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Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2 )-ATPase 2) (EC 3.6.3.8) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2 ) ATPase)

 AT2A2_HUMAN             Reviewed;        1042 AA.
P16615; A6NDN7; B4DF05; P16614; Q86VJ2;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 210.
RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
Short=SERCA2;
Short=SR Ca(2+)-ATPase 2;
EC=3.6.3.8;
AltName: Full=Calcium pump 2;
AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform;
AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
Name=ATP2A2; Synonyms=ATP2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney;
PubMed=2844796;
Lytton J., Maclennan D.H.;
"Molecular cloning of cDNAs from human kidney coding for two
alternatively spliced products of the cardiac Ca2+-ATPase gene.";
J. Biol. Chem. 263:15024-15031(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1042 (ISOFORM 4).
TISSUE=Cerebellum;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 954-1042 (ISOFORM 3), AND TISSUE
SPECIFICITY.
PubMed=12659872; DOI=10.1016/S0006-291X(03)00405-4;
Gelebart P., Martin V., Enouf J., Papp B.;
"Identification of a new SERCA2 splice variant regulated during
monocytic differentiation.";
Biochem. Biophys. Res. Commun. 303:676-684(2003).
[6]
INTERACTION WITH TRAM2.
PubMed=14749390; DOI=10.1128/MCB.24.4.1758-1768.2004;
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b
and is necessary for collagen type I synthesis.";
Mol. Cell. Biol. 24:1758-1768(2004).
[7]
NITRATION AT TYR-294 AND TYR-295.
PubMed=16399855; DOI=10.1152/ajpheart.01293.2005;
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H.,
Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.;
"Detection of sequence-specific tyrosine nitration of manganese SOD
and SERCA in cardiovascular disease and aging.";
Am. J. Physiol. 290:H2220-H2227(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INTERACTION WITH HAX1.
PubMed=18971376; DOI=10.1091/mbc.E08-06-0587;
Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D.,
Kontrogianni-Konstantopoulos A., Kranias E.G.;
"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates
its protein levels to promote cell survival.";
Mol. Biol. Cell 20:306-318(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH SLC35G1 AND STIM1.
PubMed=22084111; DOI=10.1073/pnas.1117231108;
Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
"POST, partner of stromal interaction molecule 1 (STIM1), targets
STIM1 to multiple transporters.";
Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND SER-663, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
INTERACTION WITH TMEM203.
PubMed=25996873; DOI=10.1371/journal.pone.0127480;
Shambharkar P.B., Bittinger M., Latario B., Xiong Z.,
Bandyopadhyay S., Davis V., Lin V., Yang Y., Valdez R., Labow M.A.;
"TMEM203 is a novel regulator of intracellular calcium homeostasis and
is required for spermatogenesis.";
PLoS ONE 10:E0127480-E0127480(2015).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
VARIANTS DD.
PubMed=10441323; DOI=10.1093/hmg/8.9.1611;
Sakuntabhai A., Burge S., Monk S., Hovnanian A.;
"Spectrum of novel ATP2A2 mutations in patients with Darier's
disease.";
Hum. Mol. Genet. 8:1611-1619(1999).
[20]
VARIANTS DD, AND TISSUE SPECIFICITY.
PubMed=10441324; DOI=10.1093/hmg/8.9.1621;
Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L.,
Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P.,
Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G.,
Munro C.S., Strachan T.;
"ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes
are associated with missense mutations, but neuropsychiatric features
are independent of mutation class.";
Hum. Mol. Genet. 8:1621-1630(1999).
[21]
VARIANTS DD THR-39; ARG-560 AND LEU-765.
PubMed=10441325; DOI=10.1093/hmg/8.9.1631;
Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y.,
O'Donovan M.C., Craddock N., Owen M.J.;
"ATP2A2 mutations in Darier's disease and their relationship to
neuropsychiatric phenotypes.";
Hum. Mol. Genet. 8:1631-1636(1999).
