ID A0A2A2K345_9BILA Unreviewed; 488 AA.
AC A0A2A2K345;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN ORFNames=WR25_09744 {ECO:0000313|EMBL:PAV68387.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV68387.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV68387.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV68387.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU280814}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC 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}.
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:PAV68387.1}.
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DR EMBL; LIAE01009762; PAV68387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2K345; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF76; ANOCTAMIN; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
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 217..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 251..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 299..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 18..88
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 194..437
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
SQ SEQUENCE 488 AA; 57227 MW; 96A0B8D38535CAD7 CRC64;
MLQASTEVDY PYFPFRISVD FVLVNRLDDL ANQVQRQLFE KAIRREGLIV HKEQAGGQLF
TLLSTPFHRL CREAERRQMS FPLKDEHACS INNSKDTVTL INEEPLQRKG LQYLLMEGAY
SDAFILHEPS EEEPYFKKMK GQSVVTYTEL IKEIEDDPRK KLQETWCRYF KFQPLNSIRN
YFGEQIAFYF AWQDPITGES VMFSPNIIRY LKMMCSFLVV ILCMSISVIS VIAVIMYKMY
IVDKYECDKE YTFVCMLLAA FIPSVLNTSS TMLLGFLYNK LIERLNYWEN HRTMTEHTNA
LIIKVFAFSF VNNYVSLFYI AFVRPENHGF QTNGLFGLGK AFKDTCKENT CGSLLALQLM
THMLLKPFPK FSKDVIFPYF IKLFRHKLWF HRRKETLESI LKESNETSVL IREWIKPNAG
EFALWEFNEK VILFGTTMNM VFALKYVLQS IIPTIPTGIQ MALRRKRFVI GHVLEKGDVP
TRIKHKSE
//
