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ANO7_MOUSE
ID   ANO7_MOUSE              Reviewed;         859 AA.
AC   Q14AT5; Q6IFT5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Anoctamin-7;
DE   AltName: Full=New gene expressed in prostate homolog;
DE   AltName: Full=Transmembrane protein 16G;
GN   Name=Ano7; Synonyms=Ngep, Tmem16g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=14981236; DOI=10.1073/pnas.0308746101;
RA   Bera T.K., Das S., Maeda H., Beers R., Wolfgang C.D., Kumar V., Hahn Y.,
RA   Lee B., Pastan I.;
RT   "NGEP, a gene encoding a membrane protein detected only in prostate cancer
RT   and normal prostate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:3059-3064(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA   Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA   Martins J.R., Kunzelmann K.;
RT   "Expression and function of epithelial anoctamins.";
RL   J. Biol. Chem. 285:7838-7845(2010).
RN   [5]
RP   REVIEW.
RX   PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA   Winpenny J.P., Gray M.A.;
RT   "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT   come of age.";
RL   Exp. Physiol. 97:175-176(2012).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=23532839; DOI=10.1074/jbc.m113.457937;
RA   Suzuki J., Fujii T., Imao T., Ishihara K., Kuba H., Nagata S.;
RT   "Calcium-dependent phospholipid scramblase activity of TMEM16 protein
RT   family members.";
RL   J. Biol. Chem. 288:13305-13316(2013).
CC   -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
CC       scrambles phosphatidylserine, phosphatidylcholine and
CC       galactosylceramide (PubMed:23532839). Does not exhibit calcium-
CC       activated chloride channel (CaCC) activity (PubMed:23532839). May play
CC       a role in cell-cell interactions (By similarity).
CC       {ECO:0000250|UniProtKB:Q6IWH7, ECO:0000269|PubMed:23532839}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC         sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC         ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:23532839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC         Evidence={ECO:0000305|PubMed:23532839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a
CC         beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in);
CC         Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390;
CC         Evidence={ECO:0000269|PubMed:23532839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC         Evidence={ECO:0000305|PubMed:23532839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC         sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC         ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:23532839};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC         Evidence={ECO:0000305|PubMed:23532839};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6IWH7};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6IWH7}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q6IWH7}. Note=Concentrates at sites of
CC       cell-cell contact. Shows an intracellular localization.
CC       {ECO:0000250|UniProtKB:Q6IWH7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14AT5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14AT5-2; Sequence=VSP_026009, VSP_026010;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the stomach. Expressed at low
CC       levels in small intestine and large intestine.
CC       {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:23532839}.
CC   -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC       are anion selective and have eight (OCT) transmembrane segments. There
CC       is some dissatisfaction in the field with the Ano nomenclature because
CC       it is not certain that all the members of this family are anion
CC       channels or have the 8-transmembrane topology.
CC   -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
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DR   EMBL; AC108412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC116706; AAI16707.1; -; mRNA.
DR   EMBL; BK004075; DAA04566.1; -; mRNA.
DR   CCDS; CCDS15188.1; -. [Q14AT5-1]
DR   CCDS; CCDS78656.1; -. [Q14AT5-2]
DR   RefSeq; NP_001258813.1; NM_001271884.1. [Q14AT5-2]
DR   RefSeq; NP_996914.1; NM_207031.2. [Q14AT5-1]
DR   RefSeq; XP_006529796.1; XM_006529733.2. [Q14AT5-1]
DR   AlphaFoldDB; Q14AT5; -.
DR   SMR; Q14AT5; -.
DR   BioGRID; 240364; 3.
DR   STRING; 10090.ENSMUSP00000140438; -.
DR   SwissLipids; SLP:000000375; -.
DR   GlyGen; Q14AT5; 2 sites.
DR   iPTMnet; Q14AT5; -.
DR   PhosphoSitePlus; Q14AT5; -.
DR   PaxDb; Q14AT5; -.
DR   PRIDE; Q14AT5; -.
DR   ProteomicsDB; 296311; -. [Q14AT5-1]
DR   ProteomicsDB; 296312; -. [Q14AT5-2]
DR   Antibodypedia; 47723; 121 antibodies from 26 providers.
DR   DNASU; 404545; -.
DR   Ensembl; ENSMUST00000058682; ENSMUSP00000050495; ENSMUSG00000034107. [Q14AT5-2]
DR   Ensembl; ENSMUST00000186641; ENSMUSP00000140438; ENSMUSG00000034107. [Q14AT5-1]
DR   GeneID; 404545; -.