[22]
VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
PubMed=10080178; DOI=10.1038/6784;
Sakuntabhai A., Ruiz-Perez V., Carter S., Jacobsen N., Burge S.,
Monk S., Smith M., Munro C.S., O'Donovan M.C., Craddock N.,
Kucherlapati R., Rees J.L., Owen M.J., Lathrop G.M., Monaco A.P.,
Strachan T., Hovnanian A.;
"Mutations in ATP2A2, encoding a Ca2+ pump, cause Darier disease.";
Nat. Genet. 21:271-277(1999).
[23]
VARIANT AKV LEU-602.
PubMed=12542527; DOI=10.1046/j.1523-1747.2003.t01-1-12045.x;
Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A.,
MacSween R., Saihan E., Hovnanian A.;
"Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2:
evidence that it is allelic to Darier's disease.";
J. Invest. Dermatol. 120:229-232(2003).
[24]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16402920; DOI=10.1042/BJ20051427;
Dally S., Bredoux R., Corvazier E., Andersen J.P., Clausen J.D.,
Dode L., Fanchaouy M., Gelebart P., Monceau V., Del Monte F.,
Gwathmey J.K., Hajjar R., Chaabane C., Bobe R., Raies A., Enouf J.;
"Ca2+-ATPases in non-failing and failing heart: evidence for a novel
cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c).";
Biochem. J. 395:249-258(2006).
[25]
VARIANT DD LEU-41 DEL.
PubMed=19995371; DOI=10.1111/j.1365-2133.2009.09580.x;
Tsuruta D., Akiyama M., Ishida-Yamamoto A., Imanishi H., Mizuno N.,
Sowa J., Kobayashi H., Ishii M., Kurokawa I., Shimizu H.;
"Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the
unique phenotype of comedonal Darier disease.";
Br. J. Dermatol. 162:687-689(2010).
-!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
of ATP coupled with the translocation of calcium from the cytosol
to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the
regulation of the contraction/relaxation cycle (PubMed:16402920).
Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways
via its interaction with TMEM64 which is critical for the TNFSF11-
induced CREB1 activation and mitochondrial ROS generation
necessary for proper osteoclast generation. Association between
TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for
activation of NFATC1 and production of mitochondrial ROS, thereby
triggering Ca (2+) signaling cascades that promote osteoclast
differentiation and activation (By similarity).
{ECO:0000250|UniProtKB:O55143, ECO:0000269|PubMed:16402920}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2).
-!- ENZYME REGULATION: Reversibly inhibited by phospholamban (PLN) at
low calcium concentrations (By similarity). Inhibited by
sarcolipin (SLN) and myoregulin (MRLN) (By similarity). Enhanced
by DWORF; DWORF increases activity by displacing sarcolipin (SLN),
phospholamban (PLN) and myoregulin (MRLN) (By similarity).
{ECO:0000250|UniProtKB:O55143, ECO:0000250|UniProtKB:P04191,
ECO:0000250|UniProtKB:Q8R429}.
-!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (By similarity). Interacts with
myoregulin (MRLN) (By similarity). Interacts with DWORF (By
similarity). Isoform 1 interacts with TRAM2 (via C-terminus)
(PubMed:14749390). Interacts with HAX1 (PubMed:18971376).
Interacts with S100A8 and S100A9 (By similarity). Interacts with
SLC35G1 and STIM1 (PubMed:22084111). Interacts with TMEM203
(PubMed:25996873). Interacts with TMEM64 and PDIA3 (By
similarity). {ECO:0000250|UniProtKB:O55143,
ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429,
ECO:0000269|PubMed:14749390, ECO:0000269|PubMed:18971376,
ECO:0000269|PubMed:22084111, ECO:0000269|PubMed:25996873}.
