ANO10_HUMAN
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 03-AUG-2022, entry version 147.
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 SMR; Q9NW15; -.
DR BioGRID; 120435; 35.
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 BioMuta; ANO10; -.
DR DMDM; 148887071; -.
DR EPD; Q9NW15; -.
DR jPOST; Q9NW15; -.
DR MassIVE; Q9NW15; -.
DR MaxQB; Q9NW15; -.
DR PaxDb; Q9NW15; -.
DR PeptideAtlas; Q9NW15; -.
DR PRIDE; 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 Antibodypedia; 29353; 75 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 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; NLGVDWV; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q9NW15; -.
DR TreeFam; TF314265; -.
DR PathwayCommons; Q9NW15; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q9NW15; -.
DR BioGRID-ORCS; 55129; 9 hits in 1083 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 184 other tissues.
DR ExpressionAtlas; Q9NW15; baseline and differential.
DR Genevisible; Q9NW15; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031291; Anoctamin-10.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF40; PTHR12308:SF40; 1.
DR Pfam; PF04547; Anoctamin; 1.
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
