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Anoctamin-10 (Transmembrane protein 16K)

 ANO10_HUMAN             Reviewed;         660 AA.
Q9NW15; A8K8K3; A8MV74; B3KTZ1; B3KY93; B4DJ83; B4DNK2; B7WP12;
C9JHS1; Q8IXX9;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
05-DEC-2018, entry version 126.
RecName: Full=Anoctamin-10;
AltName: Full=Transmembrane protein 16K;
Name=ANO10; Synonyms=TMEM16K;
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] (ISOFORMS 1; 3; 4 AND 5), AND
VARIANT GLN-462.
TISSUE=Substantia nigra, Teratocarcinoma, Testis, and Urinary bladder;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
MET-561 AND ALA-583.
TISSUE=Leukocyte;
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]
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).
[8]
SUBCELLULAR LOCATION.
PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
"ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
proteins.";
Am. J. Physiol. 302:C482-C493(2012).
[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).
[12]
VARIANT SCAR10 ARG-510, AND TISSUE SPECIFICITY.
PubMed=21092923; DOI=10.1016/j.ajhg.2010.10.015;
Vermeer S., Hoischen A., Meijer R.P., Gilissen C., Neveling K.,
Wieskamp N., de Brouwer A., Koenig M., Anheim M., Assoum M.,
Drouot N., Todorovic S., Milic-Rasic V., Lochmuller H., Stevanin G.,
Goizet C., David A., Durr A., Brice A., Kremer B.,
van de Warrenburg B.P., Schijvenaars M.M., Heister A., Kwint M.,
Arts P., van der Wijst J., Veltman J., Kamsteeg E.J., Scheffer H.,
Knoers N.;
"Targeted next-generation sequencing of a 12.5 Mb homozygous region
reveals ANO10 mutations in patients with autosomal-recessive
cerebellar ataxia.";
Am. J. Hum. Genet. 87:813-819(2010).
-!- FUNCTION: Does not exhibit calcium-activated chloride channel
(CaCC) activity. Can inhibit the activity of ANO1.
{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-
pass membrane protein {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:22075693, 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=5;
Name=1;
IsoId=Q9NW15-1; Sequence=Displayed;
Name=2;
IsoId=Q9NW15-2; Sequence=VSP_026033;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NW15-3; Sequence=VSP_038212;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9NW15-4; Sequence=VSP_038211;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9NW15-5; Sequence=VSP_045885;
Note=No experimental confirmation available. Ref.1 (BAG60264)
sequence is in conflict in position: 607:S->P. {ECO:0000305};
-!- TISSUE SPECIFICITY: Highly expressed in the brain. Intermediate
levels in the retina and heart and low levels in the placenta,
liver, lung, duodenum, kidney, testis and spleen. In brain areas,
highest expression in the frontal and occipital cortices and in
the cerebellum. Lower expression in the fetal brain than in the
adult brain. {ECO:0000269|PubMed:21092923}.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 10 (SCAR10)
[MIM:613728]: Spinocerebellar ataxia is a clinically and
genetically heterogeneous group of cerebellar disorders. Patients
show progressive incoordination of gait and often poor
coordination of hands, speech and eye movements, due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR10 is characterized by onset in the
teenage or young adult years of gait and limb ataxia, dysarthria,
and nystagmus associated with marked cerebellar atrophy on brain
imaging. {ECO:0000269|PubMed:21092923}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- 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=BAA91573.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=BC038855; Type=Frameshift; Positions=42; Evidence={ECO:0000305};
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EMBL; AK001237; BAA91573.1; ALT_SEQ; mRNA.
EMBL; AK096302; BAG53253.1; -; mRNA.
EMBL; AK131223; BAG54755.1; -; mRNA.
EMBL; AK292368; BAF85057.1; -; mRNA.
EMBL; AK295969; BAG58745.1; -; mRNA.
EMBL; AK297949; BAG60264.1; -; mRNA.
EMBL; AC097638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC135852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64696.1; -; Genomic_DNA.
EMBL; CH471055; EAW64697.1; -; Genomic_DNA.
EMBL; BC038855; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS2710.2; -. [Q9NW15-1]
CCDS; CCDS56247.1; -. [Q9NW15-4]
CCDS; CCDS56248.1; -. [Q9NW15-3]
CCDS; CCDS56249.1; -. [Q9NW15-2]
CCDS; CCDS56250.1; -. [Q9NW15-5]
RefSeq; NP_001191760.1; NM_001204831.2. [Q9NW15-5]
RefSeq; NP_001191761.1; NM_001204832.2. [Q9NW15-3]
RefSeq; NP_001191762.1; NM_001204833.2. [Q9NW15-4]
RefSeq; NP_001191763.1; NM_001204834.2. [Q9NW15-2]
RefSeq; NP_001333392.1; NM_001346463.1.
