YC27B_CAEEL
ID YC27B_CAEEL Reviewed; 1456 AA.
AC Q18245;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ig-like and fibronectin type-III domain-containing protein C27B7.7;
DE Flags: Precursor;
GN ORFNames=C27B7.7;
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-1207, 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 to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497; ASN-691 AND ASN-1207, AND
RP 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: Secreted {ECO:0000305}.
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DR EMBL; Z54236; CAA90982.2; -; Genomic_DNA.
DR PIR; T19506; T19506.
DR RefSeq; NP_001255352.1; NM_001268423.1.
DR AlphaFoldDB; Q18245; -.
DR BioGRID; 42816; 2.
DR STRING; 6239.C27B7.7a; -.
DR EPD; Q18245; -.
DR PaxDb; Q18245; -.
DR PeptideAtlas; Q18245; -.
DR PRIDE; Q18245; -.
DR EnsemblMetazoa; C27B7.7a.1; C27B7.7a.1; WBGene00007764.
DR GeneID; 177708; -.
DR KEGG; cel:CELE_C27B7.7; -.
DR UCSC; C27B7.7; c. elegans.
DR CTD; 177708; -.
DR WormBase; C27B7.7a; CE42680; WBGene00007764; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000176205; -.
DR HOGENOM; CLU_246685_0_0_1; -.
DR InParanoid; Q18245; -.
DR OMA; QINVTWQ; -.
DR OrthoDB; 1653734at2759; -.
DR PhylomeDB; Q18245; -.
DR PRO; PR:Q18245; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007764; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 11.
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 Pfam; PF00041; fn3; 3.
DR SMART; SM00060; FN3; 8.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 5.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1456
FT /note="Ig-like and fibronectin type-III domain-containing
FT protein C27B7.7"
FT /id="PRO_0000250557"
FT DOMAIN 24..128
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 132..227
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 236..322
FT /note="Ig-like 1"
FT DOMAIN 328..426
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 531..631
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 636..736
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 737..846
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 841..948
FT /note="Ig-like 2"
FT DOMAIN 955..1050
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1148..1234
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1236..1343
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1347..1438
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1419..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1091
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 877..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1456 AA; 163267 MW; 009DF670F8744CE7 CRC64;
MISLSLVLLL LFGVRCFDSA GQINDDSPLF ISTSIDNSMN LKILVEKKPY FTGSVTGYKL
YYTNDSSQTN EEYEKWMHQE ALSNQNSYNF VIDANKHEIV SGDVYRVRAT VFFNNVESVP
TGVISINTRQ SIPKAPLIVN TKILYNSSVL ISFVPADDVN AIENYTLMYK QMEAEEWKSL
NFKSDFDGKV LLDGLIPNHT YEIKIFVTGG IVQGTPSNLA TFTTNSTALA LVKTEPDEEY
TADPQTNEPL SITCTVKSVS KASVLWKVNG IKVSVDSSFY TVVTSVHEDF IESTIRAKSR
TRSAKFTCLA TNDAGDSSKE VNVIIKGPGS PPSEITLVAE KRGYTISWKP PSHPNGKITK
YVVYHTLNRE DPLSDWRKID LDGSEKMVRI IMDTEESFYG RVQAATELGP GIISDIVAME
RDTQPISVES DLFGVSATTM VVNPRETLSI QCTARGKPRP SISVAISDRK NASQVEVDVW
SRLQATSSAG IVSAVHNFSV LTSKFVHCRA KNSAGSNYST MELKVDKPGD APTQIQVLSV
NALDALVVWH SPQFPNSPIT SYIVLVSNDD KEDKSTWLQY ESNAKETQIN RMLLPTGNLE
KSTEYFVCVR AKNAAGIGPT SSLISFITLN GGPDSPPDNL KVLINEANQV IVYWNTPNST
TEVTGYLIYY TRDLSLSNDD YKNWQFVEMN NNSTRYKFDL SVGLKPKTFY RVRISGKNSH
ADGPASEVVE FETAYSEVPI PTDLKTEVLD DNTIHIKFNA VRDPDDHSKA LGEYRIDLAA
TDDVLHALWK QIEPKSIKID EISSMVDVEI DGDSVEKNQM YWVKVTARLD NPSWGMHSSK
PRWFRTGHGK LMTSVTLEGA PLIEKEPNLF EELSVTCTGM GSPAPIITWE WMNKSIENGT
EGWNILNIQI DDTTVVSKIT RNNIRESGDL TCLANNNEGS SSASVEIRVL GPGNPPENII
LTAYRNQINV TWQESTLPNG DIMKYIVYYS ENENDDLSDW NKFETAELET YVETFGPHTK
HFIRVQAVSD RGPGIISNVL SCISDVLYET IHLEIVASNI LDFEAEPNQN VEIRCKGTGK
PQPELFYQFA NETEQNFVEV ETNDMDLFEA KAPEINSRRN VTVTCRASNK YENVTISKVI
IIKRPGEAPT NISWSFEEEY DSTLYINWNP IENANGEKLE YNLYLSNYKT KVSGPPVKIP
DIPLDVNISL RVSAENEYGE GEKTFPIWIP TPNGGPKTAP ILSSLHAQDS KVYIFWVEPR
LPNGEIQNYT IYIQKENESE NEEHSIDKEW KKFIYGSNIT HVIIGVDDGL EENERYQMKM
TATNQRHEGP ETKVYTFDLI SFDENDVIDN FTAIVINSTV FVEVGNPIYT KYNIYIREDG
NNQTVKHEID VESGKTTFEF PFQLDHTLSY TIKMSGMKLG RESPPSEEID LEFISSPSPT
PIISGSRRKV IKEPPL