ID F6R6E1_MOUSE Unreviewed; 335 AA.
AC F6R6E1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Anoctamin {ECO:0000256|RuleBase:RU280814};
DE Flags: Fragment;
GN Name=Ano1 {ECO:0000313|Ensembl:ENSMUSP00000119653.2,
GN ECO:0000313|MGI:MGI:2142149};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000119653.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000119653.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119653.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000119653.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119653.2};
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR MaxQB; F6R6E1; -.
DR PeptideAtlas; F6R6E1; -.
DR ProteomicsDB; 373319; -.
DR Antibodypedia; 30667; 1525 antibodies from 39 providers.
DR Ensembl; ENSMUST00000152531.8; ENSMUSP00000119653.2; ENSMUSG00000031075.20.
DR AGR; MGI:2142149; -.
DR MGI; MGI:2142149; Ano1.
DR VEuPathDB; HostDB:ENSMUSG00000031075; -.
DR GeneTree; ENSGT00940000157182; -.
DR HOGENOM; CLU_832967_0_0_1; -.
DR ChiTaRS; Ano1; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000031075; Expressed in parotid gland and 286 other cell types or tissues.
DR ExpressionAtlas; F6R6E1; baseline and differential.
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:SF13; ANOCTAMIN-1; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280814};
KW Proteomics identification {ECO:0007829|MaxQB:F6R6E1,
KW ECO:0007829|PeptideAtlas:F6R6E1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 219..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280814"
FT DOMAIN 3..205
FT /note="Anoctamin dimerisation"
FT /evidence="ECO:0000259|Pfam:PF16178"
FT DOMAIN 208..335
FT /note="Anoctamin transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04547"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000119653.2"
FT NON_TER 335
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000119653.2"
SQ SEQUENCE 335 AA; 38815 MW; D0E2996A7231B400 CRC64;
XLEAGLELEN DEDTKIHGVG FVKIHAPWHV LCREAEFLKL KMPTKKVYHI SETRGLLKTI
NSVLQKITDP IQPKVAEHRP QTTKRLSYPF SREKQHLFDL TDRDSFFDSK TRSTIVYEIL
KRTTCTKAKY SMGQGEGRRK DSALLSKRRK CGKYGITSLL ANGVYSAAYP LHDGDYEGDN
VEFNDRKLLY EEWASYGVFY KYQPIDLVRK YFGEKVGLYF AWLGAYTQML IPASIVGVIV
FLYGCATVDE NIPSMEMCDQ RYNITMCPLC DKTCSYWKMS SACATARASH LFDNPATVFF
SVFMALWAAT FMEHWKRKQM RLNYRWDLTG FEEEE
//
