ID Q9XUF9_CAEEL Unreviewed; 1566 AA.
AC Q9XUF9;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 160.
DE SubName: Full=EGF-like domain-containing protein {ECO:0000313|EMBL:CAB05159.1};
GN ORFNames=C49C3.4 {ECO:0000313|EMBL:CAB05159.1,
GN ECO:0000313|WormBase:C49C3.4a}, CELE_C49C3.4
GN {ECO:0000313|EMBL:CAB05159.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB05159.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB05159.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB05159.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; BX284604; CAB05159.1; -; Genomic_DNA.
DR PIR; T20058; T20058.
DR RefSeq; NP_503080.1; NM_070679.5.
DR AlphaFoldDB; Q9XUF9; -.
DR SMR; Q9XUF9; -.
DR STRING; 6239.C49C3.4a.1; -.
DR EPD; Q9XUF9; -.
DR PaxDb; 6239-C49C3-4a; -.
DR PeptideAtlas; Q9XUF9; -.
DR EnsemblMetazoa; C49C3.4a.1; C49C3.4a.1; WBGene00008194.
DR GeneID; 178513; -.
DR KEGG; cel:CELE_C49C3.4; -.
DR UCSC; C49C3.4; c. elegans.
DR AGR; WB:WBGene00008194; -.
DR WormBase; C49C3.4a; CE19743; WBGene00008194; -.
DR eggNOG; ENOG502SDXV; Eukaryota.
DR HOGENOM; CLU_247724_0_0_1; -.
DR InParanoid; Q9XUF9; -.
DR OMA; PQYVSIQ; -.
DR OrthoDB; 2882196at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008194; Expressed in material anatomical entity and 5 other cell types or tissues.
DR ExpressionAtlas; Q9XUF9; baseline and differential.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR PANTHER; PTHR24041; MUCIN; 1.
DR PANTHER; PTHR24041:SF30; MUCIN-3A; 1.
DR SMART; SM00181; EGF; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Proteomics identification {ECO:0007829|EPD:Q9XUF9,
KW ECO:0007829|PeptideAtlas:Q9XUF9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004336713"
FT DOMAIN 31..65
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1067..1105
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1498..1531
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 499..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 55..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1076..1093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1095..1104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1521..1530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1566 AA; 169746 MW; FC14838C61C892A8 CRC64;
MLQKTALIIG ALSLISGVFS DDCPSFFNKD DNGNCTIRQC TNGGYLDVSK QICICPSGYL
GIHCEAVKTS LPPDNHFKVG GTSFNIININ LYTEYWGVST YANIQKGLEA HFDAYPTGYD
NYNLVETRGT PYLDNIDQPQ YDSISFNYDN INSNISFSLA DLEDTGIYWC YEVAIYENLI
QMIQKGGLKN TVITIVTQHP PLAEFHDEAR QIAVAFGIRI NVLWISDIVF NACSDEQISD
FKTFVDITGG LFVQLQAENG DQNNINLISQ VLLTHYKPQY VSIQSFPDCT SGQIIPVVAD
PVVSGPYNFV FLGASANPTI PLFTACHLRQ PLRSYDNQLA IFQSPDPTNP DCANLNITTA
SGGCTGIVFT NAAPASGPLD LAISTTYVEN PSIDASRYAI VEGVPFYPAL HVESNPTAQI
TLNSISASFD RSWNPQLQKR SPAAFEWIPS TTIKCDSTKT YSLFLNISVD LTIVQRAVRV
ACVPVPVITT TTAAATTTEP LASTTTGEAS STTTGEASST TTGEASSTTT GEASSTTTGE
ASSTTTGEAS STTTGEASST TTGEATSVAA TTSSASSTVV TSTEMPSSTS QAVCTTQDNS
ATFLFAYAAD FDPTTYGLVS RTIGSYVTAN LPTGQTLANV LTDLTTEMDI KYTNVANDFT
TNCVTDQPDA TLARSEVQAS TALQTIQQFL KNANATMRLE GSIIILLVNR LPKNDDDLIS
GEYDQLTNLN VKIFPIITIR NLVEHSAIAS RSGAVFNRIA AQTNGHYIVA NDTIGVDVNS
DFNKIIANFM KTSYNQNLLF VRNIGSNRFL SLGSSIGTLR IPKSPTESAT VPVTITVSLS
AVDTNVPQLP RRLLLAILGN SKFNQTKTVQ IDFLNPENVT SFANSNYYTT TVNLDAGIEN
NLILLYDAGP DQNDVLIRMW TPNAIHRSAS YVNAKSEPLT PVNKITESTG AALKFTLENQ
CSSDKTATLL ITDCNGEVSA KYDSDQIFNW KDNSTFYQFV PFFCDNQPTP TTCISGAESK
YDAQFVSNDF SVTQSFQCRP GNGPTDNCKL KDSNGNYQCS GTSPFMRGPE GSLTDCSGHG
HLEYDEPTKL FSCICDPGFS GPSCEIVTCT NQNTDPLAKD NAYHTYTVVV GLEKTNGFLV
FDDAKVLFGL PGLNGTVDLP EVWKYQLLTI CADGVFDMIY SGSDLGEFQR LFTSPNYELL
ARTCNTPPSP GVNDLTTIYK EAVKGIGRNV KGIIVYFSEV SSMINVTLDE FIAASQPYQQ
QFFVYAVDET SMPILPNGER IAKAAMTTGG FLIQSYITDD VKGHLDTQFI PDFLQSSTSI
AWYSSDQVDD FTYFTQNNIF AYVITWNVGD NFKINNGVPF RNCQIAGNEN VECKIQGPQT
VKGNIDRGAF YVAVYLLDDP LIPKVQIISD LDRDSSNAVS TSSSDTRTML TFNIPEEYDI
VANSGDGGVT RNAQRNGCTF DWTAYSVFAT QKYTPGLNIA KITLQDASSN TYTRFFPFGT
SSAPVCQNGG TPIQSDGSCL CPSGFQGSDC SLVNCSQSST SNAWSDVCVC NEIDDATCAR
QFTSIF
//