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