RefSeq; NP_001333393.1; NM_001346464.1.
RefSeq; NP_001333394.1; NM_001346465.1.
RefSeq; NP_001333395.1; NM_001346466.1. [Q9NW15-3]
RefSeq; NP_001333396.1; NM_001346467.1.
RefSeq; NP_001333397.1; NM_001346468.1. [Q9NW15-1]
RefSeq; NP_001333398.1; NM_001346469.1. [Q9NW15-3]
RefSeq; NP_060545.3; NM_018075.4. [Q9NW15-1]
RefSeq; XP_016862211.1; XM_017006722.1.
UniGene; Hs.656657; -.
PDB; 5OC9; X-ray; 3.20 A; A/B=1-660.
PDBsum; 5OC9; -.
ProteinModelPortal; Q9NW15; -.
SMR; Q9NW15; -.
BioGrid; 120435; 4.
IntAct; Q9NW15; 4.
MINT; Q9NW15; -.
STRING; 9606.ENSP00000292246; -.
TCDB; 1.A.17.1.26; the calcium-dependent chloride channel (ca-clc) family.
iPTMnet; Q9NW15; -.
PhosphoSitePlus; Q9NW15; -.
BioMuta; ANO10; -.
DMDM; 148887071; -.
EPD; Q9NW15; -.
MaxQB; Q9NW15; -.
PaxDb; Q9NW15; -.
PeptideAtlas; Q9NW15; -.
PRIDE; Q9NW15; -.
ProteomicsDB; 82887; -.
ProteomicsDB; 82888; -. [Q9NW15-2]
ProteomicsDB; 82889; -. [Q9NW15-3]
ProteomicsDB; 82890; -. [Q9NW15-4]
DNASU; 55129; -.
Ensembl; ENST00000292246; ENSP00000292246; ENSG00000160746. [Q9NW15-1]
Ensembl; ENST00000350459; ENSP00000327767; ENSG00000160746. [Q9NW15-2]
Ensembl; ENST00000396091; ENSP00000379398; ENSG00000160746. [Q9NW15-3]
Ensembl; ENST00000414522; ENSP00000396990; ENSG00000160746. [Q9NW15-5]
Ensembl; ENST00000451430; ENSP00000394119; ENSG00000160746. [Q9NW15-4]
GeneID; 55129; -.
KEGG; hsa:55129; -.
UCSC; uc003cmv.4; human. [Q9NW15-1]
CTD; 55129; -.
DisGeNET; 55129; -.
EuPathDB; HostDB:ENSG00000160746.12; -.
GeneCards; ANO10; -.
HGNC; HGNC:25519; ANO10.
HPA; HPA051569; -.
MalaCards; ANO10; -.
MIM; 613726; gene.
MIM; 613728; phenotype.
neXtProt; NX_Q9NW15; -.
OpenTargets; ENSG00000160746; -.
Orphanet; 284289; Adult-onset autosomal recessive cerebellar ataxia.
PharmGKB; PA164715433; -.
eggNOG; KOG2513; Eukaryota.
eggNOG; ENOG410XPYE; LUCA.
GeneTree; ENSGT00940000157537; -.
HOGENOM; HOG000007605; -.
HOVERGEN; HBG071385; -.
InParanoid; Q9NW15; -.
KO; K19327; -.
OMA; YIIKHEL; -.
OrthoDB; EOG091G06A3; -.
PhylomeDB; Q9NW15; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; ANO10; human.
GenomeRNAi; 55129; -.
PRO; PR:Q9NW15; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000160746; Expressed in 215 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_ANO10; -.
ExpressionAtlas; Q9NW15; baseline and differential.
Genevisible; Q9NW15; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
GO; GO:0006812; P:cation transport; IDA:UniProtKB.
GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031291; Anoctamin-10.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF40; PTHR12308:SF40; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Membrane; Neurodegeneration; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 660 Anoctamin-10.
/FTId=PRO_0000289957.
TOPO_DOM 1 207 Cytoplasmic. {ECO:0000255}.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TOPO_DOM 229 240 Extracellular. {ECO:0000255}.
TRANSMEM 241 261 Helical. {ECO:0000255}.
TOPO_DOM 262 316 Cytoplasmic. {ECO:0000255}.
TRANSMEM 317 337 Helical. {ECO:0000255}.
TOPO_DOM 338 352 Extracellular. {ECO:0000255}.
