AKAP1_MOUSE
ID AKAP1_MOUSE Reviewed; 857 AA.
AC O08715; B1AR25; O08714; P97488;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=A-kinase anchor protein 1, mitochondrial;
DE AltName: Full=Dual specificity A-kinase-anchoring protein 1;
DE Short=D-AKAP-1;
DE AltName: Full=Protein kinase A-anchoring protein 1;
DE Short=PRKA1;
DE AltName: Full=Spermatid A-kinase anchor protein;
DE Short=S-AKAP;
DE Flags: Precursor;
GN Name=Akap1 {ECO:0000312|MGI:MGI:104729}; Synonyms=Akap;
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] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=9065479; DOI=10.1074/jbc.272.12.8057;
RA Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.;
RT "Identification of a novel protein kinase A anchoring protein that binds
RT both type I and type II regulatory subunits.";
RL J. Biol. Chem. 272:8057-8064(1997).
RN [2]
RP SEQUENCE REVISION.
RA Huang L.J.-S., Durick K., Taylor S.S.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6), SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9182549; DOI=10.1074/jbc.272.24.15247;
RA Chen Q., Lin R.-Y., Rubin C.S.;
RT "Organelle-specific targeting of protein kinase AII (PKAII). Molecular and
RT in situ characterization of murine A kinase anchor proteins that recruit
RT regulatory subunits of PKAII to the cytoplasmic surface of mitochondria.";
RL J. Biol. Chem. 272:15247-15257(1997).
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 SUBCELLULAR LOCATION (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RX PubMed=10352013; DOI=10.1083/jcb.145.5.951;
RA Huang L.J.-S., Wang L., Ma Y., Durick K., Perkins G., Deerinck T.J.,
RA Ellisman M.H., Taylor S.S.;
RT "NH2-Terminal targeting motifs direct dual specificity A-kinase-anchoring
RT protein 1 (D-AKAP1) to either mitochondria or endoplasmic reticulum.";
RL J. Cell Biol. 145:951-959(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP 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-55; SER-101 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC8A3.
RX PubMed=24101730; DOI=10.1242/jcs.129668;
RA Scorziello A., Savoia C., Sisalli M.J., Adornetto A., Secondo A.,
RA Boscia F., Esposito A., Polishchuk E.V., Polishchuk R.S., Molinaro P.,
RA Carlucci A., Lignitto L., Di Renzo G., Feliciello A., Annunziato L.;
RT "NCX3 regulates mitochondrial Ca(2+) handling through the AKAP121-anchored
RT signaling complex and prevents hypoxia-induced neuronal death.";
RL J. Cell Sci. 126:5566-5577(2013).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NDUFS1, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32072193; DOI=10.1007/s00125-020-05103-w;
RA Qi B., He L., Zhao Y., Zhang L., He Y., Li J., Li C., Zhang B., Huang Q.,
RA Xing J., Li F., Li Y., Ji L.;
RT "Akap1 deficiency exacerbates diabetic cardiomyopathy in mice by NDUFS1-
RT mediated mitochondrial dysfunction and apoptosis.";
RL Diabetologia 63:1072-1087(2020).
CC -!- FUNCTION: Differentially targeted protein that binds to type I and II
CC regulatory subunits of protein kinase A (PubMed:9065479,
CC PubMed:9182549). Anchors them to the cytoplasmic face of the
CC mitochondrial outer membrane or allows them to reside in the
CC endoplasmic reticulum (PubMed:9065479, PubMed:9182549). Involved in
CC mitochondrial-mediated antiviral innate immunity (By similarity).
CC Promotes translocation of NDUFS1 into mitochondria to regulate
CC mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I)
CC activity (PubMed:32072193). Under diabetic conditions, myocardial AKAP1
CC expression decreases which blocks the translocation of NDUFS1 from the
CC cytosol to mitochondria (PubMed:32072193). Reduction of NDUFS1 in
CC mitochondria decreases ATP production and increases mitochondrial ROS
CC level, which causes mitochondrial dysfunction and cell apoptosis,
CC respectively, thereby leading to cardiac dysfunction (PubMed:32072193).
CC {ECO:0000250|UniProtKB:Q92667, ECO:0000269|PubMed:32072193,
CC ECO:0000269|PubMed:9065479, ECO:0000269|PubMed:9182549}.
CC -!- SUBUNIT: Interacts with SLC8A3 (PubMed:24101730). Interacts with
CC CFAP91. Interacts with CLPB (By similarity). Interacts with NDUFS1
CC (PubMed:32072193). {ECO:0000250|UniProtKB:Q92667,
CC ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:32072193}.
