ID   KAP0_MOUSE              Reviewed;         381 AA.
AC   Q9DBC7; Q3UKU7; Q9JHR5; Q9JHR6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
DE   Contains:
DE     RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed;
GN   Name=Prkar1a;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, Liver, and Placenta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
RX   PubMed=10913627; DOI=10.1016/s0014-5793(00)01653-7;
RA   Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M.;
RT   "Alternative 5'-exons of the mouse cAMP-dependent protein kinase subunit
RT   RIalpha gene are conserved and expressed in both a ubiquitous and tissue-
RT   restricted fashion.";
RL   FEBS Lett. 476:272-276(2000).
RN   [4]
RP   INTERACTION WITH AKAP4.
RX   PubMed=9852104; DOI=10.1074/jbc.273.51.34384;
RA   Miki K., Eddy E.M.;
RT   "Identification of tethering domains for protein kinase A type Ialpha
RT   regulatory subunits on sperm fibrous sheath protein FSC1.";
RL   J. Biol. Chem. 273:34384-34390(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [10]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=20138877; DOI=10.1016/j.febslet.2010.02.007;
RA   Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.;
RT   "Myeloid translocation gene 16b is a dual A-kinase anchoring protein that
RT   interacts selectively with plexins in a phospho-regulated manner.";
RL   FEBS Lett. 584:873-877(2010).
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. {ECO:0000250}.
CC   -!- SUBUNIT: The inactive holoenzyme is composed of two regulatory chains
CC       and two catalytic chains. Activation by cAMP releases the two active
CC       catalytic monomers and the regulatory dimer. Interacts with PRKACA and
CC       PRKACB (By similarity). PRKAR1A also interacts with RFC2; the complex
CC       may be involved in cell survival. Interacts with AKAP4
CC       (PubMed:9852104). Interacts with RARA; the interaction occurs in the
CC       presence of cAMP or FSH and regulates RARA transcriptional activity.
CC       Interacts with the phosphorylated form of PJA2. Interacts with PRKX;
CC       regulates this cAMP-dependent protein kinase (By similarity). Interacts
CC       with CBFA2T3 (PubMed:20138877). Interacts with smAKAP; this interaction
CC       may target PRKAR1A to the plasma membrane. Interacts with AICDA (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10644}.
CC   -!- INTERACTION:
CC       Q9DBC7; O54918-1: Bcl2l11; NbExp=2; IntAct=EBI-645677, EBI-526076;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC   -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC       region of the catalytic chain, resulting in the inhibition of its
CC       activity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Two types of regulatory chains are found: type I, which
CC       predominates in skeletal muscle, and type II, which predominates in
CC       cardiac muscle. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; AK005039; BAB23766.1; -; mRNA.
DR   EMBL; AK027916; BAC25664.1; -; mRNA.
DR   EMBL; AK051068; BAC34516.1; -; mRNA.
DR   EMBL; AK145797; BAE26655.1; -; mRNA.
DR   EMBL; AK145860; BAE26704.1; -; mRNA.
DR   EMBL; AK147188; BAE27748.1; -; mRNA.
DR   EMBL; AK150427; BAE29550.1; -; mRNA.
DR   EMBL; AK151124; BAE30132.1; -; mRNA.
DR   EMBL; AK153227; BAE31820.1; -; mRNA.
DR   EMBL; BC003461; AAH03461.1; -; mRNA.
DR   EMBL; BC005697; AAH05697.1; -; mRNA.
DR   EMBL; AJ278427; CAB94778.1; -; Genomic_DNA.
DR   EMBL; AJ278429; CAB94718.1; -; Genomic_DNA.
DR   CCDS; CCDS25583.1; -.
DR   RefSeq; NP_001300902.1; NM_001313973.1.
DR   RefSeq; NP_001300903.1; NM_001313974.1.
DR   RefSeq; NP_001300904.1; NM_001313975.1.
DR   RefSeq; NP_001300905.1; NM_001313976.1.
DR   RefSeq; NP_068680.1; NM_021880.3.
DR   RefSeq; XP_017169829.1; XM_017314340.1.
DR   AlphaFoldDB; Q9DBC7; -.
DR   SMR; Q9DBC7; -.