TRANSMEM 353 373 Helical. {ECO:0000255}.
TOPO_DOM 374 400 Cytoplasmic. {ECO:0000255}.
TRANSMEM 401 421 Helical. {ECO:0000255}.
TOPO_DOM 422 500 Extracellular. {ECO:0000255}.
TRANSMEM 501 521 Helical. {ECO:0000255}.
TOPO_DOM 522 553 Cytoplasmic. {ECO:0000255}.
TRANSMEM 554 574 Helical. {ECO:0000255}.
TOPO_DOM 575 590 Extracellular. {ECO:0000255}.
TRANSMEM 591 611 Helical. {ECO:0000255}.
TOPO_DOM 612 660 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 47 158 GAQLLFRPLLNKYEQETLENQNLYLVGASKIRMLLGAEAVG
LVKECNDNTMRAFTYRTRQNFKGFDDNNDDFLTMAECQFII
KHELENLRAKDEKMIPGYPQAKLYPGKSLL -> V (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038211.
VAR_SEQ 47 112 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038212.
VAR_SEQ 198 387 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026033.
VAR_SEQ 600 660 HALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQM
KLVTENLKEEPMESGKEKAT -> AASCKLVSLPRYSWSTN
SVPGTVIGPGV (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045885.
VARIANT 462 462 R -> Q (in dbSNP:rs3772165).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_032638.
VARIANT 510 510 L -> R (in SCAR10; dbSNP:rs387907089).
{ECO:0000269|PubMed:21092923}.
/FTId=VAR_064888.
VARIANT 561 561 T -> M (in dbSNP:rs17409162).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_032639.
VARIANT 583 583 V -> A (in dbSNP:rs17853862).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_032640.
STRAND 19 23 {ECO:0000244|PDB:5OC9}.
HELIX 29 40 {ECO:0000244|PDB:5OC9}.
HELIX 43 45 {ECO:0000244|PDB:5OC9}.
STRAND 51 54 {ECO:0000244|PDB:5OC9}.
HELIX 60 62 {ECO:0000244|PDB:5OC9}.
STRAND 69 73 {ECO:0000244|PDB:5OC9}.
HELIX 76 86 {ECO:0000244|PDB:5OC9}.
STRAND 89 92 {ECO:0000244|PDB:5OC9}.
STRAND 97 99 {ECO:0000244|PDB:5OC9}.
HELIX 105 107 {ECO:0000244|PDB:5OC9}.
HELIX 121 133 {ECO:0000244|PDB:5OC9}.
STRAND 141 143 {ECO:0000244|PDB:5OC9}.
STRAND 146 150 {ECO:0000244|PDB:5OC9}.
HELIX 157 163 {ECO:0000244|PDB:5OC9}.
STRAND 166 172 {ECO:0000244|PDB:5OC9}.
HELIX 176 186 {ECO:0000244|PDB:5OC9}.
HELIX 197 204 {ECO:0000244|PDB:5OC9}.
HELIX 206 234 {ECO:0000244|PDB:5OC9}.
HELIX 240 272 {ECO:0000244|PDB:5OC9}.
HELIX 279 281 {ECO:0000244|PDB:5OC9}.
STRAND 291 294 {ECO:0000244|PDB:5OC9}.
STRAND 296 298 {ECO:0000244|PDB:5OC9}.
STRAND 301 304 {ECO:0000244|PDB:5OC9}.
HELIX 307 316 {ECO:0000244|PDB:5OC9}.
HELIX 318 348 {ECO:0000244|PDB:5OC9}.
HELIX 355 358 {ECO:0000244|PDB:5OC9}.
HELIX 361 387 {ECO:0000244|PDB:5OC9}.
HELIX 393 421 {ECO:0000244|PDB:5OC9}.
HELIX 426 437 {ECO:0000244|PDB:5OC9}.
HELIX 439 448 {ECO:0000244|PDB:5OC9}.
HELIX 450 468 {ECO:0000244|PDB:5OC9}.
HELIX 477 487 {ECO:0000244|PDB:5OC9}.
HELIX 495 511 {ECO:0000244|PDB:5OC9}.
TURN 512 514 {ECO:0000244|PDB:5OC9}.
HELIX 518 539 {ECO:0000244|PDB:5OC9}.
HELIX 555 576 {ECO:0000244|PDB:5OC9}.
HELIX 578 581 {ECO:0000244|PDB:5OC9}.
HELIX 588 612 {ECO:0000244|PDB:5OC9}.
HELIX 618 638 {ECO:0000244|PDB:5OC9}.
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


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