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YF1M_CAEEL
ID   YF1M_CAEEL              Reviewed;        1437 AA.
AC   Q21874;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Uncharacterized protein R09E10.5;
DE   Flags: Precursor;
GN   ORFNames=R09E10.5;
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-315; ASN-364; ASN-492; ASN-676
RP   AND ASN-914, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-315; ASN-364 AND ASN-676, 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: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; Z70287; CAA94300.2; -; Genomic_DNA.
DR   PIR; T24088; T24088.
DR   RefSeq; NP_501890.2; NM_069489.2.
DR   AlphaFoldDB; Q21874; -.
DR   STRING; 6239.R09E10.5; -.
DR   iPTMnet; Q21874; -.
DR   EPD; Q21874; -.
DR   PaxDb; Q21874; -.
DR   PeptideAtlas; Q21874; -.
DR   EnsemblMetazoa; R09E10.5.1; R09E10.5.1; WBGene00011175.
DR   GeneID; 187743; -.
DR   KEGG; cel:CELE_R09E10.5; -.
DR   UCSC; R09E10.5; c. elegans.
DR   CTD; 187743; -.
DR   WormBase; R09E10.5; CE48460; WBGene00011175; -.
DR   eggNOG; KOG4291; Eukaryota.
DR   GeneTree; ENSGT00730000110943; -.
DR   HOGENOM; CLU_004798_0_0_1; -.
DR   InParanoid; Q21874; -.
DR   OMA; LMPITWY; -.
DR   OrthoDB; 668024at2759; -.
DR   PRO; PR:Q21874; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00011175; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   InterPro; IPR005533; AMOP_dom.
DR   InterPro; IPR003886; NIDO_dom.
DR   Pfam; PF03782; AMOP; 1.
DR   SMART; SM00723; AMOP; 1.
DR   SMART; SM00539; NIDO; 1.
DR   PROSITE; PS50856; AMOP; 1.
DR   PROSITE; PS51220; NIDO; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1437
FT                   /note="Uncharacterized protein R09E10.5"
FT                   /id="PRO_0000014297"
FT   TOPO_DOM        26..1326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1327..1347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1348..1437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          193..356
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          648..829
FT                   /note="AMOP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT   REGION          1394..1419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        676
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        914
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
SQ   SEQUENCE   1437 AA;  163398 MW;  F37B933A9D82CFEC CRC64;
     MRRGCRHHLA AVVLLIATFP PLAYNQNIGG INQNIGGTPQ NPTINQVSPG QIFSGTGNNP
     FYGVNLVPFG PEAGDLMVNP SMLTSGMTID LYMFFPYYGG LYNYTTISVN GYLGFATVLD
     QGPTINVGPE TTDWPRQEDP AMIAPYLCKQ QVPQQGNPAR RAGVYYRLLL RQSLFGRESN
     SNLNLGGTLQ QNAFFGQQAS QACPGTADSY VRCDSNSDYF LDQMMIWVQE GVAGGAMFRA
     DAAVVVTWYN TASAISGRSD IDAGQTGTYQ VIWLTDSTAR LSYVIINYDR LGFDAQDFRG
     NSRSGRCRAV FNGGNHTGTV EVDPTQPYKN TPKVLAQRSG VPHMVRGRYM FRVDDVVRPA
     GCSNKTGGTY PIMIYPNIVN MLGDMTVDVN ACCLDRTQTY IMMIEEREVA TCQVINPAIA
     RCSLPRIYDW GTKTVYFQPE SRGANDEKAF VGYIYFVPPT LDPMRLDIGN IYEWYKNPMT
     NYLMPITWYP RNFTNPDILT NGNNMGVRIS DDSMYGVQLG LYIVGYREFK DDEIKKFRPE
     YRTLARITTY SNQNNANYRW MPQEEVINTN QVQQWYLTDW ERMHTLYTYR VGFFKLAPIN
     PNDANGTQLL PGLVSAPISL HWLWTPENQQ FATLTLNQQD RDQRIEFVKE KSREMCHDWY
     DEDGALWNFI RDTETNTSCP CIETQALLDL GRFMPHPRCS QMFRDITCTT VIGSKNCYMS
     SSNIYSSYAG NGNTFNNMDT NRFMTHYGQV CCYDESGYLM QTPYQPVIKT QREYFYNPGY
     PLRAYEFGTA PYMGQFEVPG LSVFHNDYMP YFLCCKFADF RCQMFYWRRP SSACQQYQPP
     AIGHAQGAGV FQTIDNDKFI FNQPGVFNFL YIPQSVRTPE VRIQTRLERY PNRKVDFGLL
     GRYISQYELV QPTNATVITG IALEATGTER VIVMTRKDTR RFRYRTNIIV GNILRYFDTI
     RLQRFRGVLI YVNNVERGQP EIYVVLEEAQ IGVKVTESYA LDIDRLPNYQ ESMGMLDIQI
     SVSPQYGVRP DGDKTQETQY RQMYNLPRVS GLIRPYPDQT SGSLNEGLTL NDVNSDSYRQ
     QIINNYLVLG TGEPGTQQNQ AGTLNQNMPQ DNMFTTSRDE DKQFDVFPEA SMRSEPVYKT
     APIFDTGSYR FVPQTGAMIL QLLNTCRDLQ NNPNTDLQPY QSIATLSYGL QCPDDPGQVL
     TECGDSVACL YDYALLNSKV LGQEEQDAWN MFTTDRALAI RQYNSCGAIN IEYPEYMMKT
     PALSSGYLQG DVARFECYQS HWVKGDHEYK CGIVVDYNRP NEYRFEWNKG NQPWCRSRIK
     ENYFKWLAVI AGIVGIIIVI LLIFLVFWCI KRKKLQESRN YSGTAAYSNN AFQNQTYETK
     PSRALSVGDL STAPRTVAMP PPRGTTATPM TLEPRGFSPV PSDVRGSQGM LGLNTSV
 
 
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