-!- INTERACTION:
P41143:OPRD1; NbExp=3; IntAct=EBI-358933, EBI-2624456;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=SERCA2 transcripts differ only in their 3'-UTR region
and are expressed in a tissue-specific manner.;
Name=1; Synonyms=ATP2A2B, Class 2-4, HK1, SERCA2b;
IsoId=P16615-1; Sequence=Displayed;
Note=Ubiquitous housekeeping isoform.;
Name=2; Synonyms=ATP2A2A, Class 1, HK2, SERCA2a;
IsoId=P16615-2; Sequence=VSP_000358;
Note=Cardiac/slow twitch, muscle specific isoform. Has a lower
affinity for calcium and a higher catalytic turnover rate.;
Name=3; Synonyms=SERCA2C;
IsoId=P16615-3; Sequence=VSP_039393;
Note=May be due to intron retention. Shows a lower apparent
affinity for cytosolic calcium than isoform 2 and a catalytic
turnover rate similar to isoform 1.;
Name=4;
IsoId=P16615-4; Sequence=VSP_039392;
Note=No experimental confirmation available.;
Name=5;
IsoId=P16615-5; Sequence=VSP_039394;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed in smooth muscle
and nonmuscle tissues such as in adult skin epidermis, with
highest expression in liver, pancreas and lung, and intermediate
expression in brain, kidney and placenta. Also expressed at lower
levels in heart and skeletal muscle. Isoforms 2 and 3 are highly
expressed in the heart and slow twitch skeletal muscle. Expression
of isoform 3 is predominantly restricted to cardiomyocytes and in
close proximity to the sarcolemma. Both isoforms are mildly
expressed in lung, kidney, liver, pancreas and placenta.
Expression of isoform 3 is amplified during monocytic
differentiation and also observed in the fetal heart.
{ECO:0000269|PubMed:10441324, ECO:0000269|PubMed:12659872,
ECO:0000269|PubMed:16402920}.
-!- PTM: Nitrated under oxidative stress. Nitration on the two
tyrosine residues inhibits catalytic activity.
{ECO:0000269|PubMed:16399855}.
-!- DISEASE: Acrokeratosis verruciformis (AKV) [MIM:101900]: A
localized disorder of keratinization, which is inherited as an
autosomal dominant trait. Its onset is early in life with multiple
flat-topped, flesh-colored papules on the hands and feet, punctate
keratoses on the palms and soles, with varying degrees of nail
involvement. The histopathology shows a distinctive pattern of
epidermal features with hyperkeratosis, hypergranulosis and
acanthosis together with papillomatosis. These changes are
frequently associated with circumscribed elevations of the
epidermis that are said to resemble church spires. There are no
features of dyskeratosis or acantholysis, the typical findings in
lesions of Darier disease. {ECO:0000269|PubMed:12542527}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Darier disease (DD) [MIM:124200]: A skin disorder
characterized by warty papules and plaques in seborrheic areas
(central trunk, flexures, scalp and forehead), palmoplantar pits
and distinctive nail abnormalities. It is due to loss of adhesion
between epidermal cells (acantholysis) and abnormal
keratinization. Patients with mild disease may have no more than a
few scattered keratotic papules or subtle nail changes, whereas
those with severe disease are handicapped by widespread malodorous
keratotic plaques. Some patients present with hemorrhage into
acantholytic vesicles on the palms and dorsal aspects of the
fingers which gives rise to black macules. In a few families
affected by Darier disease, neuropsychiatric abnormalities such as
mild mental retardation, schizophrenia, bipolar disorder and
epilepsy have been reported. Stress, UV exposure, heat, sweat,
friction and oral contraception exacerbate disease symptoms.
Clinical variants of Darier disease include hypertrophic,
vesicobullous, hypopigmented, cornifying, zosteriform or linear,
acute and comedonal subtypes. Comedonal Darier disease is
characterized by the coexistence of acne-like comedonal lesions
with typical Darier hyperkeratotic papules on light-exposed areas.
At histopathologic level, comedonal Darier disease differs from
classic Darier disease in the prominent follicular involvement and
the presence of greatly elongated dermal villi.
