DOPO_MOUSE
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 03-AUG-2022, entry version 170.
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: Conversion of dopamine to noradrenaline.
CC {ECO:0000269|PubMed:27148966, 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 -!- 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 GlyGen; Q64237; 4 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q64237; -.
DR SwissPalm; Q64237; -.
DR CPTAC; non-CPTAC-3459; -.
DR MaxQB; Q64237; -.
DR PaxDb; Q64237; -.
DR PRIDE; Q64237; -.
DR ProteomicsDB; 277397; -.
DR Antibodypedia; 881; 540 antibodies from 47 providers.
DR DNASU; 13166; -.
DR Ensembl; ENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
DR GeneID; 13166; -.
DR KEGG; mmu:13166; -.
DR UCSC; uc008ixe.1; mouse.
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; CAPEMDN; -.
DR OrthoDB; 1472750at2759; -.
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 74 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 tissues.
DR Genevisible; Q64237; MM.
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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0045202; C:synapse; ISO:MGI.
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; -; 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; PTHR10157; 1.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00767; DBMONOXGNASE.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR PROSITE; PS50836; DOMON; 1.
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 cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 418
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P09172"
FT BINDING 491
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
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
