ID KAPCB_MOUSE Reviewed; 351 AA. AC P68181; P05206; Q3TQH5; Q3UDD0; Q3UTH5; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 180. DE RecName: Full=cAMP-dependent protein kinase catalytic subunit beta; DE Short=PKA C-beta; DE EC=2.7.11.11; GN Name=Prkacb; Synonyms=Pkacb; 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 [MRNA] (ISOFORM 1). RX PubMed=3023318; DOI=10.1016/s0021-9258(18)66717-1; RA Uhler M.D., Chrivia J.C., McKnight G.S.; RT "Evidence for a second isoform of the catalytic subunit of cAMP-dependent RT protein kinase."; RL J. Biol. Chem. 261:15360-15363(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Head; 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] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15 (ISOFORM 1). RX PubMed=2833513; DOI=10.1016/s0021-9258(18)60627-1; RA Chrivia J.C., Uhler M.D., McKnight G.S.; RT "Characterization of genomic clones coding for the C alpha and C beta RT subunits of mouse cAMP-dependent protein kinase."; RL J. Biol. Chem. 263:5739-5744(1988). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7 (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 1-8 (ISOFORM 3), FUNCTION, MYRISTOYLATION AT GLY-2, AND RP TISSUE SPECIFICITY. RX PubMed=9368018; DOI=10.1074/jbc.272.47.29560; RA Guthrie C.R., Skalhegg B.S., McKnight G.S.; RT "Two novel brain-specific splice variants of the murine Cbeta gene of cAMP- RT dependent protein kinase."; RL J. Biol. Chem. 272:29560-29565(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-351. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x; RA Kato K.; RT "A collection of cDNA clones with specific expression patterns in mouse RT brain."; RL Eur. J. Neurosci. 2:704-711(1990). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and RC 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). CC -!- FUNCTION: Mediates cAMP-dependent signaling triggered by receptor CC binding to GPCRs (By similarity). PKA activation regulates diverse CC cellular processes such as cell proliferation, the cell cycle, CC differentiation and regulation of microtubule dynamics, chromatin CC condensation and decondensation, nuclear envelope disassembly and CC reassembly, as well as regulation of intracellular transport mechanisms CC and ion flux (PubMed:9368018). Regulates the abundance of CC compartmentalized pools of its regulatory subunits through CC phosphorylation of PJA2 which binds and ubiquitinates these subunits, CC leading to their subsequent proteolysis (By similarity). Phosphorylates CC GPKOW which regulates its ability to bind RNA (By similarity). Acts as CC a negative regulator of mTORC1 by mediating phosphorylation of RPTOR CC (By similarity). {ECO:0000250|UniProtKB:P22694, CC ECO:0000269|PubMed:9368018}. 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=2.7.11.11; 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=2.7.11.11; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY REGULATION: Activated by cAMP. {ECO:0000250|UniProtKB:P22694}. CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by CC the combination of homo- or heterodimers of the different regulatory CC subunits associated with two catalytic subunits. cAMP causes the CC dissociation of the inactive holoenzyme into a dimer of regulatory CC subunits bound to four cAMP and two free monomeric catalytic subunits. CC Interacts with PRKAR1A and PRKAR2B (By similarity). The cAMP-dependent CC protein kinase catalytic subunit binds PJA2. Interacts with GPKOW. CC {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P22694}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22694}. Cell CC membrane {ECO:0000250|UniProtKB:P22694}. Membrane CC {ECO:0000250|UniProtKB:P22694}; Lipid-anchor CC {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250|UniProtKB:P05131}. CC Note=Translocates into the nucleus (monomeric catalytic subunit). The CC inactive holoenzyme is found in the cytoplasm. CC {ECO:0000250|UniProtKB:P05131}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Beta1; CC IsoId=P68181-1; Sequence=Displayed; CC Name=2; Synonyms=Beta2; CC IsoId=P68181-2; Sequence=VSP_017373, VSP_017374; CC Name=3; Synonyms=Beta3; CC IsoId=P68181-3; Sequence=VSP_017372, VSP_017375; CC Name=4; CC IsoId=P68181-4; Sequence=VSP_017376; CC -!- TISSUE SPECIFICITY: Isoform 1 is found in all tissues examined, with CC the highest expression in the brain and very low levels in the testis. CC Isoform 2 is strongly expressed in the brain, in the prelimbic and CC insular cortex. Isoform 3 is also found only in the brain, but at very CC low levels. {ECO:0000269|PubMed:9368018}. CC -!