLLKTELM PLLIEDISEL RGKNVIPGPP GPPGPRGHHG PVGPSGERGP QGLPGHSGER
GDRGDIGPPG LPGQPGAGEI SGSQSGPRGP PGLPGPPGEK GDLGPPGLPG QPGSLGLPGP
PGPMGLRGPH GTEGETGKQG PEGSKGYPGP MGPQGPPGND GEPGIDGRPG PAGEKGDQGI
PGLDAPCPTG PDGLPLPYCS WKPMDGKNDV WERRKRASLP GAQPGKGAET RPPVTD
//