CC -!- INTERACTION:
CC O08715; Q06986: Siah2; NbExp=6; IntAct=EBI-7838029, EBI-957413;
CC O08715-5; Q16825: PTPN21; Xeno; NbExp=2; IntAct=EBI-9117988, EBI-2860264;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:9182549}.
CC Mitochondrion {ECO:0000269|PubMed:32072193}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. The longest N-terminal part only present in isoform 2 acts as
CC a suppressor of mitochondrial targeting and as an activator of
CC recessive endoplasmic reticulum targeting motif.
CC {ECO:0000269|PubMed:10352013}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. The longest N-terminal part only present in isoform 4 acts as
CC a suppressor of mitochondrial targeting and as an activator of
CC recessive endoplasmic reticulum targeting motif.
CC {ECO:0000269|PubMed:10352013}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. {ECO:0000269|PubMed:10352013}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. {ECO:0000269|PubMed:10352013}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. {ECO:0000269|PubMed:10352013}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL
CC endoplasmic reticulum-targeting sequence. This explains how it is able
CC to switch its localization, either being in the endoplasmic reticulum
CC or in the mitochondria depending on which N-terminal part begins the
CC isoform. {ECO:0000269|PubMed:10352013}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3; Synonyms=D-AKAP1C, AKAP121;
CC IsoId=O08715-1; Sequence=Displayed;
CC Name=1; Synonyms=D-AKAP1A;
CC IsoId=O08715-2; Sequence=VSP_002848, VSP_002849;
CC Name=2; Synonyms=D-AKAP1B;
CC IsoId=O08715-3; Sequence=VSP_002847, VSP_002848, VSP_002849;
CC Name=4; Synonyms=D-AKAP1D;
CC IsoId=O08715-4; Sequence=VSP_002847;
CC Name=5; Synonyms=S-AKAP84;
CC IsoId=O08715-5; Sequence=VSP_002850, VSP_002851;
CC Name=6; Synonyms=AKAP100;
CC IsoId=O08715-6; Sequence=VSP_002852, VSP_002853;
CC -!- TISSUE SPECIFICITY: Highest expression in testis, heart, liver,
CC skeletal muscle, intestine and kidney, followed by brain and lung. No
CC expression in spleen. Isoform 1/D-AKAP1A is expressed predominantly in
CC testis whereas isoform 4/D-AKAP1D is expressed primarily in liver
CC (PubMed:9065479). Expression is decreased in hearts of diabetic mice
CC (at protein level) (PubMed:32072193). {ECO:0000269|PubMed:32072193,
CC ECO:0000269|PubMed:9065479}.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- DISRUPTION PHENOTYPE: Knockout in diabetogenic agent streptozotocin-
CC treated mice results in significant cardiac dysfunction which is
CC accompanied by impaired mitochondrial function and increased
CC cardiomyocyte apoptosis. {ECO:0000269|PubMed:32072193}.
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DR EMBL; U84389; AAC27100.1; -; mRNA.
DR EMBL; U95145; AAB53740.1; -; mRNA.
DR EMBL; U95146; AAB53741.1; -; mRNA.
DR EMBL; AL596180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25229.1; -. [O08715-1]
DR RefSeq; NP_001036006.1; NM_001042541.1. [O08715-1]
DR RefSeq; NP_033778.2; NM_009648.2. [O08715-1]
DR AlphaFoldDB; O08715; -.
DR SMR; O08715; -.
DR BioGRID; 198048; 4.
DR IntAct; O08715; 5.
DR MINT; O08715; -.
DR STRING; 10090.ENSMUSP00000018572; -.
DR iPTMnet; O08715; -.
DR PhosphoSitePlus; O08715; -.
DR SwissPalm; O08715; -.
DR EPD; O08715; -.
DR jPOST; O08715; -.
DR MaxQB; O08715; -.
DR PaxDb; O08715; -.
DR PeptideAtlas; O08715; -.
DR PRIDE; O08715; -.
DR ProteomicsDB; 296383; -. [O08715-1]
DR ProteomicsDB; 296384; -. [O08715-2]
DR ProteomicsDB; 296385; -. [O08715-3]
DR ProteomicsDB; 296386; -. [O08715-4]
DR ProteomicsDB; 296387; -. [O08715-5]
DR ProteomicsDB; 296388; -. [O08715-6]
DR Antibodypedia; 2388; 186 antibodies from 33 providers.
DR DNASU; 11640; -.
DR Ensembl; ENSMUST00000018572; ENSMUSP00000018572; ENSMUSG00000018428. [O08715-1]
DR Ensembl; ENSMUST00000107903; ENSMUSP00000103536; ENSMUSG00000018428. [O08715-1]
DR Ensembl; ENSMUST00000107904; ENSMUSP00000103537; ENSMUSG00000018428. [O08715-4]
DR Ensembl; ENSMUST00000143720; ENSMUSP00000122295; ENSMUSG00000018428. [O08715-5]
DR GeneID; 11640; -.
