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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
 
 
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