ID   YAO6_CAEEL              Reviewed;        1423 AA.
AC   Q20762;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 4.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Uncharacterized protein F54D1.6;
DE   Flags: Precursor;
GN   ORFNames=F54D1.6;
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-306; ASN-355; ASN-483 AND
RP   ASN-666, 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-355; ASN-666 AND ASN-903, 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 membrane
CC       protein {ECO:0000305}.
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DR   EMBL; Z77132; CAB00863.2; -; Genomic_DNA.
DR   PIR; T22643; T22643.
DR   RefSeq; NP_502119.2; NM_069718.4.
DR   AlphaFoldDB; Q20762; -.
DR   SMR; Q20762; -.
DR   STRING; 6239.F54D1.6; -.
DR   iPTMnet; Q20762; -.
DR   EPD; Q20762; -.
DR   PaxDb; Q20762; -.
DR   PeptideAtlas; Q20762; -.
DR   PRIDE; Q20762; -.
DR   EnsemblMetazoa; F54D1.6.1; F54D1.6.1; WBGene00010047.
DR   GeneID; 178037; -.
DR   KEGG; cel:CELE_F54D1.6; -.
DR   UCSC; F54D1.6; c. elegans.
DR   CTD; 178037; -.
DR   WormBase; F54D1.6; CE37523; WBGene00010047; -.
DR   eggNOG; KOG4291; Eukaryota.
DR   GeneTree; ENSGT00730000110943; -.
DR   HOGENOM; CLU_004798_0_0_1; -.
DR   InParanoid; Q20762; -.
DR   OMA; IRESYNL; -.
DR   OrthoDB; 668024at2759; -.
DR   PhylomeDB; Q20762; -.
DR   PRO; PR:Q20762; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00010047; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1423
FT                   /note="Uncharacterized protein F54D1.6"
FT                   /id="PRO_0000014285"
FT   TOPO_DOM        29..1321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1322..1342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1343..1423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          184..347
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          638..818
FT                   /note="AMOP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT   REGION          1364..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        903
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   1423 AA;  163201 MW;  3B779D522BF4FFE4 CRC64;
     MTSSVRLAFL ATLLLLLPLE AQIQQANSAN VNQNVGQQDT GTLFTGTGTN LYYGVNLVPF
     GPEVGDQEVN PGLLTAGQTI DLHMYFPFYG GLYNYSTLSV NGYIGFATVL DQGPTLNVGP
     DMTDWPRHED PAMIAPYLCK QQIPQNLNPG MRSGVFYRLM MRQSLFGRQT GSNMNMGQAT
     YQSSFFGQSA SKACPGTPDS YVRCDSQADY FLEEMQRWLI EGVAGAAAFR ADAALVVTWY
     NTASAISGRS DIDSGQLATY QAIWLTDRTA RLSYVILNYD RLGFDAADFR QNSRSGRCQA
     LFNGGNHTGL VPVDPTQDFK NTPKVLAQRS GVPQMVRGRY MFRVDDVVRP AGCSNKTGGT
     YPMLIYPNIV NMLGEMTVDV NAICLDKSQT YILMIEQRQT ATCTVLTSAI ARCNLPKIFD
     WGTKTVYFQP QSGGANDEKA FVGYIYFVPP TLDPMRLDIG NVYDWFKNPL PYTTMPLVWY
     PRNFTNPEMT QHMDQVRMND DTLYSTQLGL YVIAYREYKD DTIKKFRPEH RVICRLATYS
     NRNTYEYRWK PQEERINLYQ VEQWYMNDWE RQNDLYHYRF GYLKLAPLKT NQEQNPQQLL
     SGLVSSPISL HFLWTSNNPQ FATTTYSQQD ESARTEYVKK KSLEMCHDWY DEDGAQWNFI
     RDTETNSSCP CIERQAIADI GRFMPHPRCS QAFRDITCTT SIGSRNCYMS SQNVMTTYAG
     DGRQYNENLA RFPTHYGQVC CYDDQGHLMQ TSYQPVIKVT PEVPYNPGFP MRAYEFGTAP
     YMGQYEVPGL SAFHNDYMPY FLCCKFADFR CQMFYWRRPS SGCQEYQPPA YGEVMGAGTF
     NTIDNDKFIF NEPGVYNGLY IPHTLSTPEV KVQIRMERYP NRRVDFSLLG RYMAQQDLVQ
     PTNATVVTGV VLEATGTDRV HVVARKDTRR FRYRTSIIVG NILRYFDTMR IQRFKGVMIY
     VNNVERGQPE IYVVLEEAQI GIRVRESYAI DIDRLSEYQE SMGILNIAVS VPPQYGVRPD
     GDKTREQEIR QRYNLPRVSG VFRPFPDQSS GSYLNTLTLN DVNSETYRQQ IINMYRVQGS
     GEPGSDQNIN NQGNNYGMPT ENMFTTSRDE DKKFEVFPEA QMKSGPIFKT SPKYETGAYR
     FYPMTGQVLN QRLQTCRDMQ QNTNINMQPL QSQLTGEYGQ TQCPDNPSSI IQDCGDSVPC
     LYDYYNFNAK LLGLNVKNEW NTFTSDRFDA SRQYNSCGVI NIEYPEYLMK TSSMSSAYLQ
     GDVARFECFQ SHWIYGVHEY KCGIVVDRNQ RNIIDPRDYR FEWNKGEQPW CRSREKQNFL
     TWLAIIGGIF GVLVFVILIF LCCWIVKQKK KGEAAERRGY DMASRSSMTG SRGGKKYPIH
     ESEPLNEKRF DADTYRDDDF YPPAREEQYA ARNEDLHGLK TSV