ID   ANO10_HUMAN             Reviewed;         660 AA.
AC   Q9NW15; A8K8K3; A8MV74; B3KTZ1; B3KY93; B4DJ83; B4DNK2; B7WP12; C9JHS1;
AC   Q8IXX9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Anoctamin-10;
DE   AltName: Full=Transmembrane protein 16K;
GN   Name=ANO10; Synonyms=TMEM16K;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5), AND
RP   VARIANT GLN-462.
RC   TISSUE=Substantia nigra, Teratocarcinoma, Testis, and Urinary bladder;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-561
RP   AND ALA-583.
RC   TISSUE=Leukocyte;
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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   [6]
RP   REVIEW.
RX   PubMed=21642943; DOI=10.1038/aps.2011.48;
RA   Duran C., Hartzell H.C.;
RT   "Physiological roles and diseases of Tmem16/Anoctamin proteins: are they
RT   all chloride channels?";
RL   Acta Pharmacol. Sin. 32:685-692(2011).
RN   [7]
RP   REVIEW.
RX   PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
RA   Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
RA   Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
RT   "Anoctamins.";
RL   Pflugers Arch. 462:195-208(2011).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
RA   Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
RT   "ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
RT   proteins.";
RL   Am. J. Physiol. 302:C482-C493(2012).
RN   [9]
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   [10]
RP   REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
RX   PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
RA   Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
RT   "The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride
RT   channels.";
RL   Exp. Physiol. 97:177-183(2012).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22946059; DOI=10.1242/jcs.109553;
RA   Tian Y., Schreiber R., Kunzelmann K.;
RT   "Anoctamins are a family of Ca2+ activated Cl- channels.";
RL   J. Cell Sci. 125:4991-4998(2012).
RN   [12]
RP   VARIANT SCAR10 ARG-510, AND TISSUE SPECIFICITY.
RX   PubMed=21092923; DOI=10.1016/j.ajhg.2010.10.015;
RA   Vermeer S., Hoischen A., Meijer R.P., Gilissen C., Neveling K.,
RA   Wieskamp N., de Brouwer A., Koenig M., Anheim M., Assoum M., Drouot N.,
RA   Todorovic S., Milic-Rasic V., Lochmuller H., Stevanin G., Goizet C.,
RA   David A., Durr A., Brice A., Kremer B., van de Warrenburg B.P.,
RA   Schijvenaars M.M., Heister A., Kwint M., Arts P., van der Wijst J.,
RA   Veltman J., Kamsteeg E.J., Scheffer H., Knoers N.;
RT   "Targeted next-generation sequencing of a 12.5 Mb homozygous region reveals
RT   ANO10 mutations in patients with autosomal-recessive cerebellar ataxia.";
RL   Am. J. Hum. Genet. 87:813-819(2010).
CC   -!- FUNCTION: Does not exhibit calcium-activated chloride channel (CaCC)
CC       activity. Can inhibit the activity of ANO1.
CC       {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
CC       ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:20056604,
CC       ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows
CC       predominantly an intracellular localization with a weak expression in
CC       the cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9NW15-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NW15-2; Sequence=VSP_026033;
CC       Name=3;
CC         IsoId=Q9NW15-3; Sequence=VSP_038212;
CC       Name=4;
CC         IsoId=Q9NW15-4; Sequence=VSP_038211;
CC       Name=5;
CC         IsoId=Q9NW15-5; Sequence=VSP_045885;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain. Intermediate levels
CC       in the retina and heart and low levels in the placenta, liver, lung,
CC       duodenum, kidney, testis and spleen. In brain areas, highest expression
CC       in the frontal and occipital cortices and in the cerebellum. Lower
CC       expression in the fetal brain than in the adult brain.
CC       {ECO:0000269|PubMed:21092923}.
