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Database: UniProt
Entry: O44443
LinkDB: O44443
Original site: O44443 
ID   YC2BA_CAEEL             Reviewed;         247 AA.
AC   O44443;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=EGF-like domain-containing protein C02B10.3;
DE   Flags: Precursor;
GN   ORFNames=C02B10.3;
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], AND ALTERNATIVE
RP   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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126, AND IDENTIFICATION BY
RP   MASS 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
RT   to identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126, AND IDENTIFICATION BY
RP   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: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
DR   EMBL; FO080093; CCD61165.1; -; Genomic_DNA.
DR   PIR; T32590; T32590.
DR   RefSeq; NP_500723.1; NM_068322.3.
DR   UniGene; Cel.13615; -.
DR   ProteinModelPortal; O44443; -.
DR   SMR; O44443; -.
DR   STRING; 6239.C02B10.3; -.
DR   iPTMnet; O44443; -.
DR   EPD; O44443; -.
DR   PaxDb; O44443; -.
DR   PeptideAtlas; O44443; -.
DR   PRIDE; O44443; -.
DR   EnsemblMetazoa; C02B10.3; C02B10.3; WBGene00015328.
DR   GeneID; 177284; -.
DR   KEGG; cel:CELE_C02B10.3; -.
DR   UCSC; C02B10.3.1; c. elegans.
DR   CTD; 177284; -.
DR   WormBase; C02B10.3; CE29018; WBGene00015328; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; ENOG410XZMQ; LUCA.
DR   HOGENOM; HOG000021767; -.
DR   InParanoid; O44443; -.
DR   OMA; RCADEYE; -.
DR   OrthoDB; 1120031at2759; -.
DR   PhylomeDB; O44443; -.
DR   PRO; PR:O44443; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00015328; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   SMART; SM00181; EGF; 2.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
PE   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    247       EGF-like domain-containing protein
FT                                C02B10.3.
FT                                /FTId=PRO_0000248517.
FT   TOPO_DOM     18    220       Extracellular. {ECO:0000255}.
FT   TRANSMEM    221    240       Helical. {ECO:0000255}.
FT   TOPO_DOM    241    247       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      114    150       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      180    213       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    126    126       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754521,
FT                                ECO:0000269|PubMed:17761667}.
FT   DISULFID    123    138       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    140    149       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    190    201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    203    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   247 AA;  27307 MW;  700CB226F2AECC38 CRC64;
     MTGALCIVLF GVTMVTAERP KIKDTHGNLL VKLSDIPIGS CGDESYFGLG IMDGGLEECD
     RWKLEVTNPE YEEYKCKVLR VHASVQNGKC TCNINWKGPI CNEYDGCGKG ETLFGTSCTP
     HMCQHNGTIA VGKKEIECIC PPPWDGRFCE RLACWRKTIS TQQHRYRNNG DHCICGNHYS
     GASCDVIKSC LNNGQLIDGK CKCPDGYYGD LCDKRCQKGH VTCSTCSSFI PAALFAIILL
     CVNKFNY
//
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