WRT1_CAEEL
ID WRT1_CAEEL Reviewed; 485 AA.
AC Q94128;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Warthog protein 1;
DE Contains:
DE RecName: Full=Warthog protein 1 N-product;
DE Contains:
DE RecName: Full=Warthog protein 1 C-product;
DE Flags: Precursor;
GN Name=wrt-1; ORFNames=ZK1290.12;
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 1]: 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 1 N-product]: Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular
CC side {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 1 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCD65942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U61235; AAB17540.1; -; mRNA.
DR EMBL; FO080700; CCD65942.1; ALT_INIT; Genomic_DNA.
DR PIR; T34504; T34504.
DR RefSeq; NP_495579.3; NM_063178.6.
DR AlphaFoldDB; Q94128; -.
DR SMR; Q94128; -.
DR STRING; 6239.ZK1290.12; -.
DR MEROPS; C46.006; -.
DR EPD; Q94128; -.
DR PaxDb; Q94128; -.
DR PeptideAtlas; Q94128; -.
DR EnsemblMetazoa; ZK1290.12.1; ZK1290.12.1; WBGene00006947.
DR GeneID; 174223; -.
DR KEGG; cel:CELE_ZK1290.12; -.
DR UCSC; ZK1290.12; c. elegans.
DR CTD; 174223; -.
DR WormBase; ZK1290.12; CE15545; WBGene00006947; wrt-1.
DR eggNOG; KOG3638; Eukaryota.
DR HOGENOM; CLU_034413_0_0_1; -.
DR InParanoid; Q94128; -.
DR OrthoDB; 1169356at2759; -.
DR PhylomeDB; Q94128; -.
DR PRO; PR:Q94128; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006947; Expressed in pharyngeal muscle cell (C elegans) and 3 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:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR GO; GO:0016540; P:protein autoprocessing; NAS:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; NAS:UniProtKB.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..485
FT /note="Warthog protein 1"
FT /id="PRO_0000013259"
FT CHAIN 22..290
FT /note="Warthog protein 1 N-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013260"
FT CHAIN 291..485
FT /note="Warthog protein 1 C-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013261"
FT REGION 236..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 290..291
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT SITE 357
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000250"
FT SITE 360
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 52513 MW; 76E65E3A9DAE6B70 CRC64;
MMVMNPLTAT FLAALIGTAA SASCGSSGIP FRFEVLPSGQ PVLGCGSPTC FGAENGGRDL
RHDSSFMAGA DGDDGFFRDG DLARVRVRDP DAPAQMANCP REFSSSSCSN PMTWVGGFKA
SDNGDLSLQC CHYEGLRFAQ EVGRPVVHPG EVYSGGEVLR DGRQTGFDAI SNVRKITSGD
GTVAYEVTVT RMNCLPNPGE ESNEVSFDIQ RDIGRILDKV GETAASGVQT NHIEADQRLS
PSTDVQSDSY VSPTEADPQE PVEQFVQVGE QVVPVTSAGY YYPVASGVPA CFTGNSKVMT
PAGEKSMADL SVGDMVMTYE YGKMTYTRVA SWLHRLPDTK AAFIKLTTEQ GAIIDMTPQH
FIYKANCVTE EMELVYAEDM TIGDCLMVKE NEKLVMTTIS EKSTFYETGV YAPMTETGDL
IVDDVYASCH NVVKANTLSH TFLNFATSVQ QKMRSVLGSL EETGHLPATS EFFLNIIDVL
LPHKY
