PTR18_CAEEL
ID PTR18_CAEEL Reviewed; 895 AA.
AC Q9XWL9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Patched-related protein 18 {ECO:0000312|WormBase:Y38F1A.3};
DE AltName: Full=Patched domain-containing protein 18 {ECO:0000305};
GN Name=ptr-18 {ECO:0000312|WormBase:Y38F1A.3};
GN ORFNames=Y38F1A.3 {ECO:0000312|WormBase:Y38F1A.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DEGRADATION.
RX PubMed=33872306; DOI=10.1371/journal.pgen.1009457;
RA Chiyoda H., Kume M., Del Castillo C.C., Kontani K., Spang A., Katada T.,
RA Fukuyama M.;
RT "Caenorhabditis elegans PTR/PTCHD PTR-18 promotes the clearance of
RT extracellular hedgehog-related protein via endocytosis.";
RL PLoS Genet. 17:e1009457-e1009457(2021).
CC -!- FUNCTION: Transporter, which promotes the endocytosis-mediated
CC degradation of hedgehog-related proteins such as grl-7 in order to
CC establish the capacity of progenitor cells to maintain quiescence in
CC arrested L1 stage larvae. {ECO:0000269|PubMed:33872306}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:33872306}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the apical cell membrane during the 3-
CC fold stage during embryogenesis. {ECO:0000269|PubMed:33872306}.
CC -!- DEVELOPMENTAL STAGE: First expressed in hypodermal, seam, and P cells
CC at the 3-fold stage during embryogenesis (at protein level)
CC (PubMed:33872306). During late embryogenesis, expressed in hypodermal
CC and P neural progenitor cells (at protein level) (PubMed:33872306). At
CC the late L1 larval stage, expressed in the descendants of P cells,
CC rectal epithelial F, K, and U cells and seam cells (at protein level)
CC (PubMed:33872306). {ECO:0000269|PubMed:33872306}.
CC -!- PTM: Degraded in a lysosome-dependent manner before hatching.
CC {ECO:0000269|PubMed:33872306}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; BX284602; CAA21636.3; -; Genomic_DNA.
DR RefSeq; NP_496761.3; NM_064360.3.
DR SMR; Q9XWL9; -.
DR STRING; 6239.Y38F1A.3; -.
DR EPD; Q9XWL9; -.
DR PaxDb; Q9XWL9; -.
DR PeptideAtlas; Q9XWL9; -.
DR EnsemblMetazoa; Y38F1A.3.1; Y38F1A.3.1; WBGene00004232.
DR GeneID; 174940; -.
DR KEGG; cel:CELE_Y38F1A.3; -.
DR UCSC; Y38F1A.3; c. elegans.
DR CTD; 174940; -.
DR WormBase; Y38F1A.3; CE43376; WBGene00004232; ptr-18.
DR eggNOG; KOG1934; Eukaryota.
DR HOGENOM; CLU_002359_2_1_1; -.
DR InParanoid; Q9XWL9; -.
DR OMA; TYPSMDV; -.
DR OrthoDB; 210960at2759; -.
DR PhylomeDB; Q9XWL9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004232; Expressed in embryo and 3 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF02460; Patched; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..895
FT /note="Patched-related protein 18"
FT /id="PRO_0000455717"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 263..420
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 895 AA; 101874 MW; AE0DD0C0C196DA5E CRC64;
MKSISQCLGN VSLWIEQQTH DMFYWVGLKI ADYPKWTLFI TTIWALLMAG GVVRFKEVNN
VRDHFSATNS PSRYEYRVAR EFFQELGSPF HVVVAMQAAD GGSLLRPKYI DKALEIEDFL
QYKLKGSFGN QSYSYSDFCG TQCETSDAVS IFLSMFRDQQ IKKTAHVKLT YPSMDVFGHR
VYLANNIFQV KINNRSSIIE ESKLVAINFH AIYNNETMYE IMKEWEQKLF AYTLSTENDP
LIRVYVTSEG LVSEEVRRTG ILAMPLMGVT FLIILAFTIL TTLKRDPVKS KPFEAFLGVI
CPILSLCASF GHLFWMGFEY LPIVTVVPFL ILSIGVDDVF IFIHAWHRTP YKHSVRDRMA
ETLADAGPSI SITSLTNLLS FAIGIFTPTP AIYTFCVFIS TAVIYDYIYQ IFFFSAVLVL
SGEREEQRKN AYLWWKDVPL PEEPTGKQKK ETIVSRVLGK VLDFWVDFIM AKWSKFLIGA
IMITYWIFMA RGVMEIAVGL SSEKLFLDDS PLLPLVRLQT NVIFKEGGQV AVFVNNPGNM
SEPDAVPEIM RILRRFEVAN NSVGAASTHM WLLPYLPYVG EQEHGSIEFK YRYLPEFFKL
TEFRRWSHFV NLGNHQDCLS EKPSCLQKFV FSTGFHDAVS WSDRLALLEN WREMASEYQH
LNLTIYEDFS MYSDQLLTIV PVTQSTVFCA LICMIMILTL FTPSPVTIVT STAAVLSINL
GVFGCLVYMN IDLDPISMTT LLMAIGFSVD FVAHITWHYY KGDFHSKRAR IRHALAGIAW
PMFQAGTSTM LAITVLALVH AYMVQVFVKV VVLVIFLGMF HGLVVLPIVF SALPFTKTSG
PQKKKVAPLQ MHEAGPIPKK EEPKVIKVNG EEDEEDEKTT KEEPVEKSVR SAERA