DR   KEGG; mmu:404545; -.
DR   UCSC; uc007cdw.2; mouse. [Q14AT5-1]
DR   UCSC; uc033fku.1; mouse. [Q14AT5-2]
DR   CTD; 50636; -.
DR   MGI; MGI:3052714; Ano7.
DR   VEuPathDB; HostDB:ENSMUSG00000034107; -.
DR   eggNOG; KOG2514; Eukaryota.
DR   GeneTree; ENSGT00940000158551; -.
DR   HOGENOM; CLU_006685_0_1_1; -.
DR   InParanoid; Q14AT5; -.
DR   OMA; RWAMTSE; -.
DR   OrthoDB; 1263362at2759; -.
DR   PhylomeDB; Q14AT5; -.
DR   TreeFam; TF314265; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 404545; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q14AT5; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q14AT5; protein.
DR   Bgee; ENSMUSG00000034107; Expressed in duodenum and 32 other tissues.
DR   ExpressionAtlas; Q14AT5; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR   GO; GO:0017128; F:phospholipid scramblase activity; IDA:MGI.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IDA:MGI.
DR   GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IDA:MGI.
DR   GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IDA:MGI.
DR   GO; GO:0061588; P:calcium activated phospholipid scrambling; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; ISO:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR032394; Anoct_dimer.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR031296; Anoctamin-7.
DR   PANTHER; PTHR12308; PTHR12308; 1.
DR   PANTHER; PTHR12308:SF22; PTHR12308:SF22; 1.
DR   Pfam; PF16178; Anoct_dimer; 1.
DR   Pfam; PF04547; Anoctamin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW   Lipid transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..859
FT                   /note="Anoctamin-7"
FT                   /id="PRO_0000289327"
FT   TOPO_DOM        1..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..492
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..530
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        552..651
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        652..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        673..700
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        722..780
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        781..801
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        802..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        746
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         836..843
FT                   /note="ALLGATGV -> VTVGVTGG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026009"
FT   VAR_SEQ         844..859
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026010"
SQ   SEQUENCE   859 AA;  97128 MW;  82E1A473C59C8DA3 CRC64;
     MLRGQAREED SVVLIDMASP EAGNGCSYGS TAQASEAGKQ QVAPSRVGSS AKPPIDFVLV
     WEEDLRNQEN PTKDKTDTHE VWRETFLENL CLAGLKIDQH DVQDEAAAVH YILLRAPWAV
     LCYYAEDLRL KLPLQELPNQ ASNWSATLLE WLGIPNILLE HVPDTPPEYY SCQFKASKLQ
     WFLGSDNQDT FFTSTKRHQI LFEILAKTPY GHEKKGLFGI DQLLAEGVFS AAFPLHDGPF
     SAVPESSQVL GLIQRQVLFQ HWARWGKWNK YQPLDHVRRY FGEKVALYFA WLGFYTGWLL
     PAAVVGTVVF LVGCFLVFSD IPTQELCHSS DSFDMCPLCS DCSFWLLSSA CTLAQAGRLF
     DHGGTVFFSL FMALWAVLLL EYWKRKNATL AYRWDCSDYE DIEERPRPQF AATAPMTALN
     PITGEDEPYF PEKNRVRRML AGSVVLLMMV AVVIMCLVSV ILYRAVMAII VSRSDNAFLS
     AWASRIASLT GSVVNLVFIL ILSKVYVLLA QVLTRWEMHR TQTEFEDAFT LKVFIFQFVN
     FYASPVYIAF FKGRFVGYPG NYHTLFGIRN EECPAGGCLS ELAQELLVIM VGKQIINNVQ
     EVLVPKLKGC WQKFSRGKKA GTGTHPAPWE ADYELLPCEG LFHEYLEMVL QFGFVTIFVA
     ACPLAPLFAL LNNWVEIRLD ARKFVCEYRR PVAERAQDIG IWFHILTGLT HLAVISNAFL
     LAFSSDFLPR VYYSWTHAPD LHGFLNFTLA RAPPTFTSAH NRTCRYRAFR DDDGHYSPTY
     WTLLAIRLAF VIVFEHVVFS IGRVLDLLVP DIPESVEIKV KREYYLAKQA LAENEALLGA
     TGVKDDQPPS SEPSLGLPA
 
 
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