KAPCB_MOUSE
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 03-AUG-2022, entry version 171.
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. PKA activation regulates diverse cellular processes
CC such as cell proliferation, the cell cycle, differentiation and
CC regulation of microtubule dynamics, chromatin condensation and
CC decondensation, nuclear envelope disassembly and reassembly, as well as
CC regulation of intracellular transport mechanisms and ion flux
CC (PubMed:9368018). Regulates the abundance of compartmentalized pools of
CC its regulatory subunits through phosphorylation of PJA2 which binds and
CC ubiquitinates these subunits, leading to their subsequent proteolysis.
CC Phosphorylates GPKOW which regulates its ability to bind RNA (By
CC 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}. Cell membrane
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250}.
CC Note=Translocates into the nucleus (monomeric catalytic subunit). The
CC inactive holoenzyme is found in the cytoplasm. {ECO:0000250}.
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 deaminated to Asp in more than 25% of the proteins,
CC giving rise to 2 major isoelectric variants, called CB and CA
CC respectively (0.4 pH unit change). Deamidation proceeds via the so-
CC called beta-aspartyl shift mechanism and yields either 'D-Asp-2'
CC (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation
CC occurs after the addition of myristate. The Asn-3 form reaches a
CC significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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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; 47.
DR CORUM; P68181; -.
DR IntAct; P68181; 38.
DR MINT; P68181; -.
DR STRING; 10090.ENSMUSP00000005164; -.
DR iPTMnet; P68181; -.
DR PhosphoSitePlus; P68181; -.
DR SwissPalm; P68181; -.
DR EPD; P68181; -.
DR jPOST; P68181; -.
DR MaxQB; P68181; -.
DR PaxDb; P68181; -.
DR PeptideAtlas; P68181; -.
DR PRIDE; P68181; -.
DR ProteomicsDB; 263389; -. [P68181-1]
DR ProteomicsDB; 263390; -. [P68181-2]
DR ProteomicsDB; 263391; -. [P68181-3]
DR ProteomicsDB; 263392; -. [P68181-4]
DR Antibodypedia; 4160; 420 antibodies from 36 providers.
DR DNASU; 18749; -.
DR Ensembl; ENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034. [P68181-4]
DR Ensembl; ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034. [P68181-1]
DR Ensembl; ENSMUST00000106137; ENSMUSP00000101743; ENSMUSG00000005034. [P68181-2]
DR Ensembl; ENSMUST00000106138; ENSMUSP00000101744; ENSMUSG00000005034. [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 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; GNARYNK; -.
DR OrthoDB; 963519at2759; -.
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 77 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 274 other tissues.
DR ExpressionAtlas; P68181; baseline and differential.
DR Genevisible; P68181; MM.
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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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"
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
