ID A0A8S1F5M5_9PELO Unreviewed; 1178 AA.
AC A0A8S1F5M5;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN ORFNames=CBOVIS_LOCUS9117 {ECO:0000313|EMBL:CAB3407148.1};
OS Caenorhabditis bovis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=2654633 {ECO:0000313|EMBL:CAB3407148.1, ECO:0000313|Proteomes:UP000494206};
RN [1] {ECO:0000313|EMBL:CAB3407148.1, ECO:0000313|Proteomes:UP000494206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAB3407148.1}.
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DR EMBL; CADEPM010000006; CAB3407148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8S1F5M5; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000494206; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00063; FN3; 2.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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; IPR050149; Collagen_superfamily.
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:SF845; COLLAGEN ALPHA-1(XXII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF00041; fn3; 2.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000494206};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1178
FT /note="Fibronectin type-III domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035789673"
FT DOMAIN 27..121
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 131..229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 735..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 129285 MW; 2B1E3AC469ED4AE5 CRC64;
MRTKGVSLTL IFILRNANAI FKHENYVPNA PQNVRVKTQA TSAVLWWEAP SDTSVLIRGY
TVEYGEESIS KRIVIEGPDS TSFTVTRLEP DTNYVFAVSA YNEADGEDGA KVMLTAKTLP
LDGYTSEKLW PPTSVRSKIL DDNVAIVSWD DPNAEQSSEN SIDAHQRQYI VNYGIHGEEI
QQKVRSNAKS VKLTNLLPGK EYEVAVKVAA GNGMESSWSI RDLFVVPEVK KPYEASKFDW
SCHIDDENMC SLSLSPHWKF CAAREDHHTK RMSGVCPKTS YPHHTALIST PPIELPNAQN
LCLHMQYALL QFHPGHMKVE IIGGSNASTR NVVWKTKMAN VKTHIIQNLY LPIARQINPF
KIAISVKWDI EHQIPRLIFH HFAVSSGGCA ERTIDTETEV DLLAPVEASL NADSRVFRAK
GIDSLPAIGI QRGVEIAVPY RLYLPRNFFK QFSLLATVKP MDKMGGYLFA AVNAFDSAVD
IGLLIEPSGT KQSNISFIIR STAIASFIVE DFSQEWTQFA LEVSPTTVTF YFKCQRYGTK
HISSLPNMNF DEAEKLYIAS AGPIIDNGFE VMRVELIAIL LLAAGLANCH DAIDGDDDDE
VLLTENWEQL AFIDNETDER NPTVYQIQLA HDNVHLRHVR SSNEDTSIPP VEPIEGAIQE
LKLIDDASQG ASQCDEQWID GSGSAEMSNA PEVEVRKSQI LPPIPSPPPP LPNPIQQEDQ
ITVAKMLPQT CQQVCKGEIG PMGPPGPKGS DGMDGVPGSH GAPGRPGEPG PMGPPGLQGE
RGDQGPPGPA GMPGLPGPPG PVAAHVNQVG GQSVAAVEGP PGPPGQPGLP GPPGRDGFHG
EQGPMGPPGP PGPRGEDGRS VENLSEADVE RIARRVAALS KYNKVAENVH KPSVDFGRAS
MTPNIYATTV ELFASARATS VGQLAFATSS QQLFIRVNNG WKEVQLTHFH PAVEARKSAQ
NSRQNDVGEN PPMSIWQPRP VEHPQRDGAH NKDRKIHMIA LSNPTNGNMH GLRGADLQCY
REARAAGFTT TFRAMLSNNV QDLVKIVHHA DADTPVVNLA GQHLFPSWRA FINGAHISQA
QLFSFDRHDV LHDSKWPDKR IWHGSKADGT RGETYCDGWR RADANQHSLA GFVFSNTSLL
QSATRVACDT KLVVLCVENM SKYHIEKILR LRRLQHDF
//