{ECO:0000269|PubMed:10080178, ECO:0000269|PubMed:10441323,
ECO:0000269|PubMed:10441324, ECO:0000269|PubMed:10441325,
ECO:0000269|PubMed:19995371}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIA subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG57266.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M23114; AAA53193.1; -; mRNA.
EMBL; M23116; AAA52757.1; -; Genomic_DNA.
EMBL; M23115; AAA53194.1; -; mRNA.
EMBL; M23278; AAA52758.1; -; Genomic_DNA.
EMBL; M23116; AAA52758.1; JOINED; Genomic_DNA.
EMBL; AC006088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035588; AAH35588.1; -; mRNA.
EMBL; AK293877; BAG57266.1; ALT_INIT; mRNA.
EMBL; AY186578; AAO47398.1; -; mRNA.
CCDS; CCDS9143.1; -. [P16615-2]
CCDS; CCDS9144.1; -. [P16615-1]
PIR; A31981; A31981.
PIR; B31981; B31981.
RefSeq; NP_001672.1; NM_001681.3. [P16615-2]
RefSeq; NP_733765.1; NM_170665.3. [P16615-1]
RefSeq; XP_005253945.1; XM_005253888.2. [P16615-3]
RefSeq; XP_011536704.1; XM_011538402.2. [P16615-3]
UniGene; Hs.506759; -.
ProteinModelPortal; P16615; -.
SMR; P16615; -.
BioGrid; 106978; 79.
CORUM; P16615; -.
DIP; DIP-33868N; -.
IntAct; P16615; 72.
MINT; MINT-4991144; -.
STRING; 9606.ENSP00000440045; -.
ChEMBL; CHEMBL3901; -.
TCDB; 3.A.3.2.7; the p-type atpase (p-atpase) superfamily.
iPTMnet; P16615; -.
PhosphoSitePlus; P16615; -.
SwissPalm; P16615; -.
BioMuta; ATP2A2; -.
DMDM; 114312; -.
EPD; P16615; -.
MaxQB; P16615; -.
PaxDb; P16615; -.
PeptideAtlas; P16615; -.
PRIDE; P16615; -.
Ensembl; ENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
Ensembl; ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
GeneID; 488; -.
KEGG; hsa:488; -.
UCSC; uc001tqk.5; human. [P16615-1]
CTD; 488; -.
DisGeNET; 488; -.
EuPathDB; HostDB:ENSG00000174437.16; -.
GeneCards; ATP2A2; -.
HGNC; HGNC:812; ATP2A2.
HPA; HPA062605; -.
HPA; HPA067892; -.
MalaCards; ATP2A2; -.
MIM; 101900; phenotype.
MIM; 108740; gene.
MIM; 124200; phenotype.
neXtProt; NX_P16615; -.
OpenTargets; ENSG00000174437; -.
Orphanet; 79151; Acrokeratosis verruciformis of Hopf.
Orphanet; 218; Darier disease.
PharmGKB; PA71; -.
eggNOG; KOG0202; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265621; -.
HOVERGEN; HBG105648; -.
InParanoid; P16615; -.
KO; K05853; -.
OMA; YNNTQQF; -.
OrthoDB; EOG091G01LE; -.
PhylomeDB; P16615; -.
TreeFam; TF300651; -.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SignaLink; P16615; -.
SIGNOR; P16615; -.
ChiTaRS; ATP2A2; human.
GenomeRNAi; 488; -.
PRO; PR:P16615; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000174437; -.
CleanEx; HS_ATP2A2; -.
ExpressionAtlas; P16615; baseline and differential.
Genevisible; P16615; HS.
GO; GO:0090534; C:calcium ion-transporting ATPase complex; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0014801; C:longitudinal sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0097470; C:ribbon synapse; IEA:Ensembl.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; TAS:BHF-UCL.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:BHF-UCL.