DR   BioGRID; 202365; 10.
DR   DIP; DIP-32450N; -.
DR   IntAct; Q9DBC7; 15.
DR   MINT; Q9DBC7; -.
DR   STRING; 10090.ENSMUSP00000102288; -.
DR   GlyGen; Q9DBC7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DBC7; -.
DR   PhosphoSitePlus; Q9DBC7; -.
DR   SwissPalm; Q9DBC7; -.
DR   REPRODUCTION-2DPAGE; IPI00762049; -.
DR   REPRODUCTION-2DPAGE; Q9DBC7; -.
DR   EPD; Q9DBC7; -.
DR   jPOST; Q9DBC7; -.
DR   MaxQB; Q9DBC7; -.
DR   PaxDb; 10090-ENSMUSP00000056500; -.
DR   ProteomicsDB; 268956; -.
DR   Pumba; Q9DBC7; -.
DR   Antibodypedia; 31783; 422 antibodies from 35 providers.
DR   DNASU; 19084; -.
DR   Ensembl; ENSMUST00000049527.7; ENSMUSP00000056500.7; ENSMUSG00000020612.17.
DR   Ensembl; ENSMUST00000106677.8; ENSMUSP00000102288.2; ENSMUSG00000020612.17.
DR   GeneID; 19084; -.
DR   KEGG; mmu:19084; -.
DR   UCSC; uc007mcu.1; mouse.
DR   AGR; MGI:104878; -.
DR   CTD; 5573; -.
DR   MGI; MGI:104878; Prkar1a.
DR   VEuPathDB; HostDB:ENSMUSG00000020612; -.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000155148; -.
DR   HOGENOM; CLU_018310_1_0_1; -.
DR   InParanoid; Q9DBC7; -.
DR   OMA; DQWERAN; -.
DR   OrthoDB; 55978at2759; -.
DR   PhylomeDB; Q9DBC7; -.
DR   TreeFam; TF314920; -.
DR   Reactome; R-MMU-163615; PKA activation.
DR   Reactome; R-MMU-164378; PKA activation in glucagon signalling.
DR   Reactome; R-MMU-180024; DARPP-32 events.
DR   Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-MMU-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR   Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR   Reactome; R-MMU-9634597; GPER1 signaling.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 19084; 20 hits in 82 CRISPR screens.
DR   ChiTaRS; Prkar1a; mouse.
DR   PRO; PR:Q9DBC7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9DBC7; Protein.
DR   Bgee; ENSMUSG00000020612; Expressed in subparaventricular zone and 291 other cell types or tissues.
DR   ExpressionAtlas; Q9DBC7; baseline and differential.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR   GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI.
DR   GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0097224; C:sperm connecting piece; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0030552; F:cAMP binding; ISO:MGI.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IMP:MGI.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR   GO; GO:0071377; P:cellular response to glucagon stimulus; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0010463; P:mesenchymal cell proliferation; TAS:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12101; DD_RIalpha_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF129; CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   Genevisible; Q9DBC7; MM.
PE   1: Evidence at protein level;
KW   Acetylation; cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..381
FT                   /note="cAMP-dependent protein kinase type I-alpha
FT                   regulatory subunit"
FT                   /id="PRO_0000421786"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00514"
FT   CHAIN           2..381
FT                   /note="cAMP-dependent protein kinase type I-alpha
FT                   regulatory subunit, N-terminally processed"
FT                   /id="PRO_0000205378"
FT   REGION          2..136
FT                   /note="Dimerization and phosphorylation"
FT   REGION          73..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..100
FT                   /note="Pseudophosphorylation motif"
FT   BINDING         137..254
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         202
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         211
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT   BINDING         255..381
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         326
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   BINDING         335
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P10644"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; in cAMP-dependent protein kinase
FT                   type I-alpha regulatory subunit, N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P00514"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09456"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10644"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10644"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09456"
FT   DISULFID        18
FT                   /note="Interchain (with C-39)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        39
FT                   /note="Interchain (with C-18)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  43185 MW;  08F164BB4528C63B CRC64;
     MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL REYFERLEKE
     EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
     DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG
     EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
     RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
     AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
     PCSDILKRNI QQYNSFVSLS V
//