PASK_MOUSE
ID PASK_MOUSE Reviewed; 1383 AA.
AC Q8CEE6; E9QM58; Q91YD8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=PAS domain-containing serine/threonine-protein kinase;
DE Short=PAS-kinase;
DE Short=PASKIN;
DE EC=2.7.11.1;
GN Name=Pask; Synonyms=Kiaa0135;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11688972; DOI=10.1006/bbrc.2001.5840;
RA Hofer T., Spielmann P., Stengel P., Stier B., Katschinski D.M.,
RA Desbaillets I., Gassmann M., Wenger R.H.;
RT "Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial
RT oxygen sensors.";
RL Biochem. Biophys. Res. Commun. 288:757-764(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12972598; DOI=10.1128/mcb.23.19.6780-6789.2003;
RA Katschinski D.M., Marti H.H., Wagner K.F., Shibata J., Eckhardt K.,
RA Martin F., Depping R., Paasch U., Gassmann M., Ledermann B.,
RA Desbaillets I., Wenger R.H.;
RT "Targeted disruption of the mouse PAS domain serine/threonine kinase
RT PASKIN.";
RL Mol. Cell. Biol. 23:6780-6789(2003).
RN [6]
RP FUNCTION.
RX PubMed=15148392; DOI=10.1073/pnas.0307737101;
RA da Silva Xavier G., Rutter J., Rutter G.A.;
RT "Involvement of Per-Arnt-Sim (PAS) kinase in the stimulation of
RT preproinsulin and pancreatic duodenum homeobox 1 gene expression by
RT glucose.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8319-8324(2004).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17192472; DOI=10.2337/db06-0798;
RA Borter E., Niessen M., Zuellig R., Spinas G.A., Spielmann P., Camenisch G.,
RA Wenger R.H.;
RT "Glucose-stimulated insulin production in mice deficient for the PAS kinase
RT PASKIN.";
RL Diabetes 56:113-117(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17878307; DOI=10.1073/pnas.0705407104;
RA Hao H.X., Cardon C.M., Swiatek W., Cooksey R.C., Smith T.L., Wilde J.,
RA Boudina S., Abel E.D., McClain D.A., Rutter J.;
RT "PAS kinase is required for normal cellular energy balance.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15466-15471(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18509100; DOI=10.1152/ajpregu.00876.2007;
RA Soliz J., Soulage C., Borter E., van Patot M.T., Gassmann M.;
RT "Ventilatory responses to acute and chronic hypoxia are altered in female
RT but not male Paskin-deficient mice.";
RL Am. J. Physiol. 295:R649-R658(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND THR-31, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=21181396; DOI=10.1007/s00125-010-2010-7;
RA da Silva Xavier G., Farhan H., Kim H., Caxaria S., Johnson P., Hughes S.,
RA Bugliani M., Marselli L., Marchetti P., Birzele F., Sun G., Scharfmann R.,
RA Rutter J., Siniakowicz K., Weir G., Parker H., Reimann F., Gribble F.M.,
RA Rutter G.A.;
RT "Per-arnt-sim (PAS) domain-containing protein kinase is downregulated in
RT human islets in type 2 diabetes and regulates glucagon secretion.";
RL Diabetologia 54:819-827(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in energy
CC homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1
CC and RPS6. Probably plays a role under changing environmental conditions
CC (oxygen, glucose, nutrition), rather than under standard conditions.
CC Acts as a sensor involved in energy homeostasis: regulates glycogen
CC synthase synthesis by mediating phosphorylation of GYS1, leading to
CC GYS1 inactivation. May be involved in glucose-stimulated insulin
CC production in pancreas and regulation of glucagon secretion by glucose
CC in alpha cells; however such data require additional evidences. May
CC play a role in regulation of protein translation by phosphorylating
CC EEF1A1, leading to increase translation efficiency. May also
CC participate in respiratory regulation. {ECO:0000269|PubMed:15148392,
CC ECO:0000269|PubMed:17878307, ECO:0000269|PubMed:18509100,
CC ECO:0000269|PubMed:21181396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Protein kinase activity is inhibited by the first
CC PAS domain: binding of an unidentified ligand desinhibits the protein
CC kinase activity. May be activated by autophosphorylation on Thr-1221
CC and Thr-1225. Autophosphorylation is enhanced upon phosphatidylinositol
CC monophosphate (phosphatidylinositol 4-phosphate) binding and inhibited
CC upon phosphatidylinositol bi- and tri-phosphate binding. In contrast,
CC phosphorylation of target proteins is inhibited upon all
CC phosphatidylinositol-binding (phosphatidylinositol mono- bi- and tri-
CC phosphate) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Localizes in the nucleus of testis germ cells and in the midpiece
CC of sperm tails. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strongly up-regulated in
CC postmeiotic germ cells during spermatogenesis.
