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Anoctamin-9 (Transmembrane protein 16J) (Tumor protein p53-inducible protein 5) (p53-induced gene 5 protein)

 ANO9_HUMAN              Reviewed;         782 AA.
A1A5B4; B3KUC4; B4E134; Q8TEN4;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
27-MAY-2015, sequence version 3.
12-SEP-2018, entry version 104.
RecName: Full=Anoctamin-9;
AltName: Full=Transmembrane protein 16J;
AltName: Full=Tumor protein p53-inducible protein 5;
AltName: Full=p53-induced gene 5 protein;
Name=ANO9; Synonyms=PIG5, TMEM16J, TP53I5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-391 AND ARG-399.
TISSUE=Spleen;
PubMed=12693554; DOI=10.1093/dnares/10.1.49;
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
Ohara O.;
"Characterization of long cDNA clones from human adult spleen. II. The
complete sequences of 81 cDNA clones.";
DNA Res. 10:49-57(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS VAL-391 AND ARG-399.
TISSUE=Salivary gland, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-391 AND ARG-399.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20056604; DOI=10.1074/jbc.M109.065367;
Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
Martins J.R., Kunzelmann K.;
"Expression and function of epithelial anoctamins.";
J. Biol. Chem. 285:7838-7845(2010).
[6]
REVIEW.
PubMed=21642943; DOI=10.1038/aps.2011.48;
Duran C., Hartzell H.C.;
"Physiological roles and diseases of Tmem16/Anoctamin proteins: are
they all chloride channels?";
Acta Pharmacol. Sin. 32:685-692(2011).
[7]
ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
PubMed=22178883; DOI=10.1159/000335765;
Ousingsawat J., Kongsuphol P., Schreiber R., Kunzelmann K.;
"CFTR and TMEM16A are separate but functionally related Cl-channels.";
Cell. Physiol. Biochem. 28:715-724(2011).
[8]
REVIEW.
PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
"Anoctamins.";
Pflugers Arch. 462:195-208(2011).
[9]
REVIEW.
PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
Winpenny J.P., Gray M.A.;
"The anoctamin (TMEM16) gene family: calcium-activated chloride
channels come of age.";
Exp. Physiol. 97:175-176(2012).
[10]
REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
"The anoctamin family: TMEM16A and TMEM16B as calcium-activated
chloride channels.";
Exp. Physiol. 97:177-183(2012).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22946059; DOI=10.1242/jcs.109553;
Tian Y., Schreiber R., Kunzelmann K.;
"Anoctamins are a family of Ca2+ activated Cl- channels.";
J. Cell Sci. 125:4991-4998(2012).
-!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
scrambles phosphatidylserine, phosphatidylcholine and
galactosylceramide (By similarity). Does not exhibit calcium-
activated chloride channel (CaCC) activity. Can inhibit the
activity of ANO1. {ECO:0000250|UniProtKB:P86044,
ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.
-!- INTERACTION:
Q12959:DLG1; NbExp=2; IntAct=EBI-3843564, EBI-357481;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.
Note=Shows predominantly an intracellular localization with a weak
expression in the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=A1A5B4-1; Sequence=Displayed;
Name=2;
IsoId=A1A5B4-2; Sequence=VSP_036489, VSP_036492;
Name=3;
IsoId=A1A5B4-3; Sequence=VSP_036490, VSP_036491;
-!- MISCELLANEOUS: The term 'anoctamin' was coined because these
channels are anion selective and have eight (OCT) transmembrane
segments. There is some dissatisfaction in the field with the Ano
nomenclature because it is not certain that all the members of
this family are anion channels or have the 8-transmembrane
topology.
-!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB84914.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK074088; BAB84914.1; ALT_SEQ; mRNA.
EMBL; AK096874; BAG53386.1; -; mRNA.
EMBL; AK303642; BAG64646.1; -; mRNA.
EMBL; AC138230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC128557; AAI28558.1; -; mRNA.
CCDS; CCDS31326.1; -. [A1A5B4-1]
RefSeq; NP_001012302.2; NM_001012302.2. [A1A5B4-1]
RefSeq; XP_011518355.1; XM_011520053.2. [A1A5B4-2]
UniGene; Hs.501622; -.
ProteinModelPortal; A1A5B4; -.
BioGrid; 130747; 1.
IntAct; A1A5B4; 1.
MINT; A1A5B4; -.
STRING; 9606.ENSP00000332788; -.
TCDB; 1.A.17.1.5; the calcium-dependent chloride channel (ca-clc) family.
iPTMnet; A1A5B4; -.
PhosphoSitePlus; A1A5B4; -.
BioMuta; ANO9; -.
EPD; A1A5B4; -.
PaxDb; A1A5B4; -.
PRIDE; A1A5B4; -.
ProteomicsDB; 110; -.
ProteomicsDB; 111; -. [A1A5B4-2]
ProteomicsDB; 112; -. [A1A5B4-3]
Ensembl; ENST00000332826; ENSP00000332788; ENSG00000185101. [A1A5B4-1]
GeneID; 338440; -.
KEGG; hsa:338440; -.