GO; GO:0086039; F:calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential; ISS:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031775; F:lutropin-choriogonadotropic hormone receptor binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IDA:BHF-UCL.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0006984; P:ER-nucleus signaling pathway; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0006996; P:organelle organization; IEA:Ensembl.
GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IDA:BHF-UCL.
GO; GO:0010460; P:positive regulation of heart rate; TAS:BHF-UCL.
GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; IEA:Ensembl.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISS:BHF-UCL.
GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; ISS:BHF-UCL.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IDA:BHF-UCL.
GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0055119; P:relaxation of cardiac muscle; IDA:BHF-UCL.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:ParkinsonsUK-UCL.
GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; TAS:BHF-UCL.
GO; GO:0033292; P:T-tubule organization; IEA:Ensembl.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005782; P-type_ATPase_IIA.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Calcium transport;
Complete proteome; Disease mutation; Endoplasmic reticulum; Epilepsy;
Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1042 Sarcoplasmic/endoplasmic reticulum
calcium ATPase 2.
/FTId=PRO_0000046196.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.
TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 70 89 Lumenal. {ECO:0000250}.
TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.
TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 274 295 Lumenal. {ECO:0000250}.
TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 314 756 Cytoplasmic. {ECO:0000250}.
TRANSMEM 757 776 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 777 786 Lumenal. {ECO:0000250}.
TRANSMEM 787 807 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 808 827 Cytoplasmic. {ECO:0000250}.
TRANSMEM 828 850 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 851 896 Lumenal. {ECO:0000250}.
TRANSMEM 897 916 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 917 929 Cytoplasmic. {ECO:0000250}.
TRANSMEM 930 948 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 949 963 Lumenal. {ECO:0000250}.
TRANSMEM 964 984 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 985 1042 Cytoplasmic. {ECO:0000250}.
REGION 370 400 Interaction with phospholamban 1.
{ECO:0000250|UniProtKB:P04191}.
REGION 575 594 Interaction with HAX1.
{ECO:0000269|PubMed:18971376}.
REGION 787 807 Interaction with phospholamban 2.
{ECO:0000250|UniProtKB:P04191}.
REGION 788 1042 Interaction with TMEM64 and PDIA3.
{ECO:0000250|UniProtKB:O55143}.
ACT_SITE 351 351 4-aspartylphosphate intermediate.
{ECO:0000250|UniProtKB:P04191}.
METAL 304 304 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 305 305 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 307 307 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 309 309 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 702 702 Magnesium. {ECO:0000250}.
METAL 706 706 Magnesium. {ECO:0000250}.
METAL 767 767 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 770 770 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 795 795 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 798 798 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 907 907 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:O55143}.
MOD_RES 294 294 Nitrated tyrosine.
{ECO:0000269|PubMed:16399855}.
MOD_RES 295 295 Nitrated tyrosine.
{ECO:0000269|PubMed:16399855}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64578}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000250|UniProtKB:O55143}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 663 663 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 155 181 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039392.
VAR_SEQ 994 1042 GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDT
NFSDMFWS -> AILE (in isoform 2).
{ECO:0000303|PubMed:2844796}.
/FTId=VSP_000358.
VAR_SEQ 994 1042 GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDT
NFSDMFWS -> VLSSEL (in isoform 3).
{ECO:0000303|PubMed:12659872}.
/FTId=VSP_039393.
VAR_SEQ 994 1042 GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDT
NFSDMFWS -> DIIK (in isoform 5).
{ECO:0000305}.
/FTId=VSP_039394.
VARIANT 23 23 G -> E (in DD; dbSNP:rs28929478).
{ECO:0000269|PubMed:10080178}.
/FTId=VAR_008608.
VARIANT 39 39 N -> T (in DD).
{ECO:0000269|PubMed:10441325}.
/FTId=VAR_008609.
VARIANT 41 41 Missing (in DD; comedonal type).
