BLI1_CAEEL
ID BLI1_CAEEL Reviewed; 948 AA.
AC Q09457;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cuticle collagen bli-1;
DE AltName: Full=Blistered cuticle protein 1;
DE Flags: Precursor;
GN Name=bli-1; ORFNames=C09G5.6;
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, AND IDENTIFICATION.
RA Crew J.R., Kramer J.M.;
RT "The bli-1 and bli-2 genes encode collagens involved in strut assembly.";
RL (er) Worm Breeder's Gazette 15(2):33(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24569038; DOI=10.1534/g3.113.009522;
RA Jackson B.M., Abete-Luzi P., Krause M.W., Eisenmann D.M.;
RT "Use of an activated beta-catenin to identify Wnt pathway target genes in
RT caenorhabditis elegans, including a subset of collagen genes expressed in
RT late larval development.";
RL G3 (Bethesda) 4:733-747(2014).
CC -!- FUNCTION: Probable cuticular collagen-like protein (Probable). Nematode
CC cuticles are composed largely of collagen-like proteins (Probable). The
CC cuticle functions both as an exoskeleton and as a barrier to protect
CC the worm from its environment (Probable). Acts downstream of the Wnt
CC signaling pathway; perhaps in the formation of the adult cuticle
CC (PubMed:24569038). Required for proper strut formation within the
CC unique medial layer of the adult cuticle (Ref.2).
CC {ECO:0000269|PubMed:24569038, ECO:0000269|Ref.2,
CC ECO:0000305|PubMed:24569038}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000305|PubMed:24569038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24569038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in hypodermal cells and seam cells, in
CC the larval L4 stage, and in the young adult (PubMed:24569038). Not
CC expressed in the cells of the developing vulva (PubMed:24569038).
CC {ECO:0000269|PubMed:24569038}.
CC -!- PTM: May be processed for secretion by bli-4. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes accumulations of
CC fluid, known as blistering, in the cuticle (PubMed:24569038).
CC Hypodermal or cuticular rupture, typically in the anterior body region
CC (PubMed:24569038). Defects in cuticle integrity (PubMed:24569038).
CC {ECO:0000269|PubMed:24569038}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; Z46791; CAA86755.2; -; Genomic_DNA.
DR PIR; T19140; T19140.
DR RefSeq; NP_496311.2; NM_063910.4.
DR AlphaFoldDB; Q09457; -.
DR BioGRID; 39967; 2.
DR STRING; 6239.C09G5.6; -.
DR iPTMnet; Q09457; -.
DR EPD; Q09457; -.
DR PaxDb; Q09457; -.
DR PeptideAtlas; Q09457; -.
DR PRIDE; Q09457; -.
DR EnsemblMetazoa; C09G5.6.1; C09G5.6.1; WBGene00000251.
DR GeneID; 174653; -.
DR KEGG; cel:CELE_C09G5.6; -.
DR UCSC; C09G5.6; c. elegans.
DR CTD; 174653; -.
DR WormBase; C09G5.6; CE35827; WBGene00000251; bli-1.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000167220; -.
DR HOGENOM; CLU_311282_0_0_1; -.
DR InParanoid; Q09457; -.
DR OMA; YNTRRPN; -.
DR OrthoDB; 710836at2759; -.
DR Reactome; R-CEL-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-CEL-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-CEL-8948216; Collagen chain trimerization.
DR PRO; PR:Q09457; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000251; Expressed in material anatomical entity and 2 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0060109; C:medial layer of collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; ISS:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 2: Evidence at transcript level;
KW Collagen; Cuticle; Disulfide bond; Nucleus; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..948
FT /note="Cuticle collagen bli-1"
FT /id="PRO_0000127599"
FT REGION 65..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..408
FT /note="Triple-helical region"
FT REGION 426..488
FT /note="Triple-helical region"
FT REGION 491..552
FT /note="Triple-helical region"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 105364 MW; BC4693FFDAC8EC51 CRC64;
MVKSYTLAGL AAIACLLLAI GAVISTVYIL NDISDFYSEA QEELVEFKDI ANNIWEEMVF
ELTPEEMREA EDNDREKRSY EPEGPYQSET TTPSTTTSTA ATTTEAAEDE SGYDFVNDNG
PPSSRPRKPE PPTMPRTIQG FRAPPPAATS TYRPPHGSNY DNYGREPASS RRPYPPQQPP
STSAPHSSPN NRTSLYNPQP PPKTGYPTNP RVPYNPPQPN YTRQPTYPED NRAPYKPTRS
PNTPPPRQPS GGYDSDGQTP PSSPRIYNTR RPNNHGPGYP EDQVPTAPPV PGQQRVPPTQ
TRNPPNPTNT RQPSRPVPPT SDGHIEATTP YNPSAQYPTG KRGSHPGFGP QRPRPGTRPR
GNPCDQCSAQ PNHCPSGPPG PRGRPGPPGF PGQDGPRGLR GLNGGYSGVQ PSSYDPVIGC
VQCPIGPPGE RGPDGTPGVP GEDGIDGEQG VNGQDGQPGA PGAPGYHGMN GSPGTPGKPG
LPGRNGQSCK SIPGPPGQPG VMGVPGRDGD PGTDGEHGQD GSPGIQGPPG RDGTSGPDGQ
PGVSAPGAPG TDGGYCPCPK RSSKFDFNDA YNDDEKRGLE EHRPRGYDSE RAEEPRPRQT
VRTNTYDENS GAEHQRRPNY EPSAEVAPPR QDRYEDEERV REPPPKRPPP PHRQTPHELY
PEEQPYVRRP PPPQNRGNYE VERSREYVPE APRPRQGYEH SSGYGGDDRK EQPKYMESRP
VDEPRYETDA PSRSRPLKKV EIIRHPERGY DRRQPSYEDS KPRQEEPRRY ETEAEPRYEE
VPRKETHPPG FGRPKSEENP RETGRTYSEE AMPPVQQTEK YNGDKRKKNQ PEYEDISKPE
EDKERAMEKH HKKPNKFQEK QWEEHRKSQE LRNSREHGGQ VPVETSVPMQ QVKPESSAEE
KPVPPVHDNF QSSEKRAFSN ENPLPSEQIP YRRRNRFYRN HYYEKFLV
