ID   DOPO_MOUSE              Reviewed;         622 AA.
AC   Q64237; Q3V1U4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Dopamine beta-hydroxylase;
DE            EC=1.14.17.1 {ECO:0000269|PubMed:27148966, ECO:0000305|PubMed:7715704};
DE   AltName: Full=Dopamine beta-monooxygenase;
DE   Contains:
DE     RecName: Full=Soluble dopamine beta-hydroxylase;
GN   Name=Dbh;
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], AND TISSUE SPECIFICITY.
RX   PubMed=1280432; DOI=10.1016/0006-291x(92)91598-k;
RA   Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T.;
RT   "Mouse dopamine beta-hydroxylase: primary structure deduced from the cDNA
RT   sequence and exon/intron organization of the gene.";
RL   Biochem. Biophys. Res. Commun. 189:590-599(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=7961964; DOI=10.1016/s0021-9258(18)43941-5;
RA   Kobayashi K., Morita S., Mizuguchi T., Sawada H., Yamada K., Nagatsu I.,
RA   Fujita K., Nagatsu T.;
RT   "Functional and high level expression of human dopamine beta-hydroxylase in
RT   transgenic mice.";
RL   J. Biol. Chem. 269:29725-29731(1994).
RN   [7]
RP   DISRUPTION PHENOTYPE, FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX   PubMed=7715704; DOI=10.1038/374643a0;
RA   Thomas S.A., Matsumoto A.M., Palmiter R.D.;
RT   "Noradrenaline is essential for mouse fetal development.";
RL   Nature 374:643-646(1995).
RN   [8]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX   PubMed=27148966; DOI=10.1371/journal.pone.0154864;
RA   Cubells J.F., Schroeder J.P., Barrie E.S., Manvich D.F., Sadee W., Berg T.,
RA   Mercer K., Stowe T.A., Liles L.C., Squires K.E., Mezher A., Curtin P.,
RA   Perdomo D.L., Szot P., Weinshenker D.;
RT   "Human bacterial artificial chromosome (BAC) transgenesis fully rescues
RT   noradrenergic function in dopamine beta-hydroxylase knockout mice.";
RL   PLoS ONE 11:E0154864-E0154864(2016).
CC   -!- FUNCTION: Catalyzes the hydroxylation of dopamine to noradrenaline
CC       (also known as norepinephrine), and is thus vital for regulation of
CC       these neurotransmitters. {ECO:0000269|PubMed:27148966,
CC       ECO:0000269|PubMed:7715704}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine + 2 L-ascorbate + O2 = (R)-noradrenaline + H2O + 2
CC         monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:19117,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:59513, ChEBI:CHEBI:59905, ChEBI:CHEBI:72587;
CC         EC=1.14.17.1; Evidence={ECO:0000269|PubMed:27148966,
CC         ECO:0000305|PubMed:7715704};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19118;
CC         Evidence={ECO:0000269|PubMed:27148966};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:P09172};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:P09172};
CC   -!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline biosynthesis;
CC       (R)-noradrenaline from dopamine: step 1/1.
CC       {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}.
CC   -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers.
CC       {ECO:0000250|UniProtKB:P09172}.
CC   -!- SUBCELLULAR LOCATION: [Soluble dopamine beta-hydroxylase]: Cytoplasmic
CC       vesicle, secretory vesicle lumen {ECO:0000269|PubMed:7961964}.
CC       Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen
CC       {ECO:0000269|PubMed:7961964}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000269|PubMed:7961964}; Single-pass type II membrane protein
CC       {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, chromaffin
CC       granule membrane {ECO:0000269|PubMed:7961964}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in adrenal gland secretory granules (at
CC       protein level) (PubMed:7961964). Detected in adrenal gland
CC       (PubMed:1280432). {ECO:0000269|PubMed:1280432,
CC       ECO:0000269|PubMed:7961964}.
CC   -!- PTM: Proteolytic cleavage after the membrane-anchor leads to the
CC       release of the soluble form. {ECO:0000250|UniProtKB:P15101}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09172}.
CC   -!- DISRUPTION PHENOTYPE: Complete embryonic lethality in homozygous dams,
CC       and 88% embryonic lethality for homozygous embryos in heterozygous
CC       dams. Only 12% of the homozygous pups from heterozygous dams are alive
CC       at birth. Mutant pups have no obvious phenotype at birth, but nearly
CC       half of them die within 48 h, and only 5% survive to adulthood. Three
CC       weeks after birth, mutant pups are runted and weigh only half as much
CC       as their littermates. Still, the weight of adult males reaches 80% and
CC       that of females 88% of that of their littermates. Besides, mutant mice
CC       display ptosis. Embryonic lethality is due to a lack of noradrenaline
CC       and can be prevented by treatment with dihydroxyphenylserine, a
CC       compound that can be converted into noradrenaline in the absence of
CC       Dbh. {ECO:0000269|PubMed:27148966, ECO:0000269|PubMed:7715704}.
CC   -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC       monooxygenase family. {ECO:0000305}.
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DR   EMBL; S50200; AAB24330.1; -; mRNA.
DR   EMBL; AK132245; BAE21055.1; -; mRNA.
DR   EMBL; AL954801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466542; EDL08360.1; -; Genomic_DNA.
DR   EMBL; BC141022; AAI41023.1; -; mRNA.
DR   EMBL; BC171949; AAI71949.1; -; mRNA.
DR   CCDS; CCDS38088.1; -.
DR   PIR; JC1346; JC1346.
DR   RefSeq; NP_620392.2; NM_138942.3.
DR   PDB; 6G9Q; X-ray; 1.89 A; P=557-565.
DR   PDB; 6G9R; X-ray; 2.70 A; I/J/K/P=557-565.