{ECO:0000269|PubMed:19995371}.
/FTId=VAR_063398.
VARIANT 47 47 K -> KMFLTGK (in DD).
/FTId=VAR_008610.
VARIANT 65 65 L -> S (in DD; severe form).
/FTId=VAR_008611.
VARIANT 131 131 R -> Q (in DD; dbSNP:rs121912738).
/FTId=VAR_008612.
VARIANT 160 160 P -> L (in DD).
/FTId=VAR_008613.
VARIANT 186 186 S -> P (in DD).
/FTId=VAR_008614.
VARIANT 211 211 G -> D (in DD; severe form).
/FTId=VAR_008615.
VARIANT 223 223 V -> M (in DD).
/FTId=VAR_008616.
VARIANT 268 268 C -> F (in DD; haemorrhagic lesions;
dbSNP:rs121912733).
/FTId=VAR_008617.
VARIANT 310 310 G -> V (in DD).
/FTId=VAR_008618.
VARIANT 318 318 C -> R (in DD; severe form).
/FTId=VAR_008619.
VARIANT 348 348 I -> T (in DD).
/FTId=VAR_008620.
VARIANT 357 357 T -> K (in DD).
{ECO:0000269|PubMed:10080178}.
/FTId=VAR_009508.
VARIANT 412 412 E -> G (in DD).
/FTId=VAR_008621.
VARIANT 495 495 S -> F (in DD).
{ECO:0000269|PubMed:10080178}.
/FTId=VAR_008622.
VARIANT 560 560 C -> R (in DD; neuropsychiatric
phenotype; dbSNP:rs121912734).
{ECO:0000269|PubMed:10441325}.
/FTId=VAR_008623.
VARIANT 602 602 P -> L (in AKV; loss of activity;
dbSNP:rs121912737).
{ECO:0000269|PubMed:12542527}.
/FTId=VAR_017532.
VARIANT 675 675 F -> S (in DD; multiple neuropsychiatric
features).
/FTId=VAR_008624.
VARIANT 683 683 K -> E (in DD; depression).
/FTId=VAR_008625.
VARIANT 702 702 D -> N (in DD; moderate form).
/FTId=VAR_008626.
VARIANT 745 745 A -> D (in DD; moderate form).
/FTId=VAR_008627.
VARIANT 749 749 G -> R (in DD).
{ECO:0000269|PubMed:10080178}.
/FTId=VAR_009509.
VARIANT 754 754 Missing (in DD).
/FTId=VAR_008628.
VARIANT 765 765 S -> L (in DD).
{ECO:0000269|PubMed:10441325}.
/FTId=VAR_008629.
VARIANT 767 767 N -> S (in DD; haemorrhagic lesions and
neuropsychiatric phenotype;
dbSNP:rs121912732).
/FTId=VAR_008630.
VARIANT 769 769 G -> R (in DD; dbSNP:rs121912736).
/FTId=VAR_008631.
VARIANT 803 803 A -> T (in DD; mild/moderate form).
/FTId=VAR_008632.
VARIANT 838 838 A -> P (in DD; severe form; petit mal
epilepsy).
/FTId=VAR_008633.
VARIANT 843 843 V -> F (in DD; depression).
/FTId=VAR_008634.
VARIANT 875 875 C -> G (in DD; retinitis pigmentosa).
/FTId=VAR_008635.
VARIANT 920 920 S -> Y (in DD; mild/moderate/severe form;
one patient with epilepsy).
/FTId=VAR_008636.
VARIANT 943 943 H -> R (in DD; learning difficulties).
/FTId=VAR_008637.
VARIANT 975 975 P -> R (in DD).
/FTId=VAR_008638.
SEQUENCE 1042 AA; 114757 MW; 5462FF2DA7FB630A CRC64;
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVNCHQYDGL VELATICALC
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV
KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL
NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP
LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL
LIMPLVIWVY STDTNFSDMF WS


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