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Database: UniProt
Entry: G5EF89_CAEEL
LinkDB: G5EF89_CAEEL
Original site: G5EF89_CAEEL 
ID   G5EF89_CAEEL            Unreviewed;      1138 AA.
AC   G5EF89;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Fibronectin type-III domain-containing protein {ECO:0000313|EMBL:CAD21701.2};
GN   Name=cle-1 {ECO:0000313|EMBL:CAD21701.2,
GN   ECO:0000313|WormBase:C36B1.1a};
GN   ORFNames=C36B1.1 {ECO:0000313|WormBase:C36B1.1a}, CELE_C36B1.1
GN   {ECO:0000313|EMBL:CAD21701.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAD21701.2, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAD21701.2, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAD21701.2,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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DR   EMBL; BX284601; CAD21701.2; -; Genomic_DNA.
DR   RefSeq; NP_740896.2; NM_170904.2.
DR   AlphaFoldDB; G5EF89; -.
DR   SMR; G5EF89; -.
DR   EPD; G5EF89; -.
DR   EnsemblMetazoa; C36B1.1a.1; C36B1.1a.1; WBGene00000527.
DR   GeneID; 172678; -.
DR   KEGG; cel:CELE_C36B1.1; -.
DR   AGR; WB:WBGene00000527; -.
DR   WormBase; C36B1.1a; CE36988; WBGene00000527; cle-1.
DR   OrthoDB; 5363002at2759; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00000527; Expressed in larva and 4 other cell types or tissues.
DR   ExpressionAtlas; G5EF89; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR   GO; GO:0030054; C:cell junction; IDA:WormBase.
DR   GO; GO:0005587; C:collagen type IV trimer; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR   GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR   GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR   GO; GO:0050808; P:synapse organization; IMP:WormBase.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR   CDD; cd00247; Endostatin-like; 1.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 2.
PE   1: Evidence at protein level;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Proteomics identification {ECO:0007829|EPD:G5EF89,
KW   ECO:0007829|PeptideAtlas:G5EF89};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1138
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003476142"
FT   DOMAIN          35..126
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          136..237
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          152..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..638
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1138 AA;  124178 MW;  B2C69581A4BCFB80 CRC64;
     MIETGSQYLL FLLFICSLFN SGSTALQHED RVPNAPQNVR IKTQSTSATL WWDAPPDPTV
     LIRGYTVEYG EGSISQRILI EGPDSTSFTV TRLSPNTNYV FAVSAYNEAE GEDGTKVMVA
     AKTRPSEGSQ TEKLWPPTSV RARIDEKSAA GSAFVSWDDP NPESSSENSI DSTQKQYVIN
     YGIYESDTQQ KVRSNAKAVR LTGLIPGKEY EVAVKVVAGD GRESPWSIRD LFLVPETKTV
     SKFDWFCRLN DTEMCSIHSS PHWKLCSEKH DTYTQRDAGA CPRVQYPSSP AHLTTPAINL
     PDAQRLCLYF RFALLNFHPG QMKVEIFRDG DMANKQIVWK TRMANVRTHV VQNVYVPFSQ
     QIKPFKVSVS LKWDGQPMPR VIVHEMDVLS GGCSERSTDS ETEVDLLAPV KASLNADARV
     FRAKGIESLP AIGLQRGVEI AVPYRLYLPR NFFKQFSLLA TIKPMDKRGG YLFAAVNAYD
     SAVDIGLLIE PAGTKQTNIS LIVRSVAIVS FLVEDFSQQW TQFALEVVDQ TVTFYFKCRR
     FASRQVTSLP DFSFDEAEKL YIASAGPIID NGFEGAIQEL KLIDDATQGS RQCDEQWGAE
     GSGTPEEFKK TQESSELQKI SDFPPTPAPP PPYPTPQLAP HDLRSYEQQA ATTPFQGAPP
     SNQCTQVCRG EPGPQGPSGN DGIPGSHGAP GHQGERGADG APGLHGSRGD QGLPGPPGMP
     GLAGPPGPPG SGTGHGSGAD GPQGPPGLPG APGRDGTSGV EGQRGPQGPP GPKGDDGVSM
     ESLTDDDIER IARRVASIQK ESNEPMRGDL PEYNSKVHSF TTKGEKGERG APGAPGAPAP
     PAYGTLTTGT AVNVHATTVE LFASARSTSV GQLAFATSSQ QLFIRVTNGW KEIQLTHFHP
     FVETRHSTQN SRQNDASHAG RSRTGSAAAP WYPKANLDEP QRDAGVHNKD RVIHMIALSQ
     PFSGNLHGLR GADLQCYREA RAAGYTTTFR AMLSSNVQDL VRIVHSVDFD TTVVNVAGHH
     LFPSWRSFVN GAQMNPHAKL FSFDRHDVLN DSRWPDKRVW HGSKDGGIRA EQYCDGWRRA
     DSSLTSLAGH ISSNTSIFQS SGSEKCENKL VVLCVENMSK YHGDRILRLH RITSDFKK
//
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