IGDB1_CAEEL
ID IGDB1_CAEEL Reviewed; 1029 AA.
AC O18016;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ig-like and fibronectin type-III domain-containing protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=igdb-1 {ECO:0000312|WormBase:T04A11.3};
GN ORFNames=T04A11.3 {ECO:0000312|WormBase:T04A11.3};
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-165, 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-36; ASN-165; ASN-374; ASN-409;
RP ASN-442; ASN-482 AND ASN-552, AND IDENTIFICATION BY MASS 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; Z83123; CAB05606.2; -; Genomic_DNA.
DR PIR; T24412; T24412.
DR RefSeq; NP_502387.2; NM_069986.2.
DR AlphaFoldDB; O18016; -.
DR iPTMnet; O18016; -.
DR PaxDb; O18016; -.
DR PeptideAtlas; O18016; -.
DR EnsemblMetazoa; T04A11.3.1; T04A11.3.1; WBGene00011418.
DR GeneID; 3565301; -.
DR KEGG; cel:CELE_T04A11.3; -.
DR UCSC; T04A11.3; c. elegans.
DR CTD; 3565301; -.
DR WormBase; T04A11.3; CE42641; WBGene00011418; igdb-1.
DR GeneTree; ENSGT00940000156511; -.
DR HOGENOM; CLU_005277_0_0_1; -.
DR InParanoid; O18016; -.
DR OrthoDB; 74751at2759; -.
DR PhylomeDB; O18016; -.
DR PRO; PR:O18016; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011418; Expressed in adult organism and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR002602; DB.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF01682; DB; 3.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00289; WR1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1029
FT /note="Ig-like and fibronectin type-III domain-containing
FT protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000248520"
FT TOPO_DOM 23..918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 90..181
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 185..227
FT /note="WR1"
FT DOMAIN 330..417
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 427..523
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 619..710
FT /note="Ig-like C2-type"
FT DOMAIN 817..909
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 988..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 640..693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1029 AA; 113674 MW; D57B2BB0D0769253 CRC64;
MCNVAEDPSS FSTITIATTC RAEWPKVSPC IADGRNHTDC CLKKGVQHDC LEICSGSTKE
LGVHSVLCLN LDLQAIYQCI RQGYETHPSA PGNVTISELT AHSVTVQWTE PNSNAHLVEN
YTLFIRKNEH GEAVRTVKNV ISPHVELGLD PDSEYVLTLQ SHSANGTSLP STAKLFSTLP
TTRPPLCTIG EPIYMNDGRV MICDAVNPCP NGFRCTGAGS DLSYCCPHDG THSSEEFTSC
CKEQKMPESC MSSCQYNMTL PESCKENLNT WVQCASEGHD HLRCCLQEEV SKPCQTACMH
PFTVPADECF SEVSKYRTCF SAAHQALPAA VRNVEVSSIS KDSATISWED LEANIIVFRV
QLFEKGGNLI KTENSSADIF RFIDLEPNKD YSVRVTAINF LGEGPPSWNA TFTTKPAQIY
EGDRPVAPEK LRISWNSGPR VNVTWDPVSV RRNAEVVTKP IEYTIYYLDT EQSSTWTTLR
TNQTWVVMRD LRKDALYYVY VTAKEDNRTS RSSSIITILA QKDSPGLPEP TIVIEPDHKD
GVFSPGEKIS INCSLPNIKK HLNIDLTVGS HVVQNDHGAL WVILETEADE AMDTATCAVS
DTDGRQHVAM KHLVLERKAS VTMKKDKIRV LDDQSVEIEC IYRGGGLDPK ISFEKDGKKA
SRGFLNLKKT EAGYVAKWHI RKVKQEDAGF YKCVVTSSDG SRVEASSEVI FSTETLPVNP
KLILQCCEDE GITGDCLQAC NIGRTSLSIK NQNCTRFAVS LLKCASDIRD HSDCCIASGV
TSKCLPLCSG DSFSPDIDCS EHAVSIMTCS VKSHEHAPSE VSNVRIKASE GKVNIEWDYP
LTKDYKYFAV YYRKAHDDHE DWHKLKTIQQ NIELDVDPSE DYEVGILAAN ALGHSRLMYS
AIPKDSEPRR SASKGSSSAF WIVVILVVFG VLIAGLAVLS KRRELPYPIG KFIGRRNDPN
QPTVAFENPA YGEPWGGAEV EIRGLGGSAT TGTAAATQSE WQSANLEANS TTDNSHEYRN
GMRYAKLET
