WRT8_CAEEL
ID WRT8_CAEEL Reviewed; 550 AA.
AC Q94130; O45273;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Warthog protein 8;
DE AltName: Full=Protein M89;
DE Contains:
DE RecName: Full=Warthog protein 8 N-product;
DE Contains:
DE RecName: Full=Warthog protein 8 C-product;
DE Flags: Precursor;
GN Name=wrt-8; ORFNames=C29F3.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8689684; DOI=10.1016/s0092-8674(00)80074-4;
RA Porter J.A., Ekker S.C., Park W.-J., von Kessler D.P., Young K.E.,
RA Chen C.-H., Ma Y., Woods A.S., Cotter R.J., Koonin E.V., Beachy P.A.;
RT "Hedgehog patterning activity: role of a lipophilic modification mediated
RT by the carboxy-terminal autoprocessing domain.";
RL Cell 86:21-34(1996).
RN [2]
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).
CC -!- FUNCTION: Intercellular signal essential for a variety of patterning
CC events during development. {ECO:0000250|UniProtKB:Q02936}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 8]: 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 8 N-product]: Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular
CC side {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 8 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 -!- PTM: The C-terminal domain displays an autoproteolysis activity.
CC {ECO:0000269|PubMed:8689684}.
CC -!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
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DR EMBL; U61237; AAB17542.1; -; mRNA.
DR EMBL; Z81043; CAB02804.2; -; Genomic_DNA.
DR EMBL; AL023813; CAB02804.2; JOINED; Genomic_DNA.
DR PIR; T19563; T19563.
DR RefSeq; NP_506805.1; NM_074404.5.
DR AlphaFoldDB; Q94130; -.
DR SMR; Q94130; -.
DR BioGRID; 45030; 1.
DR STRING; 6239.C29F3.2; -.
DR MEROPS; C46.008; -.
DR EPD; Q94130; -.
DR PaxDb; Q94130; -.
DR EnsemblMetazoa; C29F3.2.1; C29F3.2.1; WBGene00006954.
DR GeneID; 180035; -.
DR KEGG; cel:CELE_C29F3.2; -.
DR UCSC; C29F3.2; c. elegans.
DR CTD; 180035; -.
DR WormBase; C29F3.2; CE29200; WBGene00006954; wrt-8.
DR eggNOG; KOG3638; Eukaryota.
DR GeneTree; ENSGT00970000196193; -.
DR HOGENOM; CLU_034413_0_0_1; -.
DR InParanoid; Q94130; -.
DR OMA; INIGECF; -.
DR OrthoDB; 1169356at2759; -.
DR PhylomeDB; Q94130; -.
DR PRO; PR:Q94130; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006954; Expressed in embryo and 2 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0016540; P:protein autoprocessing; NAS:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; NAS:UniProtKB.
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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Cell membrane; Developmental protein; Hydrolase;
KW Membrane; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..550
FT /note="Warthog protein 8"
FT /id="PRO_0000013265"
FT CHAIN 20..342
FT /note="Warthog protein 8 N-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013266"
FT CHAIN 343..548
FT /note="Warthog protein 8 C-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013267"
FT SITE 342..343
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT SITE 409
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000250"
FT SITE 412
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000250"
FT CONFLICT 433
FT /note="S -> T (in Ref. 1; AAB17542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 62087 MW; 2CD8B1A7178C0E0B CRC64;
MNYLLLVSGL LSVWQPVFGS RCGESTIPFS LEILPSGHPV LGCARPTCFG WHPKGYQLPT
TAKFSRLNRK LDGFLRDDSL FTYPFETDSS KIYKVQNSTC EPGFQSSKCD SKDQWVGGIE
PETDAFQDVA YQCCTYAPLR ESTDRNIATV SAGEIVIGGE VYQNESQYAF DYISNIEKSM
DENGEVYYEV NIRRFACLDP HNADRRIDEV WSSENTIRKV NGQKPIAQQA PNVAVNAPIE
AGTFDGEVVD GQTVVIEEII AQQGFIVENE TTVAPFAGPF QAQGFQPRFG APQGFQPAFQ
QPPPQQFFPQ NFQPVVQQPV QFPAQPVGYA PYAPAGWQLH YCFPADAEVN VYEKGVKRMD
ELEVGDWVQA LHGKETTYSP VKYWLHRDPE QEAEFVEFLL ENGESFTLTE KHLVFATDCQ
QNVKNLDDLN PTSTGKINIG ECFFMAQPEN ASKFQKVQIL DIQRVRKTGI YAPMTSLGHL
LVNQIHTSCH SEIDHHLLQN SFFKHVLKLK NRISKYFWNE ESNTEGNIGT SLNFLIEIFE
LIVPSKMISY