CC {ECO:0000269|PubMed:12972598}.
CC -!- DOMAIN: The protein kinase domain mediates binding to
CC phosphatidylinositol. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on Thr-1221 and Thr-1225. Autophosphorylation
CC is activated by phospholipids (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal conditions:
CC mice show normal development, growth and reproduction. Fertility and
CC sperm production and motility are not affected in males. Under high-fat
CC diet, mice seem to be protected from deleterious effects, including
CC obesity, liver triglyceride accumulation and insulin resistance
CC (PubMed:17878307). In contrast, the lean phenotype appears only after
CC feeding a high-fat diet: under normal chow diet, body weight, fat
CC composition, oxygen consumption are not distinguishable from wild-type
CC mice (PubMed:17192472). The only difference between these 2 experiments
CC is that mice were backcrossed into C57BL/6 5 times in the first study
CC (PubMed:17878307), while the 10th backcross was used in the second
CC study (PubMed:17192472). Female but not male mice show an increased
CC ventilatory response to acute hypoxia and fail to reach ventilatory
CC acclimatization to chronic hypoxia. {ECO:0000269|PubMed:12972598,
CC ECO:0000269|PubMed:17192472, ECO:0000269|PubMed:17878307,
CC ECO:0000269|PubMed:18509100}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ318757; CAC45054.2; -; Genomic_DNA.
DR EMBL; AK028435; BAC25951.1; -; mRNA.
DR EMBL; AK129063; BAC97873.1; -; mRNA.
DR EMBL; AC124669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15186.1; -.
DR RefSeq; NP_543126.2; NM_080850.2.
DR RefSeq; XP_006529728.1; XM_006529665.3.
DR RefSeq; XP_006529729.1; XM_006529666.2.
DR RefSeq; XP_006529730.1; XM_006529667.2.
DR RefSeq; XP_017176526.1; XM_017321037.1.
DR AlphaFoldDB; Q8CEE6; -.
DR SMR; Q8CEE6; -.
DR BioGRID; 234624; 6.
DR STRING; 10090.ENSMUSP00000027493; -.
DR iPTMnet; Q8CEE6; -.
DR PhosphoSitePlus; Q8CEE6; -.
DR EPD; Q8CEE6; -.
DR jPOST; Q8CEE6; -.
DR MaxQB; Q8CEE6; -.
DR PaxDb; Q8CEE6; -.
DR PRIDE; Q8CEE6; -.
DR ProteomicsDB; 288066; -.
DR Antibodypedia; 20301; 220 antibodies from 29 providers.
DR DNASU; 269224; -.
DR Ensembl; ENSMUST00000027493; ENSMUSP00000027493; ENSMUSG00000026274.
DR GeneID; 269224; -.
DR KEGG; mmu:269224; -.
DR UCSC; uc007cdt.2; mouse.
DR CTD; 23178; -.
DR MGI; MGI:2155936; Pask.
DR VEuPathDB; HostDB:ENSMUSG00000026274; -.
DR eggNOG; KOG1152; Eukaryota.
DR GeneTree; ENSGT00940000159035; -.
DR HOGENOM; CLU_006086_0_0_1; -.
DR InParanoid; Q8CEE6; -.
DR OMA; NPDLYFS; -.
DR OrthoDB; 297397at2759; -.
DR PhylomeDB; Q8CEE6; -.
DR TreeFam; TF323242; -.
DR BioGRID-ORCS; 269224; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Pask; mouse.
DR PRO; PR:Q8CEE6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CEE6; protein.
DR Bgee; ENSMUSG00000026274; Expressed in spermatocyte and 137 other tissues.
DR ExpressionAtlas; Q8CEE6; baseline and differential.