CC   -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 10 (SCAR10)
CC       [MIM:613728]: A form of spinocerebellar ataxia, a clinically and
CC       genetically heterogeneous group of cerebellar disorders. Patients show
CC       progressive incoordination of gait and often poor coordination of
CC       hands, speech and eye movements, due to degeneration of the cerebellum
CC       with variable involvement of the brainstem and spinal cord. SCAR10 is
CC       characterized by onset in the teenage or young adult years of gait and
CC       limb ataxia, dysarthria, and nystagmus associated with marked
CC       cerebellar atrophy on brain imaging. {ECO:0000269|PubMed:21092923}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91573.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC       Sequence=BC038855; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK001237; BAA91573.1; ALT_SEQ; mRNA.
DR   EMBL; AK096302; BAG53253.1; -; mRNA.
DR   EMBL; AK131223; BAG54755.1; -; mRNA.
DR   EMBL; AK292368; BAF85057.1; -; mRNA.
DR   EMBL; AK295969; BAG58745.1; -; mRNA.
DR   EMBL; AK297949; BAG60264.1; -; mRNA.
DR   EMBL; AC097638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64696.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW64697.1; -; Genomic_DNA.
DR   EMBL; BC038855; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS2710.2; -. [Q9NW15-1]
DR   CCDS; CCDS56247.1; -. [Q9NW15-4]
DR   CCDS; CCDS56248.1; -. [Q9NW15-3]
DR   CCDS; CCDS56249.1; -. [Q9NW15-2]
DR   CCDS; CCDS56250.1; -. [Q9NW15-5]
DR   RefSeq; NP_001191760.1; NM_001204831.2. [Q9NW15-5]
DR   RefSeq; NP_001191761.1; NM_001204832.2. [Q9NW15-3]
DR   RefSeq; NP_001191762.1; NM_001204833.2. [Q9NW15-4]
DR   RefSeq; NP_001191763.1; NM_001204834.2. [Q9NW15-2]
DR   RefSeq; NP_001333392.1; NM_001346463.1.
DR   RefSeq; NP_001333393.1; NM_001346464.1.
DR   RefSeq; NP_001333394.1; NM_001346465.1.
DR   RefSeq; NP_001333395.1; NM_001346466.1. [Q9NW15-3]
DR   RefSeq; NP_001333396.1; NM_001346467.1.
DR   RefSeq; NP_001333397.1; NM_001346468.1. [Q9NW15-1]
DR   RefSeq; NP_001333398.1; NM_001346469.1. [Q9NW15-3]
DR   RefSeq; NP_060545.3; NM_018075.4. [Q9NW15-1]
DR   RefSeq; XP_016862211.1; XM_017006722.1.
DR   PDB; 5OC9; X-ray; 3.20 A; A/B=1-660.
DR   PDB; 6R65; X-ray; 3.50 A; A/B=1-660.
DR   PDB; 6R7X; EM; 3.47 A; A/B=1-660.
DR   PDB; 6R7Y; EM; 4.20 A; A/B=1-660.
DR   PDB; 6R7Z; EM; 5.14 A; A/B=1-660.
DR   PDBsum; 5OC9; -.
DR   PDBsum; 6R65; -.
DR   PDBsum; 6R7X; -.
DR   PDBsum; 6R7Y; -.
DR   PDBsum; 6R7Z; -.
DR   AlphaFoldDB; Q9NW15; -.
DR   EMDB; EMD-4746; -.
DR   EMDB; EMD-4747; -.
DR   EMDB; EMD-4748; -.
DR   SMR; Q9NW15; -.
DR   BioGRID; 120435; 39.
DR   IntAct; Q9NW15; 11.
DR   MINT; Q9NW15; -.
DR   STRING; 9606.ENSP00000292246; -.
DR   TCDB; 1.A.17.1.26; the calcium-dependent chloride channel (ca-clc) family.
DR   iPTMnet; Q9NW15; -.
DR   PhosphoSitePlus; Q9NW15; -.
DR   SwissPalm; Q9NW15; -.
