ID A0A182W3X2_9DIPT Unreviewed; 1325 AA.
AC A0A182W3X2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN005033-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN005033-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN005033-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 EnsemblMetazoa; AMIN005033-RA; AMIN005033-PA; AMIN005033.
DR VEuPathDB; VectorBase:AMIN005033; -.
DR OrthoDB; 534027at2759; -.
DR Proteomes; UP000075920; 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 741..770
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 825..843
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 895..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 933..954
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 1060..1082
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 1112..1135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 1214..1235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 496..729
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 906..1249
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 152011 MW; 11CEF5E052DAC92B CRC64;
MNEQRSYSSR DSRTLFYPAR KPAHMRPHSS SSSNSVAVVS DSAKTRVSDC IETQKHCETR
NDASSNDGHA PISSSTRSQS LHSVSSRMAT NDSAEGAAHF KHFPEAIDVG GHFDVLLPNC
IVQQEQSHNQ NTKTEKQTIC SRTIHSSPVG KPRRRRYSQD SCAPVYERLS VAGFARNGTL
NGSCENDKMT QQHQVLMRHS TDNLRSINNH QCSGTGGLHH KREIAEKAAD SVGTGMGTEV
TNHVKTKYFM HRMTAQDLGS GNEPSSSQDS TASPSSTILP KSVEIVVDTD QTPTNGYAAM
VNGTVTAVSP KDTSFIDKLP PLEDIMESPL LKAPVEKWLQ TEDRLSREEM VPSYDTEEPS
RSPDLYSNLF GPKISASENI PGTPMDTPDI VSEFNKSFNS STTSIINERR RSSSKLLATD
HDPVSIGGVA TGTLNSLTDH QTGGTVLGGA SVDKNNSFGK GSLRNLLKLR KASDQSQDTR
RSSQQDKEGL DPESLMFRDG RRKIDMVLCY EEDDQGVMTE LDALKRHQRK LFHENLIREG
LEFEVEDKAQ AFDGKTYFVK IHIPWRTESR YAEVMNLKLP VKRFITISVK EEETALRRQQ
NKILSYWNRV MSMTEYNHGR IEKEPSFYSA TANGNPEEQF IVKDRCTSYT SAQRSLIVMQ
ILMRTRFDET EKVNNVGIRR LLNDGTYLAC FPLHEGRYDK DHSSGSLFDR RLLYLEWARP
IKWYKKQPLC LVRKYFGDKI ALYFCWLGFY TKMLYAPAIV GLFCFLYGLA SMDSSDNIPT
KEICDENGPG KTILCPLCDR ACSYQQLHES CFFAQLTYLF DNPSTVFFAI FMSFWATTFL
ELWKRKQSVL VWEWDLQNIE NEEDMRPEFE TTVKTFRINP VTREKEPYMP TWTRAVRFIA
TSSAVLFMIY HKLALYLTNM ENPRTQTEYE DSYTVKIFVF EFMNFYSSLI YIAFFKGRFY
DYPGDDVARK SEFLRLKGDI CDPAGCLSEL CIQLAIIMVG KQCWNNFMEY FFPAFYNWWR
QRKHKQLTKD ETHLHMAWEQ DYHLQDPGRL ALFDEYLEMI VQYGFVTLFV AAFPLAPLFA
LLNNIAEIRL DAYKMVTQSR RPLAERVEDI GAWYGILKII TYTAVVSNAF VIAYTSDFIP
RMVYKYVYSP QFSLHGYIEH SLSTFNTSDY KEEWGTKTES DPDTCQYRGY RNGPEADEQY
GLSPHYWHVF AARLAFVVIF EHIVFVLTGI MQFIIPDIPI EVKTQMQREQ LLAKEAKYQH
GLKKSRETDY EEILHTLREQ SNNSRQGVRG SWARRLSRLS DGLDAHVEVP NRPRHSLEST
VWEVT
//