DR Genevisible; Q8CEE6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0070092; P:regulation of glucagon secretion; IMP:UniProtKB.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Kinase; Lipid-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1383
FT /note="PAS domain-containing serine/threonine-protein
FT kinase"
FT /id="PRO_0000086481"
FT DOMAIN 117..188
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 333..400
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 1059..1311
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1344..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1065..1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1088
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1142..1149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96RG2"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RG2"
FT MOD_RES 1221
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q96RG2"
FT MOD_RES 1225
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q96RG2"
FT CONFLICT 587
FT /note="S -> L (in Ref. 2; BAC25951)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="A -> V (in Ref. 1; CAC45054 and 3; BAC97873)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="H -> R (in Ref. 2; BAC25951)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="Q -> H (in Ref. 2; BAC25951)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296
FT /note="P -> L (in Ref. 1; CAC45054)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330
FT /note="Q -> H (in Ref. 2; BAC25951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1383 AA; 151250 MW; D020885E8C2C2E19 CRC64;
MEDRGPPVFA EDWKCLSESP PVQEGPAAQA TFEPSKPLSI AHKHLSRKNG LSRLCQSRMA
LSEDRWSSYC LSSLAAQNIC TSKLHCAAAP EYADPTAGPL GSTSCCSLLR GLASGCSGSL
LSTPVCNPNK AVFTVDAKTT EILVANDKAC SLLGYSSHDL IGQKLAQFFL KSDSEVVEAL
SEEHVEADGH AAVVFGTVVD IVSRIGEKIP VSVWIKRLQQ DRGLCCVVVL EPVERVSAWV
AFQSDGTITS CDSLFAHLHG FTSPKDVVGQ CVIDLIPSMQ LPPPGQHIPK SLKIQRSVGR
ARDGTTFPLS LKLKSKPSGR AVADSEAASE PGYQASVWVF CTISGLITLL PDGTIYGVNH
SFALMLFGYG KTELLGKNIT FLIPGFYHYM DLTYDSSVQL PDLVNCLDIG RKSGPGEMNS
DAQHNWELAS GAQGPRIDVV LARDHMPSQD ETLKLVGGQV SSRTQTRLET GYKILPSSAC
QPSLGVDSNP EDGEQSLLTD QQSIPKRNLP AHGGQNQLDT SEISLPVLKE HLLSEIQKNI
SEESPLTHRK WLSKVQQNPT KGSLPIHEEQ LLFAGQHIHV LGKEDPSAAE SYRESLLEES
KSKPVDAKLF ASCEDSEPLV SVKDRGSSVD TCNLHQEAQL ELMGVSSPNP WADATMPEPH
TTGQIAGGSL TYCPQYRSEW ASQQRGQDSA PSPSGMACVL LGTPTLDEPW PGVRNDREEL
QTCLIKEQLS KSSCEGNLGI SRVELVPEEH PPFTAPVSFC DLGGRDLHAS RSGSSSACYA
LATDLPGVLE AVEAQEADVN SYSWNLKELF LKDQTDRTPS HCSCTTSELS EAPSLSVVGS
DLDVGILHRQ TSDILVDREM LLLTGTYFDL SEGQRFQEMG AGHDRAELSN ISLVSSEHYE
TSDIESPGCD PPLPDPGPND MCLSAEKPRP SAQITSTPVA RGATSLQQEI QEGIYSGSCY
HRDGLQLSIQ FEVKRVELQG SATLFCCWLV KDLFHSHRDS ATRTRLFLAS LPSSTHSMPE
LSGSSFGEVL RAKPWFEESP TPAELEGLAA CEGEYDYKYN TISPLGSGAF GFVWTAVEKE
CNKEVVVKFI KKEKVLEDCW IEDPKLGRVT LEIAILSKVD HANIIKVLDI FENQEFFQLV
MEKHGSGMDL FAFIDHHPCL DEPLASFIFR QLVSAVGYLH SQGIIHRDIK DENIVIAEDF
TIKLIDFGSA AYLERGKLFY TFCGTIEYCA PEVLIGNPYR GPELEMWSLG VTLYTLIFEE
NPFCEVEETM EAVIHPPFLV SQELMSLLSG LLQPCPEQRT TLEKLIRDPW VTQPVNLASY
TWEEVCRTNQ PESGLLSAAS LEIGSRSPSE MAQREGLCGP PAPRETRGDQ HCLHLKDPSL
PVS
