WRT6_CAEEL
ID WRT6_CAEEL Reviewed; 593 AA.
AC P91573; Q9U7D2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Warthog protein 6;
DE Contains:
DE RecName: Full=Warthog protein 6 N-product;
DE Contains:
DE RecName: Full=Warthog protein 6 C-product;
DE Flags: Precursor;
GN Name=wrt-6; ORFNames=ZK377.1;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-180, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=10523520; DOI=10.1101/gr.9.10.909;
RA Aspoeck G., Kagoshima H., Niklaus G., Buerglin T.R.;
RT "Caenorhabditis elegans has scores of hedgehog-related genes: sequence and
RT expression analysis.";
RL Genome Res. 9:909-923(1999).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Intercellular signal essential for a variety of patterning
CC events during development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 6]: Secreted {ECO:0000250}. Cell
CC surface {ECO:0000250}. Note=Also secreted in either cleaved or
CC uncleaved form to mediate signaling to other cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 6 N-product]: Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular
CC side {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 6 C-product]: Secreted,
CC extracellular space {ECO:0000250}. Note=Also secreted in either cleaved
CC or uncleaved form to mediate signaling to other cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in 4 to 7 sheath and socket cells of the
CC anterior sensilla. {ECO:0000269|PubMed:10523520}.
CC -!- PTM: The C-terminal domain displays an autoproteolysis activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080516; CCD64326.1; -; Genomic_DNA.
DR EMBL; AF139521; AAD33831.1; -; mRNA.
DR PIR; T29550; T29550.
DR RefSeq; NP_508597.2; NM_076196.5.
DR AlphaFoldDB; P91573; -.
DR SMR; P91573; -.
DR BioGRID; 45577; 1.
DR IntAct; P91573; 1.
DR STRING; 6239.ZK377.1; -.
DR MEROPS; C46.A04; -.
DR iPTMnet; P91573; -.
DR EPD; P91573; -.
DR PaxDb; P91573; -.
DR PeptideAtlas; P91573; -.
DR EnsemblMetazoa; ZK377.1.1; ZK377.1.1; WBGene00006952.
DR GeneID; 180638; -.
DR KEGG; cel:CELE_ZK377.1; -.
DR UCSC; ZK377.1; c. elegans.
DR CTD; 180638; -.
DR WormBase; ZK377.1; CE37175; WBGene00006952; wrt-6.
DR eggNOG; KOG3638; Eukaryota.
DR GeneTree; ENSGT00940000173917; -.
DR HOGENOM; CLU_034413_0_0_1; -.
DR InParanoid; P91573; -.
DR OMA; NENALWP; -.
DR OrthoDB; 1169356at2759; -.
DR PhylomeDB; P91573; -.
DR PRO; PR:P91573; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006952; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR InterPro; IPR001657; Hedgehog.
DR InterPro; IPR001767; Hedgehog_Hint.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
DR Pfam; PF01079; Hint; 1.
DR PRINTS; PR00632; SONICHHOG.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Cell membrane; Developmental protein; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..593
FT /note="Warthog protein 6"
FT /id="PRO_0000268643"
FT CHAIN 20..394
FT /note="Warthog protein 6 N-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000268644"
FT CHAIN 395..593
FT /note="Warthog protein 6 C-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000268645"
FT SITE 394..395
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT SITE 460
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000250"
FT SITE 463
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521"
SQ SEQUENCE 593 AA; 66416 MW; 1E590B780E2F4A8B CRC64;
MTLLNLFYCF CLLFGAVLAD SIHDGGSCGT NSIPYKMEVD SEGKPVISCE APSCLGVSSS
AARRPRVLDV SCDPFKEIVC VKDLQWTSGL VEINNGTHRT LKTECCSYEG MSDAKTIKSI
FLGPGQSFVG GMVEKDGEQS GFDLIKEIRK TVNADNQVQY IVGVYRMPCE ATSDSSEEAL
PLLSRNRRKL RDRVGKYDDY EEDRNYRSER RRPFAMRRRA LLQRLEDMYD DYDYEFRVVR
RPFRKSRLPY NENALWPLQY SSPQRSRTFA DNTYNKETVE SGPLPPPPSS NYIDNVAPAS
PVVQSPAYPQ TPAEMPLPPQ SGSYSGSYSG YPTADASQYN AYPAMQQPAY QPAYQPAYQP
AYQPAYQPAY QPAYSARGYS PNLNGLFGGT GMQCFSGDME VETEDGIKMI KDLKIGDKVL
SMDEAFVTYS PVIMFLHKRD EEIAEFNLIE TANGHSIKLT DNHLIYVSDC RTRSDLKLVA
AKEVKMDDCI HVTTDSNVVI KKKVSKISKV IETGIYSPLT STGDIIVNRV LASCHSNLAL
KSLQQTFFSL YKRTSSVFHN LMFFKSSTEE GDLPVGVETL TSVMDLFIPQ SFV
