ANO7_RAT
ID ANO7_RAT Reviewed; 860 AA.
AC Q6IFT6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
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).
CC -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
CC scrambles phosphatidylserine, phosphatidylcholine and
CC galactosylceramide (By similarity). Does not exhibit calcium-activated
CC chloride channel (CaCC) activity (By similarity). May play a role in
CC cell-cell interactions (By similarity). {ECO:0000250|UniProtKB:Q14AT5,
CC ECO:0000250|UniProtKB:Q6IWH7}.
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:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
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:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
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:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
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 -!- 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; AABR03068351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03070767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004074; DAA04565.1; -; mRNA.
DR RefSeq; NP_001004071.1; NM_001004071.1.
DR AlphaFoldDB; Q6IFT6; -.
DR SMR; Q6IFT6; -.
DR STRING; 10116.ENSRNOP00000033330; -.
DR CarbonylDB; Q6IFT6; -.
DR GlyGen; Q6IFT6; 2 sites.
DR PaxDb; Q6IFT6; -.
DR PRIDE; Q6IFT6; -.
DR Ensembl; ENSRNOT00000033233; ENSRNOP00000033330; ENSRNOG00000023427.
DR GeneID; 367318; -.
DR KEGG; rno:367318; -.
DR CTD; 50636; -.
DR RGD; 1302987; Ano7.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000158551; -.
DR HOGENOM; CLU_006685_0_1_1; -.
DR InParanoid; Q6IFT6; -.
DR OMA; RWAMTSE; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q6IFT6; -.
DR TreeFam; TF314265; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:Q6IFT6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000023427; Expressed in jejunum and 5 other tissues.
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:RGD.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; ISO:RGD.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061591; P:calcium activated galactosylceramide scrambling; ISO:RGD.
DR GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; ISO:RGD.
DR GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; ISO:RGD.
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:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..860
FT /note="Anoctamin-7"
FT /id="PRO_0000289328"
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..652
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 860 AA; 97170 MW; 96BE3CBD6DE96101 CRC64;
MLRKQAGEED SVVLIDMTSP EAGNGCSYGS TAQASEAGKQ QVAPSRVGSS ANPPIDFVLV
WEEDLRSREN PTQDKTDTHE IWRETFLENL RVAGLKIDQR DVQDEAAAVH YILLSAPWAV
LCYYAEDLRL KLPLQELPNQ ASNWSATLLE WLGIPNILLE NVPDTPPEYY SCQFKASKLQ
WFLGSDNQDT FFTSTKRHQI LFEILAKTPY GHQKKGLFGI DQLLAEGVFS AAFPLHDGPF
SVVPESSQVL GLTQRQVLFK HWARWGKWRK YQPLDHVRRY FGEKVALYFA WLGFYTGWLL
PAAVVGTVVF LAGCFLVFSD VPTQELCHSS DTFDMCPLCS DCSFWLLSSA CTLAQAGRLF
DHGGTVFFSL FMALWAVLLL EYWKRKNATL AYRWDCSDYE DIEERPRPQF AATAPMTALN
PITGEDEPYF PEKNRVRRML AGSVVLLMMV AVVIMCLVSI ILYRAVMAII VSKSNNAFLS
AWASRIASLT GSVVNLVFIL ILSKVYVILA QVLTRWEMHR TQTAFEDAFT LKVFIFQFVN
FYASPVYIAF FKGRFVGYPG NYHTLFGVRN EECPAGGCLS ELAQELLVIM VGKQIINNVQ
EVLVPKLKGC WQKLCSRRKK AGMGANPAPW EADYELLPCE GLFHEYLEMV LQFGFVTIFV
AACPLAPLFA LLNNWVEIRL DARKFVCEYR RPVAERAQDI GIWFHILAGL THLAVISNAF
LLAFSSDFLP RVYYSWTRAP DLRGFLNFTL ARAPPTFTSA HNRTCRYRAF RDDDGHYSPT
YWTLLAIRLA FVIVFEHVVF STGRFLDLLV PDIPESVEIK VKREYYLAKQ ALADNEALLG
ATGVKGEQPP SSEPSLGLPA