DR   BioMuta; ANO10; -.
DR   DMDM; 148887071; -.
DR   EPD; Q9NW15; -.
DR   jPOST; Q9NW15; -.
DR   MassIVE; Q9NW15; -.
DR   MaxQB; Q9NW15; -.
DR   PaxDb; 9606-ENSP00000292246; -.
DR   PeptideAtlas; Q9NW15; -.
DR   ProteomicsDB; 10245; -.
DR   ProteomicsDB; 82887; -. [Q9NW15-1]
DR   ProteomicsDB; 82888; -. [Q9NW15-2]
DR   ProteomicsDB; 82889; -. [Q9NW15-3]
DR   ProteomicsDB; 82890; -. [Q9NW15-4]
DR   Pumba; Q9NW15; -.
DR   Antibodypedia; 29353; 80 antibodies from 25 providers.
DR   DNASU; 55129; -.
DR   Ensembl; ENST00000292246.8; ENSP00000292246.3; ENSG00000160746.13. [Q9NW15-1]
DR   Ensembl; ENST00000350459.8; ENSP00000327767.4; ENSG00000160746.13. [Q9NW15-2]
DR   Ensembl; ENST00000396091.7; ENSP00000379398.3; ENSG00000160746.13. [Q9NW15-3]
DR   Ensembl; ENST00000414522.6; ENSP00000396990.2; ENSG00000160746.13. [Q9NW15-5]
DR   Ensembl; ENST00000451430.6; ENSP00000394119.2; ENSG00000160746.13. [Q9NW15-4]
DR   GeneID; 55129; -.
DR   KEGG; hsa:55129; -.
DR   MANE-Select; ENST00000292246.8; ENSP00000292246.3; NM_018075.5; NP_060545.3.
DR   UCSC; uc003cmv.4; human. [Q9NW15-1]
DR   AGR; HGNC:25519; -.
DR   CTD; 55129; -.
DR   DisGeNET; 55129; -.
DR   GeneCards; ANO10; -.
DR   HGNC; HGNC:25519; ANO10.
DR   HPA; ENSG00000160746; Low tissue specificity.
DR   MalaCards; ANO10; -.
DR   MIM; 613726; gene.
DR   MIM; 613728; phenotype.
DR   neXtProt; NX_Q9NW15; -.
DR   OpenTargets; ENSG00000160746; -.
DR   Orphanet; 284289; Adult-onset autosomal recessive cerebellar ataxia.
DR   PharmGKB; PA164715433; -.
DR   VEuPathDB; HostDB:ENSG00000160746; -.
DR   eggNOG; KOG2513; Eukaryota.
DR   GeneTree; ENSGT00940000157537; -.
DR   HOGENOM; CLU_615312_0_0_1; -.
DR   InParanoid; Q9NW15; -.
DR   OMA; YENHRTA; -.
DR   OrthoDB; 534027at2759; -.
DR   PhylomeDB; Q9NW15; -.
DR   TreeFam; TF314265; -.
DR   PathwayCommons; Q9NW15; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion.
DR   SignaLink; Q9NW15; -.
DR   BioGRID-ORCS; 55129; 13 hits in 1162 CRISPR screens.
DR   ChiTaRS; ANO10; human.
DR   GenomeRNAi; 55129; -.
DR   Pharos; Q9NW15; Tbio.
DR   PRO; PR:Q9NW15; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9NW15; Protein.
DR   Bgee; ENSG00000160746; Expressed in stromal cell of endometrium and 186 other cell types or tissues.
DR   ExpressionAtlas; Q9NW15; baseline and differential.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005227; F:calcium-activated cation channel activity; IDA:UniProtKB.
DR   GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR   GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR   GO; GO:0006812; P:monoatomic cation transport; IDA:UniProtKB.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR049452; Anoctamin_TM.
DR   PANTHER; PTHR12308; ANOCTAMIN; 1.
