ID A0A0B2VVS7_TOXCA Unreviewed; 792 AA.
AC A0A0B2VVS7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cathepsin D {ECO:0000313|EMBL:KHN85065.1};
GN Name=ctsd {ECO:0000313|EMBL:KHN85065.1};
GN ORFNames=Tcan_02977 {ECO:0000313|EMBL:KHN85065.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN85065.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN85065.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN85065.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN85065.1}.
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; JPKZ01000872; KHN85065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2VVS7; -.
DR STRING; 6265.A0A0B2VVS7; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd15096; 7tmA_AstA_R_insect; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..321
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT DOMAIN 443..760
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 461
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 648
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 474..481
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 639..643
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 682..719
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 792 AA; 89221 MW; B86B34168A218A18 CRC64;
MGLLDNISDE YRQRVMQFYN ETKRFEAHIG IVIPAIFAGV IAIGLVGNLL VVVVALHRQM
RNSTNTLIIG LACSDLMFLT LCVPFTAIDY ALPVWIFPRW MCSMINYLQH SAAYFSVWTL
TLMAADRFLA VCYPVESMTL RNTSNTAVAL AVIYTAIIIS QIPVANIHDI YEYDFIIETR
STCAIVRIAT GEASITEARL YFFSFNVFGY LLPLGITCVF YYFMLRRLWY TPRPGIEAEG
IRVSIKSRPE TVKAKKKVTR LVFCVVVIWA FCWLPLNVCF MFSGVVYPET LVMKGGKLMV
IIQILSQVLA YTNSCLNPIL YAFLSDNFRK GFMRIFTVAI NICTMGRCCE ENRETAHIDL
THCNNGMTTN SGRQSLTRIP IRKQNTVKEQ LVESGSWSTY LHQRHHILKK HFYSIANHRI
HFLRGQSGNE IDELLKNYMD AQYYGEISIG TPAQNFTVIF DTGSANLWVP SRKCPFTDIA
CLLHHKYDAA KSSTYEEDGR KIQIQYGTGS MKGFISLDNV CVAEVCAREQ PFAEATSEPG
LTFIAAKFDG ILGMGFPEIA VLGVKPVFNT MVDQQLLAEP VFAFWLDRNP NDEIGGEITF
GGTDSKRYVE PITYSPVTHR GYWQFKMDKV IGQESTLACP NGCQAIADTG TSLIAGPKEQ
IEAIQKFIGA EPLFRGEYMV PCDKLPTMPD VSFVIAGKTY TLTPTDYVLN MTAMGKSVCL
SGFMGIDLPE RLGELWILGD VFIGRFYTVF DMGQERVGFA QAKDSNGHRI GRPVKHLVQF
DFDEVKSDEY FL
//