UCSC; uc001lpi.3; human. [A1A5B4-1]
CTD; 338440; -.
DisGeNET; 338440; -.
EuPathDB; HostDB:ENSG00000185101.12; -.
GeneCards; ANO9; -.
HGNC; HGNC:20679; ANO9.
HPA; HPA039948; -.
HPA; HPA040112; -.
neXtProt; NX_A1A5B4; -.
OpenTargets; ENSG00000185101; -.
PharmGKB; PA164715791; -.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG100444; -.
InParanoid; A1A5B4; -.
KO; K19503; -.
OMA; KLIAAWY; -.
OrthoDB; EOG091G02JM; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; ANO9; human.
GenomeRNAi; 338440; -.
PRO; PR:A1A5B4; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000185101; Expressed in 125 organ(s), highest expression level in mucosa of transverse colon.
CleanEx; HS_ANO9; -.
Genevisible; A1A5B4; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IMP:UniProtKB.
GO; GO:0017128; F:phospholipid scramblase activity; IEA:Ensembl.
GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IEA:Ensembl.
GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IEA:Ensembl.
GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IEA:Ensembl.
GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:1902939; P:negative regulation of intracellular calcium activated chloride channel activity; IDA:UniProtKB.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031290; Anoctamin-9.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF37; PTHR12308:SF37; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Lipid transport; Membrane; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 782 Anoctamin-9.
/FTId=PRO_0000289329.
TOPO_DOM 1 198 Cytoplasmic. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TOPO_DOM 220 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 285 Helical. {ECO:0000255}.
TOPO_DOM 286 331 Cytoplasmic. {ECO:0000255}.
TRANSMEM 332 352 Helical. {ECO:0000255}.
TOPO_DOM 353 373 Extracellular. {ECO:0000255}.
TRANSMEM 374 394 Helical. {ECO:0000255}.
TOPO_DOM 395 423 Cytoplasmic. {ECO:0000255}.
TRANSMEM 424 444 Helical. {ECO:0000255}.
TOPO_DOM 445 552 Extracellular. {ECO:0000255}.
TRANSMEM 553 573 Helical. {ECO:0000255}.
TOPO_DOM 574 604 Cytoplasmic. {ECO:0000255}.
TRANSMEM 605 625 Helical. {ECO:0000255}.
TOPO_DOM 626 703 Extracellular. {ECO:0000255}.
TRANSMEM 704 724 Helical. {ECO:0000255}.
TOPO_DOM 725 782 Cytoplasmic. {ECO:0000255}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 674 674 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 299 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036489.
VAR_SEQ 156 186 GEGRLKKTWARWRHMFREQPVDEIRNYFGEK -> VRGGPA
WRGPWGGTLGWGLSLSVTRARGRDA (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036490.
VAR_SEQ 187 782 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036491.
VAR_SEQ 300 305 VWDEEQ -> MPAVSE (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036492.
VARIANT 93 93 L -> F (in dbSNP:rs7395065).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_054621.
VARIANT 391 391 I -> V (in dbSNP:rs10794324).
{ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_032617.
VARIANT 399 399 C -> R (in dbSNP:rs10794323).
{ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_032618.
SEQUENCE 782 AA; 90333 MW; 6A359B63DD92AFF7 CRC64;
MQGEESLRIL VEPEGDSFPL MEISTCETEA SEQWDYVLVA QRHTQRDPRQ ARQQQFLEEL
RRKGFHIKVI RDQKQVFFGI RADNSVFGLY RTLLLEPEGP APHAELAAPT TIPVTTSLRI
RIVNFVVMNN KTSAGETFED LMKDGVFEAR FPLHKGEGRL KKTWARWRHM FREQPVDEIR
NYFGEKVALY FVWLGWYTYM LVPAALTGLL VFLSGFSLFE ASQISKEICE AHDILMCPLG
DHSRRYQRLS ETCTFAKLTH LFDNDGTVVF AIFMALWATV FLEIWKRQRA RVVLHWDLYV
WDEEQEEMAL QLINCPDYKL RPYQHSYLRS TVILVLTLLM ICLMIGMAHV LVVYRVLASA
LFSSSAVPFL EEQVTTAVVV TGALVHYVTI IIMTKINRCV ALKLCDFEMP RTFSERESRF
TIRFFTLQFF THFSSLIYIA FILGRINGHP GKSTRLAGLW KLEECHASGC MMDLFVQMAI
IMGLKQTLSN CVEYLVPWVT HKCRSLRASE SGHLPRDPEL RDWRRNYLLN PVNTFSLFDE
FMEMMIQYGF TTIFVAAFPL APLLALFSNL VEIRLDAIKM VWLQRRLVPR KAKDIGTWLQ
VLETIGVLAV IANGMVIAFT SEFIPRVVYK YRYSPCLKEG NSTVDCLKGY VNHSLSVFHT
KDFQDPDGIE GSENVTLCRY RDYRNPPDYN FSEQFWFLLA IRLAFVILFE HVALCIKLIA
AWFVPDIPQS VKNKVLEVKY QRLREKMWHG RQRLGGVGAG SRPPMPAHPT PASIFSARST
DV


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