ID A0A2K6ESW5_PROCO Unreviewed; 608 AA.
AC A0A2K6ESW5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
GN Name=ANO3 {ECO:0000313|Ensembl:ENSPCOP00000004811.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000004811.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000004811.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A2K6ESW5; -.
DR STRING; 379532.ENSPCOP00000004811; -.
DR Ensembl; ENSPCOT00000015125.1; ENSPCOP00000004811.1; ENSPCOG00000013172.1.
DR GeneTree; ENSGT00940000156257; -.
DR OMA; DWENSEI; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IEA:UniProt.
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:SF16; ANOCTAMIN-3; 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:UP000233160};
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 367..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 411..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 485..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 529..548
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 569..591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 148..353
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 356..608
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
SQ SEQUENCE 608 AA; 71224 MW; 881B01940306541A CRC64;
SRDHNGSIAM DLNKKETVDI KSEITKETSL KPSRRSLPCL AQSYAYSKSL SQSTSLFQSI
ESDSQAPTSI TLISADKAEQ GKQQLLFSSL GKDKDYTDES EHATYDRSRL INDFVIKDKS
EFKTKLSKVM QIQSHKFIDW STWPYCKQSS RADERDYFSD NLGKYCLLLS PIASPDIMFI
KIHIPWDTLC KYAERLNIRM PFRKKCYYTD RRSKSMGRVQ SYFRRIKNWM AQNPMVLDKS
AFPNLGESDC YTGPFSRARI HHFIINNKDT FFSNATRSRI VYHVLERTKY ENGISKVGIR
KLINNGSYIA AFPPHEGAYK SSQPIKTHGP QNNRHLLYER WARWGMWYKH QPLDLIRLYF
GEKIGLYFAW LGWYTGMLIP AAAVGLCVFF YGLLTMNKSQ VTYLFDNGGT VFFAIFMAIW
ATVFLEFWKR RRSILTYTWD LTEWEEEEET LRPQFETKYY KMEVINPITG KPEPHQPSSD
KITRLLVSVS GIFFMISLVI TAVFGVVVYR LVVMERFASF KWNFIKQHWQ FATSAAAVCI
NFIIIMLLNL VKYPRTESEW ENSFALKMFL FQFVNLNSSI FYIAFFLGRF VGRPGKYNKL
FDRWRLEE
//
