WRT4_CAEEL
ID WRT4_CAEEL Reviewed; 557 AA.
AC Q94129; Q94410;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Warthog protein 4;
DE AltName: Full=Protein M75;
DE Contains:
DE RecName: Full=Warthog protein 4 N-product;
DE Contains:
DE RecName: Full=Warthog protein 4 C-product;
DE Flags: Precursor;
GN Name=wrt-4; ORFNames=ZK678.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAB01902.2};
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 4]: 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 4 N-product]: Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Extracellular
CC side {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Warthog protein 4 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; U61236; AAB17541.1; -; mRNA.
DR EMBL; Z79605; CAB01902.2; -; Genomic_DNA.
DR PIR; T27975; T27975.
DR RefSeq; NP_510593.1; NM_078192.5.
DR AlphaFoldDB; Q94129; -.
DR SMR; Q94129; -.
DR BioGRID; 46556; 3.
DR IntAct; Q94129; 1.
DR STRING; 6239.ZK678.5; -.
DR MEROPS; C46.007; -.
DR EPD; Q94129; -.
DR PaxDb; Q94129; -.
DR PeptideAtlas; Q94129; -.
DR EnsemblMetazoa; ZK678.5.1; ZK678.5.1; WBGene00006950.
DR GeneID; 181664; -.
DR KEGG; cel:CELE_ZK678.5; -.
DR UCSC; ZK678.5.1; c. elegans.
DR CTD; 181664; -.
DR WormBase; ZK678.5; CE24735; WBGene00006950; wrt-4.
DR eggNOG; KOG3638; Eukaryota.
DR GeneTree; ENSGT00970000196193; -.
DR HOGENOM; CLU_034413_0_0_1; -.
DR InParanoid; Q94129; -.
DR OMA; TAKFFRI; -.
DR OrthoDB; 1169356at2759; -.
DR PhylomeDB; Q94129; -.
DR PRO; PR:Q94129; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006950; Expressed in larva and 4 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..557
FT /note="Warthog protein 4"
FT /id="PRO_0000013262"
FT CHAIN 21..346
FT /note="Warthog protein 4 N-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013263"
FT CHAIN 347..557
FT /note="Warthog protein 4 C-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000013264"
FT REGION 272..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 345..346
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:Q02936"
FT SITE 415
FT /note="Involved in auto-cleavage"
FT /evidence="ECO:0000250"
FT SITE 418
FT /note="Essential for auto-cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q02936"
FT CONFLICT 53
FT /note="H -> N (in Ref. 1; AAB17541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61929 MW; F9B785A3E3AD73A2 CRC64;
MRFSLLALVL LSSSYKFTYG SECGDSTIPY SLEVLSSGQP ILGCARPTCF GWHSNGHQLP
TNAKFFRIDQ QSDGFLRDDP LAIHTFDAAD PRVYAQQQAS CEQEFQSLSC NPEDQWVGGI
APVMNASTTK IVAYKCCTYA PLRASIDRGV ATVSGGQIVV GGEIFADNKP YAFDYISNVE
KKIDSEGEIF YEVNIKRFSC LDLQKVDRSV PEILNSENTI RHVNGHRFVV HQAPTVDVET
PVETGQLVVP QGVQNGQEVI IEEIVAQEGF VQETNPQPPP PPGQQGGFVQ PQGFQPQGGF
QPQGFQPQGF QPQAFQPQVV QNPVPAAPAG YAPMGFAPSG LQLYYCFPGD AMVNVYNGGF
KRMDELAVGD WVQALDKNGS QVTFIPVQYW LHRDPKQVAD FVEFTLDNGE TFSLTEKHLV
FVTQCSVPYS EDENINANPV PAERVNIGDC FYIAHRKKSQ MYQRVKVLDI NIVQKTGIYS
PMTSRGHLLV DRIHASCHSE TDNYSLQNTF FTNVLRWKSQ IRNYFWTVED STNEDNIGYG
LNGVMAVLDI VIPSKLM