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major CC isoelectric variants, called CB and CA respectively. CC {ECO:0000250|UniProtKB:P05383}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cAMP subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02626; AAA39941.1; -; mRNA. DR EMBL; AK048319; BAC33301.1; -; mRNA. DR EMBL; AK139419; BAE24005.1; -; mRNA. DR EMBL; AK148728; BAE28648.1; -; mRNA. DR EMBL; AK150122; BAE29323.1; -; mRNA. DR EMBL; AK150134; BAE29331.1; -; mRNA. DR EMBL; AK163585; BAE37407.1; -; mRNA. DR EMBL; BC054533; AAH54533.1; -; mRNA. DR EMBL; M21096; AAA39938.1; -; Genomic_DNA. DR EMBL; AF022239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X61434; CAA43676.1; -; mRNA. DR CCDS; CCDS17906.1; -. [P68181-1] DR CCDS; CCDS51090.1; -. [P68181-2] DR CCDS; CCDS51091.1; -. [P68181-3] DR CCDS; CCDS51092.1; -. [P68181-4] DR PIR; A24596; OKMSCB. DR RefSeq; NP_001157670.1; NM_001164198.1. [P68181-2] DR RefSeq; NP_001157671.1; NM_001164199.1. [P68181-3] DR RefSeq; NP_001157672.1; NM_001164200.1. [P68181-4] DR RefSeq; NP_035230.1; NM_011100.4. [P68181-1] DR AlphaFoldDB; P68181; -. DR SMR; P68181; -. DR BioGRID; 202193; 48. DR CORUM; P68181; -. DR IntAct; P68181; 38. DR MINT; P68181; -. DR STRING; 10090.ENSMUSP00000005164; -. DR GlyGen; P68181; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P68181; -. DR PhosphoSitePlus; P68181; -. DR SwissPalm; P68181; -. DR EPD; P68181; -. DR jPOST; P68181; -. DR MaxQB; P68181; -. DR PaxDb; 10090-ENSMUSP00000005164; -. DR PeptideAtlas; P68181; -. DR ProteomicsDB; 263389; -. [P68181-1] DR ProteomicsDB; 263390; -. [P68181-2] DR ProteomicsDB; 263391; -. [P68181-3] DR ProteomicsDB; 263392; -. [P68181-4] DR Pumba; P68181; -. DR Antibodypedia; 4160; 485 antibodies from 36 providers. DR DNASU; 18749; -. DR Ensembl; ENSMUST00000005164.12; ENSMUSP00000005164.8; ENSMUSG00000005034.16. [P68181-4] DR Ensembl; ENSMUST00000102515.10; ENSMUSP00000099573.4; ENSMUSG00000005034.16. [P68181-1] DR Ensembl; ENSMUST00000106137.8; ENSMUSP00000101743.2; ENSMUSG00000005034.16. [P68181-2] DR Ensembl; ENSMUST00000106138.8; ENSMUSP00000101744.2; ENSMUSG00000005034.16. [P68181-3] DR GeneID; 18749; -. DR KEGG; mmu:18749; -. DR UCSC; uc008rrs.2; mouse. [P68181-2] DR UCSC; uc008rrt.2; mouse. [P68181-3] DR UCSC; uc008rru.1; mouse. [P68181-4] DR UCSC; uc008rrv.2; mouse. [P68181-1] DR AGR; MGI:97594; -. DR CTD; 5567; -. DR MGI; MGI:97594; Prkacb. DR VEuPathDB; HostDB:ENSMUSG00000005034; -. DR eggNOG; KOG0616; Eukaryota. DR GeneTree; ENSGT00940000161169; -. DR HOGENOM; CLU_000288_63_5_1; -. DR InParanoid; P68181; -. DR OMA; FAKEVQD; -. DR OrthoDB; 10768at2759; -. DR PhylomeDB; P68181; -. DR TreeFam; TF313399; -. DR BRENDA; 2.7.11.11; 3474. 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-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-MMU-392517; Rap1 signalling. DR Reactome; R-MMU-422356; Regulation of insulin secretion. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-MMU-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase. DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-MMU-8853659; RET signaling. DR Reactome; R-MMU-8963896; HDL assembly. DR Reactome; R-MMU-9634597; GPER1 signaling. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 18749; 3 hits in 82 CRISPR screens. DR ChiTaRS; Prkacb; mouse. DR PRO; PR:P68181; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P68181; Protein. DR Bgee; ENSMUSG00000005034; Expressed in ventromedial nucleus of hypothalamus and 278 other cell types or tissues. DR ExpressionAtlas; P68181; baseline and differential. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; ISO:MGI. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0097546; C:ciliary base; IDA:MGI. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; ISO:MGI. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB. DR GO; GO:0001843; P:neural tube closure; IGI:MGI. DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0070613; P:regulation of protein processing; IGI:MGI. DR CDD; cd14209; STKc_PKA; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR044109; STKc_PKA. DR PANTHER; PTHR24353:SF116; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT BETA; 1. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P68181; MM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; cAMP; Cell membrane; Cytoplasm; Kinase; KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9368018" FT CHAIN 2..351 FT /note="cAMP-dependent protein kinase catalytic subunit FT beta" FT /id="PRO_0000086061" FT DOMAIN 44..298 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 299..351 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 50..58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 3 FT /note="Deamidated asparagine" FT /evidence="ECO:0000250|UniProtKB:P05383" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 69 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 198 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68182" FT MOD_RES 331 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68182" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:9368018" FT VAR_SEQ 1..16 FT /note="MGNTAIAKKGSEVESV -> MAAHKELSSGQHSGTPTALQKLEGFASRLFHR FT HSRGTAQEHRAALEDDGLRASEHTASWDKSM (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017376" FT VAR_SEQ 1..13 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017373" FT VAR_SEQ 1..12 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017372" FT VAR_SEQ 13..16 FT /note="VESV -> MGLL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017375" FT VAR_SEQ 14..15 FT /note="ES -> MN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017374" SQ SEQUENCE 351 AA; 40708 MW; EBAC9B8041DF9F47 CRC64; MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE FPFLVRLEYS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEEIRVSI TEKCGKEFCE F //