DR KEGG; mmu:11640; -.
DR UCSC; uc007kvu.2; mouse. [O08715-1]
DR CTD; 8165; -.
DR MGI; MGI:104729; Akap1.
DR VEuPathDB; HostDB:ENSMUSG00000018428; -.
DR eggNOG; KOG2279; Eukaryota.
DR GeneTree; ENSGT00390000001360; -.
DR HOGENOM; CLU_016731_0_0_1; -.
DR InParanoid; O08715; -.
DR OMA; VMEDSGC; -.
DR TreeFam; TF105401; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 11640; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Akap1; mouse.
DR PRO; PR:O08715; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O08715; protein.
DR Bgee; ENSMUSG00000018428; Expressed in seminiferous tubule of testis and 238 other tissues.
DR ExpressionAtlas; O08715; baseline and differential.
DR Genevisible; O08715; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:MGI.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW RNA-binding; Transit peptide; Transmembrane.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..857
FT /note="A-kinase anchor protein 1, mitochondrial"
FT /id="PRO_0000016660"
FT DOMAIN 561..625
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 712..771
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 65..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..319
FT /note="PKA-RII subunit binding domain"
FT REGION 336..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT VAR_SEQ 1
FT /note="M -> MGCKTGPKPFGGGETIRPIRIRRCSYFTSTDSKM (in isoform
FT 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9065479"
FT /id="VSP_002847"
FT VAR_SEQ 526..547
FT /note="GSDGNSMDSVDSCCGLTKPDSP -> VAAPPQERGHFGNGGCTGFFEC (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:9182549"
FT /id="VSP_002850"
FT VAR_SEQ 527..544
FT /note="SDGNSMDSVDSCCGLTKP -> RKVLGCFLGESGRGPIIC (in isoform
FT 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:9065479"
FT /id="VSP_002848"
FT VAR_SEQ 545..857
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:9065479"
FT /id="VSP_002849"
FT VAR_SEQ 548..857
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9182549"
FT /id="VSP_002851"
FT VAR_SEQ 614..637
FT /note="SQHHVDKALNLIGKKFKELNLTNI -> CVSVLTRRLSAPCRQSSELDWEEV
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9182549"
FT /id="VSP_002852"
FT VAR_SEQ 638..857
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9182549"
FT /id="VSP_002853"
FT CONFLICT 80
FT /note="C -> S (in Ref. 2; AAC27100 and 3; AAB53740/
FT AAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> I (in Ref. 2; AAC27100)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="F -> L (in Ref. 2; AAC27100 and 3; AAB53740/
FT AAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> P (in Ref. 3; AAB53740/AAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> I (in Ref. 2; AAC27100 and 3; AAB53740/
FT AAB53741)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="M -> I (in Ref. 2; AAC27100 and 3; AAB53740/
FT AAB53741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 857 AA; 92195 MW; 455679FCF95C28E6 CRC64;
MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK DRRLSEEACP
GVLSVAPTVT QPPGREEQRC VDKPSTEPLA LPRTRQVRRR SESSGNLPSV ADTRSQPGPC
RDEIAKVELS LMGDKAKSIP LGCPLLPKDA SFPYEAVERC KQESALGKTP GRGWPSPYAA
SGEKARETGG TEGTGDAVLG ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP
QVAELLKKEE YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV
PENDQIKQAA FQLISQVILE ATEEFRATTV GKTVAQVHPT SATQPKGKEE SCVPASQETS
LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP TKDQKPKNSA HHISLAPCPP
PVTPQRQSLE GASNPRGDDN FVACMANNSQ SVLSVSSLGQ CSDPVSTSGL EDSCTETISS
SGDKAMTPPL PVSTQPFSNG VLKEELSDLG TEDGWTMDTE ADHSGGSDGN SMDSVDSCCG
LTKPDSPQSV QAGSNPKKVD LIIWEIEVPK HLVGRLIGKQ GRYVSFLKQT SGAKIYISTL
PYTQNIQICH IEGSQHHVDK ALNLIGKKFK ELNLTNIYAP PLPSLALPSL PMTSWLMLPD
GITVEVIVVN QVNAGHLFVQ QHTHPTFHAL RSLDQQMYLC YSQPGIPTLP TPVEITVICA
APGADGAWWR AQVVASYEET NEVEIRYVDY GGYKRVKVDV LRQIRSDFVT LPFQGAEVLL
DSVVPLSDDD HFSPEADAAM SEMTGNTALL AQVTSYSATG LPLIQLWSVV GDEVVLINRS
LVERGLAQWV DSYYASL
