IGDB2_CAEEL
ID IGDB2_CAEEL Reviewed; 1526 AA.
AC O18023; C1P642; Q18174; Q95ZY5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ig-like and fibronectin type-III domain-containing protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=igdb-2 {ECO:0000312|WormBase:C25G4.10a};
GN ORFNames=C25G4.10 {ECO:0000312|WormBase:C25G4.10a};
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-427, 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-87; ASN-158; ASN-181; ASN-414;
RP ASN-427; ASN-489; ASN-533; ASN-662; ASN-871; ASN-906; ASN-939; ASN-979 AND
RP ASN-1049, 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O18023-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O18023-2; Sequence=VSP_039736, VSP_039737;
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DR EMBL; Z70680; CAC42260.1; -; Genomic_DNA.
DR EMBL; Z70680; CAX65049.1; -; Genomic_DNA.
DR EMBL; Z83123; CAX65049.1; JOINED; Genomic_DNA.
DR PIR; T19473; T19473.
DR RefSeq; NP_001255649.1; NM_001268720.1. [O18023-1]
DR RefSeq; NP_001255650.1; NM_001268721.1. [O18023-2]
DR AlphaFoldDB; O18023; -.
DR STRING; 6239.C25G4.10a; -.
DR iPTMnet; O18023; -.
DR EPD; O18023; -.
DR PaxDb; O18023; -.
DR PeptideAtlas; O18023; -.
DR PRIDE; O18023; -.
DR EnsemblMetazoa; C25G4.10a.1; C25G4.10a.1; WBGene00007736. [O18023-1]
DR EnsemblMetazoa; C25G4.10b.1; C25G4.10b.1; WBGene00007736. [O18023-2]
DR GeneID; 178199; -.
DR KEGG; cel:CELE_C25G4.10; -.
DR UCSC; C25G4.10; c. elegans. [O18023-1]
DR UCSC; C25G4.11; c. elegans.
DR CTD; 178199; -.
DR WormBase; C25G4.10a; CE15638; WBGene00007736; igdb-2. [O18023-1]
DR WormBase; C25G4.10b; CE28207; WBGene00007736; igdb-2. [O18023-2]
DR eggNOG; ENOG502QRA3; Eukaryota.
DR GeneTree; ENSGT00940000156511; -.
DR HOGENOM; CLU_005277_0_0_1; -.
DR InParanoid; O18023; -.
DR OMA; CCAAQNV; -.
DR OrthoDB; 74751at2759; -.
DR PhylomeDB; O18023; -.
DR PRO; PR:O18023; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007736; Expressed in embryo 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; 4.
DR Gene3D; 2.60.40.10; -; 7.
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; 4.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00289; WR1; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1526
FT /note="Ig-like and fibronectin type-III domain-containing
FT protein 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000248521"
FT TOPO_DOM 20..1415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1416..1436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1437..1526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..170
FT /note="Ig-like C2-type 1"
FT DOMAIN 379..470
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 587..678
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 682..724
FT /note="WR1"
FT DOMAIN 827..914
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 924..1020
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1116..1207
FT /note="Ig-like C2-type 2"
FT DOMAIN 1314..1406
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 979
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1137..1190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 285..319
FT /note="LPYPDPPTAIEVNAVEHDKLSVCWKEPEKHESNKM -> RMLSNEKGGVSSA
FT RGGAGGAAHLSAFMIDKPVRG (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_039736"
FT VAR_SEQ 320..1526
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_039737"
SQ SEQUENCE 1526 AA; 169660 MW; 35351BE1DF0CA800 CRC64;
MMRWRLAVLF LTLLASTTGD DTTTKASVST TTKKGTDGPH LTTDDEGFLT VIQGFATQLQ
CVLNTCSKDV IWYKDGSQIS KGSQFLNTTS EKAYKIQHSI EVDYEKGCSG ECDDSKPCGD
GFSCVDNQCC SCRREEFTLV LRNLTFDESG RYRCQLGNKS ELLEFQVEVL ESGLKGGFHE
NISYDHSECC QEKGISPLCR GMCKPSEMDQ HHFDPTSCKT DDYKHFLSCA TEDGTRSHVH
CCKTQLVPSF CYDFCSGDFQ MLRRSHRLCL YYLPEIFSCL DRAYLPYPDP PTAIEVNAVE
HDKLSVCWKE PEKHESNKMF PILDYAVYFK EIPNFPLLGG DMGLPLLTGD YSDIGDIQED
DYQQEEDDAE EVVKDSTIAP RGKRDVDFES DGVKVQIREK RSTMVIVTRD DVTNSTTIRE
FAFQNVNTTE RCVTLSDLRS STRYIVYVTA RNEYGTSVPS VRNIASTNVH MVKNNASLPD
SMKCCTDANV TSFCSSKMCN VAEDPSSFST ITIATTCRAE WPKVSPCIAD GRNHTDCCLK
KGVQHDCLEI CSGSTKELGV HSVLCLNLDL QAIYQCIRQG YETHPSAPGN VTISELTAHS
VTVQWTEPNS NAHLVENYTL FIRKNEHGEA VRTVKNVISP HVELGLDPDS EYVLTLQSHS
ANGTSLPSTA KLFSTLPTTR PPLCTIGEPI YMNDGRVMIC DAVNPCPNGF RCTGAGSDLS
YCCPHDGTHS SEEFTSCCKE QKMPESCMSS CQYNMTLPES CKENLNTWVQ CASEGHDHLR
CCLQEEVSKP CQTACMHPFT VPADECFSEV SKYRTCFSAA HQALPAAVRN VEVSSISKDS
ATISWEDLEA NIIVFRVQLF EKGGNLIKTE NSSADIFRFI DLEPNKDYSV RVTAINFLGE
GPPSWNATFT TKPAQIYEGD RPVAPEKLRI SWNSGPRVNV TWDPVSVRRN AEVVTKPIEY
TIYYLDTEQS STWTTLRTNQ TWVVMRDLRK DALYYVYVTA KEDNRTSRSS SIITILAQKD
SPGLPEPTIV IEPDHKDGVF SPGEKISINC SLPNIKKHLN IDLTVGSHVV QNDHGALWVI
LETEADEAMD TATCAVSDTD GRQHVAMKHL VLERKASVTM KKDKIRVLDD QSVEIECIYR
GGGLDPKISF EKDGKKASRG FLNLKKTEAG YVAKWHIRKV KQEDAGFYKC VVTSSDGSRV
EASSEVIFST ETLPVNPKLI LQCCEDEGIT GDCLQACNIG RTSLSIKNQN CTRFAVSLLK
CASDIRDHSD CCIASGVTSK CLPLCSGDSF SPDIDCSEHA VSIMTCSVKS HEHAPSEVSN
VRIKASEGKV NIEWDYPLTK DYKYFAVYYR KAHDDHEDWH KLKTIQQNIE LDVDPSEDYE
VGILAANALG HSRLMYSAIP KDSEPRRSAS KGSSSAFWIV VILVVFGVLI AGLAVLSKRR
ELPYPIGKFI GRRNDPNQPT VAFENPAYGE PWGGAEVEIR GLGGSATTGT AAATQSEWQS
ANLEANSTTD NSHEYRNGMR YAKLET
