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   03-AUG-2022, entry version 122.
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 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-126, 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-126, AND IDENTIFICATION BY MASS
RP   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}.
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DR   EMBL; FO080093; CCD61165.1; -; Genomic_DNA.
DR   PIR; T32590; T32590.
DR   RefSeq; NP_500723.1; NM_068322.3.
DR   AlphaFoldDB; O44443; -.
DR   STRING; 6239.C02B10.3; -.
DR   iPTMnet; O44443; -.
DR   EPD; O44443; -.
DR   PaxDb; O44443; -.
DR   PeptideAtlas; O44443; -.
DR   EnsemblMetazoa; C02B10.3.1; C02B10.3.1; 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   HOGENOM; CLU_1262937_0_0_1; -.
DR   InParanoid; O44443; -.
DR   OMA; CRCADEY; -.
DR   OrthoDB; 1120031at2759; -.
DR   PhylomeDB; O44443; -.
DR   PRO; PR:O44443; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00015328; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..247
FT                   /note="EGF-like domain-containing protein C02B10.3"
FT                   /id="PRO_0000248517"
FT   TOPO_DOM        18..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..247
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..150
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          180..213
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   DISULFID        123..138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        140..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        190..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        203..212
FT                   /evidence="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