DR   PDBsum; 6G9Q; -.
DR   PDBsum; 6G9R; -.
DR   AlphaFoldDB; Q64237; -.
DR   SMR; Q64237; -.
DR   STRING; 10090.ENSMUSP00000000910; -.
DR   GlyConnect; 2266; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q64237; 4 sites, 1 glycan.
DR   GlyGen; Q64237; 4 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q64237; -.
DR   PhosphoSitePlus; Q64237; -.
DR   SwissPalm; Q64237; -.
DR   CPTAC; non-CPTAC-3459; -.
DR   MaxQB; Q64237; -.
DR   PaxDb; 10090-ENSMUSP00000000910; -.
DR   ProteomicsDB; 277397; -.
DR   Antibodypedia; 881; 582 antibodies from 47 providers.
DR   DNASU; 13166; -.
DR   Ensembl; ENSMUST00000000910.7; ENSMUSP00000000910.7; ENSMUSG00000000889.9.
DR   GeneID; 13166; -.
DR   KEGG; mmu:13166; -.
DR   UCSC; uc008ixe.1; mouse.
DR   AGR; MGI:94864; -.
DR   CTD; 1621; -.
DR   MGI; MGI:94864; Dbh.
DR   VEuPathDB; HostDB:ENSMUSG00000000889; -.
DR   eggNOG; KOG3568; Eukaryota.
DR   GeneTree; ENSGT00530000063085; -.
DR   HOGENOM; CLU_017939_3_0_1; -.
DR   InParanoid; Q64237; -.
DR   OMA; FPHFSGP; -.
DR   OrthoDB; 37880at2759; -.
DR   PhylomeDB; Q64237; -.
DR   TreeFam; TF320698; -.
DR   BRENDA; 1.14.17.1; 3474.
DR   Reactome; R-MMU-209905; Catecholamine biosynthesis.
DR   UniPathway; UPA00748; UER00735.
DR   BioGRID-ORCS; 13166; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Dbh; mouse.
DR   PRO; PR:Q64237; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q64237; Protein.
DR   Bgee; ENSMUSG00000000889; Expressed in superior cervical ganglion and 69 other cell types or tissues.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0034774; C:secretory granule lumen; IDA:UniProtKB.
DR   GO; GO:0030667; C:secretory granule membrane; IDA:UniProtKB.
DR   GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043196; C:varicosity; ISO:MGI.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0004500; F:dopamine beta-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0042420; P:dopamine catabolic process; IMP:UniProtKB.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0042309; P:homoiothermy; IMP:MGI.
DR   GO; GO:0002443; P:leukocyte mediated immunity; IMP:MGI.
DR   GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
DR   GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046333; P:octopamine metabolic process; ISO:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI.
DR   GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:1904705; P:regulation of vascular associated smooth muscle cell proliferation; IMP:MGI.
DR   GO; GO:1905562; P:regulation of vascular endothelial cell proliferation; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0042310; P:vasoconstriction; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   CDD; cd09631; DOMON_DOH; 1.
DR   Gene3D; 2.60.120.230; -; 1.
DR   Gene3D; 2.60.120.310; Copper type II, ascorbate-dependent monooxygenase, N-terminal domain; 1.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR   InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR   InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR   InterPro; IPR024548; Cu2_monoox_C.
DR   InterPro; IPR000945; DBH-like.
DR   InterPro; IPR045266; DOH_DOMON.
DR   InterPro; IPR005018; DOMON_domain.
DR   InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR   InterPro; IPR028460; Tbh/DBH.
DR   PANTHER; PTHR10157; DOPAMINE BETA HYDROXYLASE RELATED; 1.
DR   PANTHER; PTHR10157:SF29; DOPAMINE BETA-HYDROXYLASE; 1.
DR   Pfam; PF03712; Cu2_monoox_C; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF03351; DOMON; 1.
DR   PRINTS; PR00767; DBMONOXGNASE.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49742; PHM/PNGase F; 2.
DR   PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR   PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR   PROSITE; PS50836; DOMON; 1.
DR   Genevisible; Q64237; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Catecholamine biosynthesis; Copper; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Vitamin C.
FT   CHAIN           1..622
FT                   /note="Dopamine beta-hydroxylase"
FT                   /id="PRO_0000006357"
FT   CHAIN           44..622
FT                   /note="Soluble dopamine beta-hydroxylase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000308210"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..621
FT                   /note="Intragranular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..177
FT                   /note="DOMON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT   REGION          594..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000255"
FT   BINDING         266
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   BINDING         267
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   BINDING         337
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   BINDING         416
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   BINDING         418
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   BINDING         491
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   SITE            43..44
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P15101"
FT   MOD_RES         350
FT                   /note="Phosphoserine; by CaMK"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        158..600
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        236..287
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        273..299
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        394..507
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        398..569
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        470..492
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        532
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   DISULFID        534
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P09172"
FT   CONFLICT        109
FT                   /note="T -> S (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="Q -> L (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="T -> Q (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="H -> P (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="V -> E (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="Q -> R (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="D -> N (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        618..621
FT                   /note="EADA -> GGRC (in Ref. 1; AAB24330)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   622 AA;  70314 MW;  7D9FA1B622F3FCA8 CRC64;
     MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE
     GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWTD GDRAYFADAW
     SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP
     FQSLEAINTS GLHTGLQRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN ETTYWCYITE
     LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR
     HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLHYTAT
     LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT
     GRKVVTVLAR DGQERKVVNR DNHYSPHFQE IRMLKKVVTV YPGDVLITSC TYNTENKTLA
     TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP
     QQFSSVPWNS FNRDMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC
     PIRQTQSPAN PTVPITTEAD AE
//