ID A0A158PH81_ANGCS Unreviewed; 720 AA.
AC A0A158PH81;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN ORFNames=ACOC_LOCUS6113 {ECO:0000313|EMBL:VDM57698.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000611201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000611201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM57698.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM57698.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU280814}.
CC -!- SIMILARITY: Belongs to the anoctamin family.
CC {ECO:0000256|ARBA:ARBA00009671, ECO:0000256|RuleBase:RU280814}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU280814}.
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DR EMBL; UYYA01003921; VDM57698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PH81; -.
DR STRING; 334426.A0A158PH81; -.
DR WBParaSite; ACOC_0000611201-mRNA-1; ACOC_0000611201-mRNA-1; ACOC_0000611201.
DR OMA; RLIWFNR; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF76; ANOCTAMIN; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU280814};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU280814}.
FT TRANSMEM 243..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 394..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 533..559
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 579..607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 628..645
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 25..191
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
SQ SEQUENCE 720 AA; 83404 MW; D8372BBD08AC76A3 CRC64;
MLRASTNIDY PYFPFRIPVD YAAQREGLIV NHEFAGPICF TLISTPFHRL CREAEKMQMS
FPLKDCPVNP SSPPCCPTLF NAFVTDDTVN YISAPFSRRN CQLFLNYENE KLFFTSAQRD
MLTHEILTQL DIRRELKEQN HNVSVVGDES QQSVIADEPL RRKGLQYLRM KNSYEDSFIL
HEPSQEEPYF KKMKDNSSIT YMELITEIET DPRKKLSNLW SRFFRFQPLG LVREYFGEQI
AFYFAWQGTF LTMLWPATVL GLAVFVFGFV KSVRLNPATF GNCTVVNYAG ESFIVSCTFR
NKLAQFFTTV SSWFTNSFDN ELNAFFAAFM SIWGTFFCQI WRRNNTVLAY EWDCEDFNEV
EPDRPEYRGS ATRIDPTRTE PECFSPDFLR FLKLAVSCIV VILSMCLVII SVLLVTLYKL
WAVSSQACNK EGFQTKGLFG LGENYKDACL PGTCGSLLAI QLISHMIIKP LPKFTKDIVI
PFFVRICRLR KWYKRQRNIS HETLNENEMN VLLREWMKPN AGDFTLSEFN EKIILFGTTM
MFAALFPLAP LIALVIGFID LRVDAFRLLW INRRPVPVMA NGIGIWLSIL YFLQYAAVMT
NAFIIAFTSD FCSNFFSDVM YCDVKNRFLI VIVFQNMVFI LKYVLQSIIP TVPSSIRVAQ
RRKRYVVNYV IEKGDVPYKI RNRRRARNAK LAWIMSHKKG SKSPKLISRV DVETANISSS
//