DR   PANTHER; PTHR12308:SF40; ANOCTAMIN-10; 1.
DR   Pfam; PF04547; Anoctamin; 1.
DR   Genevisible; Q9NW15; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW   Membrane; Neurodegeneration; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..660
FT                   /note="Anoctamin-10"
FT                   /id="PRO_0000289957"
FT   TOPO_DOM        1..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        338..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..400
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        575..590
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        591..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        612..660
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         47..158
FT                   /note="GAQLLFRPLLNKYEQETLENQNLYLVGASKIRMLLGAEAVGLVKECNDNTMR
FT                   AFTYRTRQNFKGFDDNNDDFLTMAECQFIIKHELENLRAKDEKMIPGYPQAKLYPGKSL
FT                   L -> V (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_038211"
FT   VAR_SEQ         47..112
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_038212"
FT   VAR_SEQ         198..387
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026033"
FT   VAR_SEQ         600..660
FT                   /note="HALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQMKLVTENLKEEP
FT                   MESGKEKAT -> AASCKLVSLPRYSWSTNSVPGTVIGPGV (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045885"
FT   VARIANT         462
FT                   /note="R -> Q (in dbSNP:rs3772165)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_032638"
FT   VARIANT         510
FT                   /note="L -> R (in SCAR10; dbSNP:rs387907089)"
FT                   /evidence="ECO:0000269|PubMed:21092923"
FT                   /id="VAR_064888"
FT   VARIANT         561
FT                   /note="T -> M (in dbSNP:rs17409162)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032639"
FT   VARIANT         583
FT                   /note="V -> A (in dbSNP:rs17853862)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032640"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           29..40
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           76..86
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           121..133
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           197..204
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           206..234
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   HELIX           240..272
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           307..316
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           318..348
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   HELIX           355..358
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           361..387
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           393..421
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           426..437
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           439..448
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           450..468
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           477..487
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           495..511
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   TURN            512..514
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           518..539
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           555..576
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           578..581
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:6R7X"
FT   HELIX           588..612
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   HELIX           618..638
FT                   /evidence="ECO:0007829|PDB:5OC9"
FT   CONFLICT        Q9NW15-5:607
FT                   /note="S -> P (in Ref. 1; BAG60264)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   660 AA;  76329 MW;  21582D364497ADFD CRC64;
     MKVTLSALDT SESSFTPLVV IELAQDVKEE TKEWLKNRII AKKKDGGAQL LFRPLLNKYE
     QETLENQNLY LVGASKIRML LGAEAVGLVK ECNDNTMRAF TYRTRQNFKG FDDNNDDFLT
     MAECQFIIKH ELENLRAKDE KMIPGYPQAK LYPGKSLLRR LLTSGIVIQV FPLHDSEALK
     KLEDTWYTRF ALKYQPIDSI RGYFGETIAL YFGFLEYFTF ALIPMAVIGL PYYLFVWEDY
     DKYVIFASFN LIWSTVILEL WKRGCANMTY RWGTLLMKRK FEEPRPGFHG VLGINSITGK
     EEPLYPSYKR QLRIYLVSLP FVCLCLYFSL YVMMIYFDME VWALGLHENS GSEWTSVLLY
     VPSIIYAIVI EIMNRLYRYA AEFLTSWENH RLESAYQNHL ILKVLVFNFL NCFASLFYIA
     FVLKDMKLLR QSLATLLITS QILNQIMESF LPYWLQRKHG VRVKRKVQAL KADIDATLYE
     QVILEKEMGT YLGTFDDYLE LFLQFGYVSL FSCVYPLAAA FAVLNNFTEV NSDALKMCRV
     FKRPFSEPSA NIGVWQLAFE TMSVISVVTN CALIGMSPQV NAVFPESKAD LILIVVAVEH
     ALLALKFILA FAIPDKPRHI QMKLARLEFE SLEALKQQQM KLVTENLKEE PMESGKEKAT
//