ID   A0A1A9Z2X2_GLOPL        Unreviewed;      1252 AA.
AC   A0A1A9Z2X2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
OS   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI002136-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI002136-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI002136-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; A0A1A9Z2X2; -.
DR   EnsemblMetazoa; GPAI002136-RA; GPAI002136-PA; GPAI002136.
DR   VEuPathDB; VectorBase:GPAI002136; -.
DR   Proteomes; UP000092445; 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:SF84; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU280814};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU280814}.
FT   TRANSMEM        609..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        763..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        816..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        859..880
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        986..1008
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   TRANSMEM        1131..1152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280814"
FT   DOMAIN          353..597
FT                   /note="Anoctamin dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16178"
FT   DOMAIN          600..1166
FT                   /note="Anoctamin transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF04547"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1252 AA;  144767 MW;  63B59EC45430AE20 CRC64;
     MNSNTQHKQL KTRISSEDET STAPITEASS HEDLISKDIN ESEAKAKERL SHADGLPFSR
     FLSVPSLRNV RTKHLRRPIA SSPAKSEYLK EHSCPSDELP IRRLSQDSGI VAGRLFGGGP
     PFVESAPTQR LTSKTYSENT FSFVINEQPP PRNKNFLETF SMTSMGKEMT RLPSLNYYTS
     AENNSIISQK LGNYNENSRS AYQKLNADND RHGTPLTTNF ESCTKRQTSI QPFGPKVENN
     EVIPGTAMHH SLGLQISTPP TPDPNNEMDG QSDENITIDN NLNSPSSDTS NMAPNQFAYK
     QLVPYEGNHT QPSMENSLDG SYHSNYKANV NQHNGVTRKL KQDNEGLDDE SLMFRDGRRK
     IDMVVAWEEE NLGVMTETES RKRDCRRTFM ENLIKEGLEV ELEDKMQSFN EKTFFMKIHL
     PWRLETRLGE VMNIKLPTKR FITISVKPSW ITARLTILFL KDEDNIVTRN VQHWKDIWQK
     ITERIQLDHQ VVEGEISFKS ATRNGNPEEQ FIVKDRATAY TSAQRSLMVM QVLVRTPFDD
     SDRCGIRRLL NDNTYLACFP LHEGRYDRPH SSGITLDRRI LYLTWAHPSQ WYKKQPLCLV
     RKYFGDKIAL YFCWLGFYTQ MLVYPAVVGT LCFIYGLATL DSEDNTPSKE ICNESGTGNV
     TLCPLCDKAC SYQHLYESCL FSRITYLFDN PSTVFFAIFM SFWATTFLEL WKRKQSVIVW
     EWDLRNVESD EENRPEFETN ATNFRINPVT REREPYMSTW NRWIRFAITG SAVLFMSITI
     TIVLSAVLGT IIYRISVVTV IYGGGGFFVK EHAKLFTTIT AALINLVVIM ILTKIYHRLA
     IRLTNLENPR TQTEYEDSYT FKIFFFEFMN FYSSLIYIAF FKGRFFDYPG DDQARRSEFF
     RLKNDICDPA GCLSELCIQL AIIMVGKQCW NNFMEYLFPK FYNWWRQRKH KKDTKDESHL
     HMAWEQDYHM QDPGRLALFD EYLEMILQYG FVTLFVAAFP LAPLFALLNN VAEIRLDAYK
     MVTQARRPLA ERVEDIGAWY AVVSNAFVIA YTSDFIPRMV YKFVYSETYT LVGYIEHSLS
     LFNTSDYKEE WGAKTEKDPD TCAYRGYRNG PQDYEPYGLS PHYWHVFAAR LAFVVVFEHV
     VFVLTGVMQF VIPDIPAEVQ TQMQREQLLA KEAKYQHGIK RAQGDKQDLM SLFREASNRN
     NPNTPIPELG SVMPRRSWAR RFSRLSDTLD AHVEVAGRPK RSTETSTVWE VS
//